AU2024299365A1 - Compositions for delivery of plasmodium antigens and related methods - Google Patents

Abstract

The present disclosure provides compositions (e.g., pharmaceutical compositions) for delivery of Plasmodium protein antigens and related technologies (e.g., components thereof and/or methods relating thereto). Among other things, the present disclosure provides combinations comprising a first pharmaceutical composition comprising a first polyribonucleotide and a second pharmaceutical composition comprising a second polyribonucleotide. In some embodiments, a first polyribonucleotide encodes a first polypeptide that comprises one or more Plasmodium T-cell antigens. In some embodiments, a second polyribonucleotide encodes a second polypeptide that comprises one or more Plasmodium polypeptide (e.g., CSP) or antigenic portions thereof.

Description

COMPOSITIONS FOR DELIVERY OF PLASMODIUM ANTIGENS AND RELATED METHODS CROSS-REFERENCE TO RELATED APPLICATIONS [0001] This application claims priority to United States Provisional Application Serial Nos.63/515,330, filed July 24, 2023, 63/580,303, filed September 01, 2023, 63/570,777, filed March 27, 2024, 63/634,381, filed April 15, 2024, and 63/641,939, filed May 02, 2024, the entirety of each of which is incorporated herein by reference. BACKGROUND [0002] Malaria is a mosquito-borne infectious disease caused by protozoan parasites of the Plasmodium genus. According to the World Health Organization, an estimated 3.4 billion people in 92 countries are at risk of being infected with the malaria parasite and developing disease. SUMMARY [0003] The present disclosure provides technologies (e.g., compositions, methods, etc.) for delivery of Plasmodium antigens. [0004] For instance, the present disclosure provides pharmaceutical compositions (e.g., immunogenic compositions, e.g., vaccines) for delivering particular Plasmodium polypeptide constructs to a subject (e.g., a patient) and related technologies (e.g., methods). As described further herein, Plasmodium polypeptide constructs can comprise one or more Plasmodium polypeptide or antigenic portions thereof. In particular, the present disclosure provides Plasmodium vaccine compositions and related technologies (e.g., methods). [0005] In some embodiments, the present disclosure provides particular pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) formats including, for example, polyribonucleotides comprising particular elements and/or sequences useful for delivery of Plasmodium antigens. [0006] The present disclosure provides a variety of insights and technologies related to such Plasmodium antigen constructs and vaccine (e.g., RNA vaccine) compositions. For example, the present disclosure provides technologies for preventing, characterizing, treating, and/or monitoring malaria outbreaks and/or infections including, as noted, various nucleic acid constructs and encoded proteins, as well as agents (e.g., antibodies) that bind to such proteins, and compositions that comprise and/or deliver them. [0007] In some aspects, provided herein are technologies (e.g., compositions and methods) for augmenting, inducing, promoting, enhancing and/or improving an immune response against a Plasmodium parasite. In some embodiments, technologies described herein are designed to act as immunological boost to a primary vaccine, such as a vaccine directed to antigen(s) and/or epitope(s) of a Plasmodium parasite. [0008] The present disclosure further recognizes that an approach comprising the delivery of one or more Plasmodium polypeptides or antigenic portions thereof that are present and/or exposed at various time points in a Plasmodium life cycle may elicit a more robust immune response. In particular, it can be beneficial to deliver one or more Plasmodium polypeptides or antigenic portions thereof that will generate an immune response that targets Plasmodium parasites at an early life cycle stage, e.g., (1) in the asymptomatic infection stage from the deposition of the parasites in the skin until the infection of hepatocytes (see FIG.1, 1 – Sporozoite), and/or (2) after infection of a subject’s hepatocytes (see FIG.1, 2 – Liver Stage), and/or (3) after egress from hepatocytes but before infecting a subject’s erythrocytes (see FIG.1, 3 – Pre-invasion). Preventing the symptomatic phase of a Plasmodium parasite, e.g., killing the parasites prior to infecting erythrocytes, can help prevent disease and death of a subject, as well as mitigate onward transmission. When such an approach is applied to a large enough proportion of a target population (e.g., constituting an infectious reservoir), the approach may enable interruption of transmission and aid in malaria elimination. [0009] Thus, the present disclosure provides, among other things, combinations comprising more than one Plasmodium polypeptide construct that each include one or more Plasmodium polypeptides or antigenic fragments thereof, wherein the more than one Plasmodium polypeptide constructs comprise Plasmodium polypeptides or antigenic fragments thereof that are expressed at different stages of the asymptomatic phase of infection, such as the initial sporozoite stage and the liver stage of infection. In some embodiments, a combination of two or more Plasmodium polypeptide constructs that include Plasmodium polypeptides or antigenic fragments thereof that are expressed at different stages within the asymptomatic phase (such as sporozoite and liver stage) may prevent erythrocyte infection by parasites and thereby prevent symptomatic malaria disease and disrupting onwards transmission. In some embodiments, Plasmodium polypeptide constructs described herein provide a combination that acts as a pre-erythrocytic vaccine. In some embodiments, targeting two or more stages of the parasitic infection (such as sporozoite and liver stage) can provide additional layers of immune protection for a subject, e.g., fewer Plasmodium sporozoites invading the liver, leading to fewer infected hepatocytes that need to be eliminated. In some embodiments, a combination as described herein includes two or more Plasmodium polypeptide constructs, wherein the Plasmodium polypeptide constructs comprise Plasmodium polypeptides or antigenic fragments thereof that are expressed at different stages within the asymptomatic phase (such as sporozoite and liver stage). In some embodiments, the two or more Plasmodium polypeptide constructs do not interfere with each other (e.g., the elicitation of an immune response by one Plasmodium polypeptide construct does not interfere with the elicitation of an immune response by another of the Plasmodium polypeptide constructs. For example, in some embodiments, the presence of two or more Plasmodium polypeptide constructs in a combination does not abolish an immunogenic effect of one or more antigens on a first Plasmodium polypeptide constructs that is otherwise present in the absence of a second Plasmodium polypeptide constructs. In some embodiments, the lack of interference by one Plasmodium polypeptide construct with another is observed regardless of whether there are three or more (e.g., three, four, five, six, etc.) present in a combination. [0010] In some embodiments, a combination of two or more Plasmodium polypeptide constructs elicits a humoral and/or cellular immune response. In some embodiments, in a combination of two or more Plasmodium polypeptide constructs, each Plasmodium polypeptide construct elicits a humoral and/or cellular immune response. In particular, the present disclosure provides the insight that antigens or epitopes that are present on the surface of cells, particularly the Plasmodium cell surface, may be able to induce a B cell response, while antigens or epitopes that are not surface exposed or are minimally exposed may still be able to induce a T cell response. The resulting combined B cell and T cell response may be important for developing strong immune protection against current and future Plasmodium infections. As such, the present disclosure provides compositions for delivering antigens or epitopes that can be useful prophylactically or therapeutically. [0011] The present disclosure also provides the insight that certain, multi-prong approaches can be useful for providing protection against Plasmodium infections (e.g., malaria). For example, a combination as described herein can comprise a first pharmaceutical composition comprising a first polyribonucleotide and a second pharmaceutical composition comprising a second polyribonucleotide. In some embodiments, a first polyribonucleotide encodes a first polypeptide that comprises one or more Plasmodium T-cell antigens. In some embodiments, a second polyribonucleotide encodes a second polypeptide that comprises one or more Plasmodium polypeptides or antigenic portions thereof. [0012] In some embodiments, a first polypeptide comprises an amino acid sequence with at least 85% identity to an amino acid sequence according to any one of SEQ ID NOs 167, 170, 173, 176, 179, 182, 185, 188, 191, 194, 197, 200, 203, 206, 209, 212, 215, 218, and 221; and a second polyribonucleotide comprises an amino acid sequence with at least 85% identity to an amino acid sequence according to any one of SEQ ID NOs: 5, 8, 10, 12, 15, 18, 21, 24, 27, 30, 33, 36, 39, 42, 45, 48, 51, 54, 57, 60, 63, 66, 69, 72, 75, 78, 81, 84, 87, 90, 93, 96, 99, 102, 105 , 107-112, 117, 122, 125, 130, 135, 138, and 141. [0013] In some embodiments, a first polypeptide comprises (i) an antigenic Plasmodium CSP polypeptide fragment, (ii) an antigenic Plasmodium TRAP polypeptide fragment, (iii) an antigenic Plasmodium UIS3 polypeptide fragment, (iv) an antigenic Plasmodium ETRAMP10.3 polypeptide fragment, and (v) an antigenic Plasmodium LSAP2 polypeptide fragment. In some embodiments, a second polyribonucleotide comprises (i) a secretory signal, (ii) a Plasmodium CSP N-terminal end region, (iii) a Plasmodium CSP junction region, (iv) nine repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223), (v) a Plasmodium CSP C-terminal region, a Plasmodium CSP C-terminal region variant, or an antigenic portion thereof, (vi) a serine-valine sequence immediately following the Plasmodium CSP C-terminal region, a Plasmodium CSP C-terminal region variant, or an antigenic portion thereof, (vii) a linker, and (viii) a transmembrane region, and wherein the second polypeptide does not comprise any of (a) a Plasmodium CSP N-terminal region or portion thereof, and (b) an amino acid sequence of NPNA (SEQ ID NO: 228). In some embodiments, a second polyribonucleotide comprises (i) a secretory signal, (ii) a Plasmodium CSP N-terminal end region, (iii) a Plasmodium CSP junction region, (iv) nine repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223), (v) a Plasmodium CSP C-terminal region, (vi) a serine-valine sequence immediately following the Plasmodium CSP C-terminal region, (vii) a linker, and (viii) a transmembrane region, and wherein the second polypeptide does not comprise any of (a) a Plasmodium CSP N-terminal region or portion thereof, and (b) an amino acid sequence of NPNA (SEQ ID NO: 228). [0014] In some embodiments, a first polypeptide comprises (i) an antigenic Plasmodium LSA-1(a) polypeptide fragment, (ii) an antigenic Plasmodium LSA-1(b) polypeptide fragment, (iii) an antigenic Plasmodium LISP-2 polypeptide fragment, and (iv) an antigenic Plasmodium LISP-1 polypeptide fragment. In some embodiments, a second polyribonucleotide comprises (i) a secretory signal, (ii) a Plasmodium CSP N-terminal region, (iii) a Plasmodium CSP N-terminal end region, (iv) a Plasmodium CSP junction region, (v) three repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223), (vi) a Plasmodium CSP major repeat region, (vii) a Plasmodium CSP C- terminal region, a Plasmodium CSP C-terminal region variant, or an antigenic portion thereof, and a transmembrane region. In some embodiments, a first polypeptide comprises (i) an antigenic Plasmodium LSA-1(a) polypeptide fragment, (ii) an antigenic Plasmodium LSA-1(b) polypeptide fragment, (iii) an antigenic Plasmodium LISP-2 polypeptide fragment, and (iv) an antigenic Plasmodium LISP-1 polypeptide fragment. In some embodiments, a second polyribonucleotide comprises (i) a secretory signal, (ii) a Plasmodium CSP N-terminal region, (iii) a Plasmodium CSP N-terminal end region, (iv) a Plasmodium CSP junction region, (v) three repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223), (vi) a Plasmodium CSP major repeat region, (vii) a Plasmodium CSP C- terminal region, and a transmembrane region. [0015] In some embodiments, a combination includes a first pharmaceutical composition and a second pharmaceutical composition. In some embodiments, a first pharmaceutical composition comprises a first polyribonucleotide. In some embodiments, a first polyribonucleotide encodes a first polypeptide. In some embodiments, a first polypeptide comprises one or more Plasmodium T-cell antigens. In some embodiments, a second pharmaceutical composition comprises a second polyribonucleotide. In some embodiments, a second polyribonucleotide encodes a second polypeptide. In some embodiments, a second polypeptide comprises one or more Plasmodium polypeptide or antigenic portions thereof. In some embodiments, a combination includes: (i) a first pharmaceutical composition comprising a first polyribonucleotide, wherein the first polyribonucleotide encodes a first polypeptide, and a first polypeptide comprises one or more Plasmodium T-cell antigens and (ii) a second pharmaceutical composition comprising a second polyribonucleotide, wherein the second polyribonucleotide encodes a second polypeptide, and the second polypeptide comprises one or more Plasmodium polypeptide or antigenic portions thereof. [0016] In some embodiments, a first polypeptide comprises at least 10 amino acids and at most 1100 amino acids. In some embodiments, a first polypeptide comprises at least 10 amino acids and at most 500 amino acids. In some embodiments, one or more Plasmodium T-cell antigens comprised in a first polypeptide comprise at least 2 Plasmodium T-cell antigens. In some embodiments, one or more Plasmodium T-cell antigens comprised in a first polypeptide comprise at most 10 Plasmodium T-cell antigens. In some embodiments, one or more Plasmodium T-cell antigens comprised in a first polypeptide comprise at least 2 and at most 10 Plasmodium T-cell antigens. [0017] In some embodiments, one or more Plasmodium T cell antigens comprised in a first polypeptide comprise an antigenic Plasmodium CSP polypeptide fragment. In some embodiments, one or more Plasmodium T cell antigens comprised in a first polypeptide comprise an antigenic Plasmodium LSA-1 polypeptide fragment. In some embodiments, one or more Plasmodium T cell antigens comprised in a first polypeptide comprise an antigenic Plasmodium TRAP polypeptide fragment. In some embodiments, one or more Plasmodium T cell antigens comprised in a first polypeptide comprise an antigenic Plasmodium LSAP2 polypeptide fragment. In some embodiments, one or more Plasmodium T cell antigens comprised in a first polypeptide comprise an antigenic Plasmodium UIS3 polypeptide fragment. In some embodiments, one or more Plasmodium T cell antigens comprised in a first polypeptide comprise an antigenic Plasmodium ETRAMP10.3 polypeptide fragment. In some embodiments, one or more Plasmodium T cell antigens comprised in a first polypeptide comprise an antigenic Plasmodium LISP-1 polypeptide fragment. In some embodiments, one or more Plasmodium T cell antigens comprised in a first polypeptide comprise an antigenic Plasmodium LISP-2 polypeptide fragment. In some embodiments, one or more Plasmodium T cell antigens comprised in a first polypeptide comprise an antigenic Plasmodium LSA-3 polypeptide fragment. In some embodiments, one or more Plasmodium T cell antigens comprised in a first polypeptide comprise an antigenic Plasmodium LSA-1(a) polypeptide fragment. In some embodiments, one or more Plasmodium T cell antigens comprised in a first polypeptide comprise an antigenic Plasmodium LSA-1(b) polypeptide fragment. [0018] In some embodiments, one or more Plasmodium T cell antigens comprised in a first polypeptide comprise two or more of: (i) an antigenic Plasmodium CSP polypeptide fragment; (ii) an antigenic Plasmodium LSA-1 polypeptide fragment; (iii) an antigenic Plasmodium TRAP polypeptide fragment; (iv) an antigenic Plasmodium LSAP2 polypeptide fragment; (v) an antigenic Plasmodium UIS3 polypeptide fragment; (vi) an antigenic Plasmodium ETRAMP10.3 polypeptide fragment; (vii) an antigenic Plasmodium LISP-1 polypeptide fragment; (viii) an antigenic Plasmodium LISP-2 polypeptide fragment; and (ix) an antigenic Plasmodium LSA-3 polypeptide fragment. In some embodiments, a first polypeptide comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 179. [0019] In some embodiments, one or more Plasmodium T cell antigens comprised in a first polypeptide comprise: (i) an antigenic Plasmodium CSP polypeptide fragment; (ii) an antigenic Plasmodium TRAP polypeptide fragment; (iii) an antigenic Plasmodium UIS3 polypeptide fragment; (iv) an antigenic Plasmodium ETRAMP10.3 polypeptide fragment; (v) an antigenic Plasmodium LSAP2 polypeptide fragment; (vi) an antigenic Plasmodium LSA-3 polypeptide fragment; (vii) an antigenic Plasmodium LSA-1(a) polypeptide fragment; and (viii) an antigenic Plasmodium LSA-1(b) polypeptide fragment. In some embodiments, a first polypeptide comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 182. [0020] In some embodiments, one or more Plasmodium T cell antigens comprised in a first polypeptide comprise: (i) an antigenic Plasmodium CSP polypeptide fragment; (ii) an antigenic Plasmodium TRAP polypeptide fragment; (iii) an antigenic Plasmodium UIS3 polypeptide fragment; (iv) an antigenic Plasmodium ETRAMP10.3 polypeptide fragment; (v) an antigenic Plasmodium LSAP2 polypeptide fragment; (vi) an antigenic Plasmodium LSA- 1(a) polypeptide fragment; (vii) an antigenic Plasmodium LSA-1(b) polypeptide fragment; (viii) an antigenic Plasmodium LISP-2 polypeptide fragment; and (ix) an antigenic Plasmodium LISP-1 polypeptide fragment. In some embodiments, a first polypeptide comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 188. [0021] In some embodiments, one or more Plasmodium T cell antigens comprised in a first polypeptide comprise: (i) an antigenic Plasmodium CSP polypeptide fragment; (ii) an antigenic Plasmodium TRAP polypeptide fragment; (iii) an antigenic Plasmodium UIS3 polypeptide fragment; (iv) an antigenic Plasmodium ETRAMP10.3 polypeptide fragment; (v) an antigenic Plasmodium LSAP2 polypeptide fragment; (vi) an antigenic Plasmodium LSA- 1(a) polypeptide fragment; (vii) an antigenic Plasmodium LSA-1(b) polypeptide fragment; and (viii) an antigenic Plasmodium LISP-1 polypeptide fragment. In some embodiments, a first polypeptide comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 191. [0022] In some embodiments, one or more Plasmodium T cell antigens comprised in a first polypeptide comprise: (i) an antigenic Plasmodium CSP polypeptide fragment; (ii) an antigenic Plasmodium TRAP polypeptide fragment; (iii) an antigenic Plasmodium UIS3 polypeptide fragment; (iv) an antigenic Plasmodium ETRAMP10.3 polypeptide fragment; (v) an antigenic Plasmodium LSAP2 polypeptide fragment; (vi) an antigenic Plasmodium LISP- 2 polypeptide fragment; and (vii) an antigenic Plasmodium LISP-1 polypeptide fragment. In some embodiments, a first polypeptide comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 194. [0023] In some embodiments, one or more Plasmodium T cell antigens comprised in a first polypeptide comprise: (i) an antigenic Plasmodium CSP polypeptide fragment; (ii) an antigenic Plasmodium TRAP polypeptide fragment; (iii) an antigenic Plasmodium UIS3 polypeptide fragment; (iv) an antigenic Plasmodium ETRAMP10.3 polypeptide fragment; (v) an antigenic Plasmodium LSAP2 polypeptide fragment; (vi) an antigenic Plasmodium LSA- 1(b) polypeptide fragment; and (vii) an antigenic Plasmodium LISP-1 polypeptide fragment. In some embodiments, a first polypeptide comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 197. [0024] In some embodiments, one or more Plasmodium T cell antigens comprised in a first polypeptide comprise: (i) an antigenic Plasmodium CSP polypeptide fragment; (ii) an antigenic Plasmodium TRAP polypeptide fragment; (iii) an antigenic Plasmodium UIS3 polypeptide fragment; (iv) an antigenic Plasmodium ETRAMP10.3 polypeptide fragment; (v) an antigenic Plasmodium LSAP2 polypeptide fragment; (vi) an antigenic Plasmodium LSA- 1(a) polypeptide fragment; (vii) an antigenic Plasmodium LSA-1(b) polypeptide fragment; (viii) an antigenic Plasmodium LISP-2 polypeptide fragment; (ix) an antigenic Plasmodium LISP-1 polypeptide fragment; and (x) an antigenic Plasmodium LSA-3 polypeptide fragment. In some embodiments, a first polypeptide comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 200. [0025] In some embodiments, one or more Plasmodium T cell antigens comprised in the first polypeptide comprise: (i) an antigenic Plasmodium LSA-1(a) polypeptide fragment; (ii) an antigenic Plasmodium LSA-1(b) polypeptide fragment; (iii) an antigenic Plasmodium LISP-2 polypeptide fragment; (iv) an antigenic Plasmodium LISP- 1 polypeptide fragment; and (v) an antigenic Plasmodium LSA-3 polypeptide fragment. In some embodiments, a first polypeptide comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 212. [0026] In some embodiments, one or more Plasmodium T cell antigens comprised in the first polypeptide comprise: (i) an antigenic Plasmodium LSA-1(a) polypeptide fragment; (ii) an antigenic Plasmodium LSA-1(b) polypeptide fragment; (iii) an antigenic Plasmodium LISP-2 polypeptide fragment; and (iv) an antigenic Plasmodium LISP-1 polypeptide fragment. In some embodiments, a first polypeptide comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 209. [0027] In some embodiments, one or more Plasmodium T cell antigens comprised in a first polypeptide comprise an antigenic Plasmodium CSP polypeptide fragment, and wherein the antigenic Plasmodium CSP polypeptide fragment comprises a Plasmodium CSP N-terminal region. In some embodiments, an antigenic Plasmodium CSP polypeptide fragment further comprises a Plasmodium CSP N-terminal end region. In some embodiments, an antigenic Plasmodium CSP polypeptide fragment further comprises a Plasmodium CSP junction region. In some embodiments, an antigenic Plasmodium CSP polypeptide fragment comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 437. [0028] In some embodiments, one or more Plasmodium T cell antigens comprised in a first polypeptide do not comprise an antigenic Plasmodium berghei CSP polypeptide fragment. [0029] In some embodiments, one or more Plasmodium T cell antigens comprised in a first polypeptide comprise an antigenic Plasmodium LSA-1(a) polypeptide fragment, and wherein the antigenic Plasmodium LSA-1(a) polypeptide fragment comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 447. [0030] In some embodiments, one or more Plasmodium T cell antigens comprised in a first polypeptide comprise an antigenic Plasmodium LSA-1(b) polypeptide fragment, and wherein the antigenic Plasmodium LSA-1(b) polypeptide fragment comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 457. [0031] In some embodiments, one or more Plasmodium T cell antigens comprised in a first polypeptide comprise an antigenic Plasmodium TRAP polypeptide fragment, and wherein the antigenic Plasmodium TRAP polypeptide fragment comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 472. [0032] In some embodiments, one or more Plasmodium T cell antigens comprised in a first polypeptide comprise an antigenic Plasmodium LSAP2 polypeptide fragment, and wherein the antigenic Plasmodium LSAP2 polypeptide fragment comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 497. [0033] In some embodiments, one or more Plasmodium T cell antigens comprised in a first polypeptide comprise an antigenic Plasmodium UIS3 polypeptide fragment, and wherein the antigenic Plasmodium UIS3 polypeptide fragment comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 510. [0034] In some embodiments, one or more Plasmodium T cell antigens comprised in a first polypeptide comprise an antigenic Plasmodium ETRAMP10.3 polypeptide fragment, and wherein the antigenic Plasmodium ETRAMP10.3 polypeptide fragment comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 516. [0035] In some embodiments, one or more Plasmodium T cell antigens comprised in a first polypeptide comprise an antigenic Plasmodium LISP-1 polypeptide fragment, and wherein the antigenic Plasmodium LISP-1 polypeptide fragment comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 252. [0036] In some embodiments, one or more Plasmodium T cell antigens comprised in a first polypeptide comprise an antigenic Plasmodium LISP-2 polypeptide fragment, and wherein the antigenic Plasmodium LISP-2 polypeptide fragment comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 533. [0037] In some embodiments, one or more Plasmodium T cell antigens comprised in a first polypeptide comprise an antigenic Plasmodium LSA-3 polypeptide fragment, and wherein the antigenic Plasmodium LSA-3 polypeptide fragment comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 543. [0038] In some embodiments, one or more Plasmodium T cell antigens comprised in a first polypeptide each comprise one or more T cell epitopes. [0039] In some embodiments, a first polypeptide further comprises an MHC class I trafficking signal (MITD). In some embodiments, a MITD is located at the C-terminal end comprised in the first polypeptide. In some embodiments, a MITD comprises or consists of an amino acid sequence according to SEQ ID NO: 561. [0040] In some embodiments, a first polypeptide comprises a secretory signal. In some embodiments, a secretory signal comprises or consists of a Plasmodium secretory signal. In some embodiments, a Plasmodium secretory signal comprises or consists of a Plasmodium CSP secretory signal. In some embodiments, a Plasmodium CSP secretory signal comprises or consists of an amino acid sequence according to SEQ ID NO: 332. In some embodiments, a secretory signal comprises or consists of a heterologous secretory signal. In some embodiments, a heterologous secretory signal comprises or consists of a non-human secretory signal. In some embodiments, a heterologous secretory signal comprises or consists of a viral secretory signal. In some embodiments, a viral secretory signal comprises or consists of an HSV secretory signal. In some embodiments, a HSV secretory signal comprises or consists of an HSV-1 or HSV-2 secretory signal. In some embodiments, a HSV secretory signal comprises or consists of an HSV glycoprotein D (gD) secretory signal. In some embodiments, a HSV gD secretory signal comprises or consists of an amino acid sequence according to SEQ ID NO: 314. In some embodiments, a HSV gD secretory signal comprises or consists of an amino acid sequence according to SEQ ID NO: 320. In some embodiments, a viral secretory signal comprises or consists of an Ebola virus secretory signal. In some embodiments, an Ebola virus secretory signal comprises or consists of an Ebola virus spike glycoprotein (SGP) secretory signal. In some embodiments, an Ebola virus SGP secretory signal comprises or consists of an amino acid sequence according to SEQ ID NO: 335. In some embodiments, a secretory signal is located at the N-terminus of the polypeptide. In some embodiments, a first polypeptide does not comprise a secretory signal. [0041] In some embodiments, a polypeptide comprises one or more linkers. In some embodiments, one or more linkers comprise one or more glycine-serine linkers. In some embodiments, one or more linkers comprise at least one linker comprising an amino acid sequence according to SEQ ID NO: 404. In some embodiments, one or more linkers comprise at least one linker comprising an amino acid sequence according to SEQ ID NO: 411. In some embodiments, one or more linkers comprise at least one linker comprising an amino acid sequence according to SEQ ID NO: 408. In some embodiments, one or more linkers comprise at least one linker comprising an amino acid sequence according to SEQ ID NO: 412. In some embodiments, a polypeptide comprises a linker between two Plasmodium T-cell antigens. [0042] In some embodiments, a polypeptide comprises a transmembrane region. In some embodiments, a transmembrane region comprises or consists of a Plasmodium transmembrane region. In some embodiments, a Plasmodium transmembrane region comprises or consists of a Plasmodium CSP glycosylphosphatidylinositol (GPI) anchor region. In some embodiments, a Plasmodium CSP GPI anchor region comprises or consists of an amino acid sequence according to SEQ ID NO: 385. In some embodiments, a transmembrane region comprises or consists of a heterologous transmembrane region. In some embodiments, a heterologous transmembrane region does not comprise a hemagglutinin transmembrane region. In some embodiments, a heterologous transmembrane region comprises or consists of a non-human transmembrane region. In some embodiments, a heterologous transmembrane region comprises or consists of a viral transmembrane region. In some embodiments, a heterologous transmembrane region comprises or consists of an HSV transmembrane region. In some embodiments, a HSV transmembrane region comprises or consists of an HSV-1 or HSV-2 transmembrane region. In some embodiments, a HSV transmembrane region comprises or consists of an HSV gD transmembrane region. In some embodiments, a HSV gD transmembrane region comprises or consists of an amino acid sequence according to SEQ ID NO: 379. In some embodiments, a transmembrane region comprises or consists of a human transmembrane region. In some embodiments, a human transmembrane region comprises or consists of a human decay accelerating factor glycosylphosphatidylinositol (hDAF-GPI) anchor region. In some embodiments, a hDAF-GPI anchor region comprises or consists of an amino acid sequence according to SEQ ID NO: 382. In some embodiments, a polypeptide does not comprise a transmembrane region. [0043] In some embodiments, a polypeptide does not comprise an antigenic fragment of a bacterial polypeptide. In some embodiments, a polypeptide does not comprise an antigenic bacillus Calmette-Guérin (BCG) polypeptide fragment, optionally wherein the antigenic BCG polypeptide fragment comprises an amino acid sequence according to SEQ ID NO: 416. In some embodiments, a polypeptide does not comprise an antigenic tetanus toxin (TT) polypeptide fragment, optionally wherein the antigenic TT polypeptide fragment comprises an amino acid sequence according to SEQ ID NO: 417. [0044] In some embodiments, one or more Plasmodium T cell antigens comprised in a first polypeptide do not comprise an antigenic Plasmodium sporozoite threonine–asparagine-rich protein (STARP) polypeptide fragment, and optionally wherein the antigenic Plasmodium STARP polypeptide fragment comprises an amino acid sequence according to SEQ ID NO: 418. [0045] In some embodiments, one or more Plasmodium polypeptide or antigenic portions thereof comprised in a second polypeptide are one or more Plasmodium CSP polypeptide regions or antigenic portions thereof. In some embodiments, each of the one or more Plasmodium CSP polypeptide regions or portions thereof comprised in a second polypeptide comprise 10 or more contiguous amino acids of the amino acid sequence according to SEQ ID NO: 1. In some embodiments, one or more Plasmodium CSP polypeptide regions or portions thereof comprised in a second polypeptide comprise one or more repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223). In some embodiments, one or more Plasmodium CSP polypeptide regions or portions thereof comprised in a second polypeptide comprise one or more repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223), and wherein the second polypeptide does not comprise the amino acid sequence of NPNA (SEQ ID NO: 228). In some embodiments, one or more Plasmodium CSP polypeptide regions or portions thereof comprised in a second polypeptide comprise two or more repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223). In some embodiments, one or more Plasmodium CSP polypeptide regions or portions thereof comprised in a second polypeptide comprise five or more repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223). In some embodiments, one or more Plasmodium CSP polypeptide regions or portions thereof comprised in a second polypeptide comprise between two and twelve repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223). In some embodiments, one or more Plasmodium CSP polypeptide regions or portions thereof comprised in a second polypeptide comprise exactly three repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223). In some embodiments, one or more Plasmodium CSP polypeptide regions or portions thereof comprised in a second polypeptide comprise between four and twelve repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223). [0046] In some embodiments, one or more Plasmodium CSP polypeptide regions or portions thereof comprised in a second polypeptide comprise exactly eight repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223). In some embodiments, one or more Plasmodium CSP polypeptide regions or portions thereof comprised in a second polypeptide comprise exactly nine repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223). [0047] In some embodiments, repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223) are all contiguous with each other. In some embodiments, repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223) are not all contiguous with each other. [0048] In some embodiments, one or more Plasmodium CSP polypeptide regions or portions thereof comprised in a second polypeptide comprise three portions of a Plasmodium CSP polypeptide, wherein each portion comprises three contiguous repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223), and wherein each of the portions are not contiguous with each other. In some embodiments, one or more Plasmodium CSP polypeptide regions or portions thereof comprised in a second polypeptide comprise four portions of a Plasmodium CSP polypeptide, and wherein each portion comprises two contiguous repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223). [0049] In some embodiments, one or more Plasmodium CSP polypeptide regions or antigenic portions thereof comprise at least two repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223). In some embodiments, one or more Plasmodium CSP polypeptide regions or antigenic portions thereof comprise two to eighteen repeats of the amino acid sequence of NANP. In some embodiments, one or more Plasmodium CSP polypeptide regions or antigenic portions thereof comprise a Plasmodium CSP C-terminal region, a Plasmodium CSP C-terminal region variant, or an antigenic portion thereof. In some embodiments, one or more Plasmodium CSP polypeptide regions or antigenic portions thereof comprise: (i) at least two repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223); (ii) two to eighteen repeats of the amino acid sequence of NANP; and (iii) a Plasmodium CSP C-terminal region, a Plasmodium CSP C-terminal region variant, or an antigenic portion thereof. In some embodiments, one or more Plasmodium CSP polypeptide regions or antigenic portions thereof comprise, in N-terminal to C-terminal order: (i) at least two repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223); (ii) two to eighteen repeats of the amino acid sequence of NANP; and (iii) a Plasmodium CSP C-terminal region, a Plasmodium CSP C-terminal region variant, or an antigenic portion thereof. [0050] In some embodiments, one or more Plasmodium CSP polypeptide regions or portions thereof comprised in a second polypeptide comprise one or more Plasmodium CSP C-terminal regions or antigenic portions thereof. In some embodiments, one or more Plasmodium CSP polypeptide regions or portions thereof comprised in a second polypeptide comprise one or more Plasmodium CSP C-terminal region variants, or antigenic portions thereof. [0051] In some embodiments, one or more Plasmodium CSP polypeptide regions or portions thereof comprised in a second polypeptide comprise exactly one Plasmodium CSP C-terminal region. In some embodiments, one or more Plasmodium CSP polypeptide regions or portions thereof comprised in a second polypeptide comprise exactly one Plasmodium CSP C-terminal region, and wherein the Plasmodium CSP C-terminal region comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 235. [0052] In some embodiments, one or more Plasmodium CSP polypeptide regions or antigenic portions thereof comprise an antigenic portion of a Plasmodium CSP C-terminal region. In some embodiments, one or more Plasmodium CSP polypeptide regions or antigenic portions thereof comprise a Plasmodium CSP C-terminal region variant. In some embodiments, one or more Plasmodium CSP polypeptide regions or portions thereof comprised in a second polypeptide comprise two or more antigenic portions of a Plasmodium CSP C-terminal region. [0053] In some embodiments, an antigenic portion of a Plasmodium CSP C-terminal region comprises an amino acid sequence according SEQ ID NO: 261, wherein X3 is N or K, X4 is K, I, or R, and X5 is N or Y. In some embodiments, an antigenic portion of a Plasmodium CSP C-terminal region comprises an amino acid sequence according SEQ ID NO: 262, wherein X3 is N or K, X4 is K, I, or R, and X5 is N or Y. In some embodiments, an antigenic portion of a Plasmodium CSP C-terminal region comprises an amino acid sequence according SEQ ID NO: 263, wherein X3 is N or K, X4 is K, I, or R, and X5 is N or Y. In some embodiments, an antigenic portion of a Plasmodium CSP C-terminal region comprises an amino acid sequence according SEQ ID NO: 264, wherein X1X2 is EK or KE, X3 is N or K, X4 is K, I, or R, and X5 is N or Y. In some embodiments, an antigenic portion of a Plasmodium CSP C-terminal region comprises an amino acid sequence according SEQ ID NO: 265, wherein X1X2 is EK or KE, X3 is N or K, X4 is K, I, or R, and X5 is N or Y. In some embodiments, an antigenic portion of a Plasmodium CSP C-terminal region comprises an amino acid sequence according SEQ ID NO: 266, wherein X1X2 is EK or KE, X3 is N or K, X4 is K, I, or R, and X5 is N or Y. In some embodiments, an antigenic portion of a Plasmodium CSP C-terminal region comprises an amino acid sequence according SEQ ID NO: 267. In some embodiments, an antigenic portion of a Plasmodium CSP C-terminal region or a Plasmodium CSP C-terminal region variant comprises an amino acid sequence according SEQ ID NO: 992. In some embodiments, an antigenic portion of a Plasmodium CSP C-terminal region or a Plasmodium CSP C-terminal region variant comprises an amino acid sequence according SEQ ID NO: 993. [0054] In some embodiments, one or more Plasmodium CSP polypeptide regions or antigenic portions thereof comprise a Plasmodium CSP C-terminal region variant or antigenic portion thereof. In some embodiments, a Plasmodium CSP C-terminal region variant or antigenic portion thereof comprises one or more amino acid substitutions, insertions, or deletions. [0055] In some embodiments, a Plasmodium CSP C-terminal region variant or antigenic portion thereof comprises one or more amino acid substitutions. In some embodiments, a Plasmodium CSP C-terminal region variant or antigenic portion thereof comprises one or more amino acid substitutions, wherein the one or more amino acid substitutions comprise S301N, wherein the amino acid numbering is relative to SEQ ID NO: 1. In some embodiments, a Plasmodium CSP C-terminal region variant or antigenic portion thereof comprises one or more amino acid substitutions, wherein the one or more amino acid substitutions comprise K317E, wherein the amino acid numbering is relative to SEQ ID NO: 1. In some embodiments, a Plasmodium CSP C-terminal region variant or antigenic portion thereof comprises one or more amino acid substitutions, wherein the one or more amino acid substitutions comprise E318Q, wherein the amino acid numbering is relative to SEQ ID NO: 1. In some embodiments, a Plasmodium CSP C- terminal region variant or antigenic portion thereof comprises one or more amino acid substitutions, wherein the one or more amino acid substitutions comprise N321K, wherein the amino acid numbering is relative to SEQ ID NO: 1. In some embodiments, a Plasmodium CSP C-terminal region variant or antigenic portion thereof comprises one or more amino acid substitutions, wherein the one or more amino acid substitutions comprise E357Q, wherein the amino acid numbering is relative to SEQ ID NO: 1. In some embodiments, a Plasmodium CSP C-terminal region variant or antigenic portion thereof comprises one or more amino acid substitutions, wherein the one or more amino acid substitutions comprise A361E, wherein the amino acid numbering is relative to SEQ ID NO: 1. In some embodiments, a Plasmodium CSP C-terminal region variant or antigenic portion thereof comprises one or more amino acid substitutions, wherein the one or more amino acid substitutions comprise S301N K317E, E318Q, N321K, E357Q, A361E, or any combination thereof, wherein the amino acid numbering is relative to SEQ ID NO: 1. In some embodiments, a Plasmodium CSP C-terminal region variant or antigenic portion thereof comprises one or more amino acid substitutions, wherein the one or more amino acid substitutions comprise S301N, K317E, E318Q, N321K, E357Q, and A361E, wherein the amino acid numbering is relative to SEQ ID NO: 1. [0056] In some embodiments, a Plasmodium CSP C-terminal region variant comprises or consists of an amino acid sequence that is at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identical to the amino acid sequence of SEQ ID NO: 994. [0057] In some embodiments, a second polypeptide comprises one or more portions of the Plasmodium CSP C- terminal region, wherein each of the one or more portions comprise or consist of an amino acid sequence according to SEQ ID NO: 244. In some embodiments, a second polypeptide comprises one or more portions of the Plasmodium CSP C-terminal region, wherein each of the one or more portions comprise or consist of an amino acid sequence according to SEQ ID NO: 248. In some embodiments, a second polypeptide comprises one or more portions of the Plasmodium CSP C-terminal region, wherein each of the one or more portions comprise or consist of an amino acid sequence according to SEQ ID NO: 262. In some embodiments, a second polypeptide comprises one or more portions of the Plasmodium CSP C-terminal region, wherein each of the one or more portions comprise or consist of an amino acid sequence according to SEQ ID NO: 256. In some embodiments, a second polypeptide comprises one or more portions of the Plasmodium CSP C-terminal region, wherein each of the one or more portions comprise or consist of: (i) an amino acid sequence according to SEQ ID NO: 244; (ii) an amino acid sequence according to SEQ ID NO: 248; (iii) an amino acid sequence according to SEQ ID NO: 262; (iv) an amino acid sequence according to SEQ ID NO: 256; or (v) a combination thereof. [0058] In some embodiments, a second polypeptide comprises one portion of the Plasmodium CSP C-terminal region, wherein the portion comprises or consists of an amino acid sequence according to SEQ ID NO: 244. In some embodiments, a second polypeptide comprises one portion of the Plasmodium CSP C-terminal region, wherein the portion comprises or consists of an amino acid sequence according to SEQ ID NO: 248. In some embodiments, a second polypeptide comprises one portion of the Plasmodium CSP C-terminal region, wherein the portion comprises or consists of an amino acid sequence according to SEQ ID NO: 262. In some embodiments, a second polypeptide comprises one portion of the Plasmodium CSP C-terminal region, wherein the portion comprises or consists of an amino acid sequence according to SEQ ID NO: 256. In some embodiments, a second polypeptide comprises one portion of the Plasmodium CSP C-terminal region, wherein the portion comprises or consists of: (i) an amino acid sequence according to SEQ ID NO: 244; (ii) an amino acid sequence according to SEQ ID NO: 248; (iii) an amino acid sequence according to SEQ ID NO: 262; (iv) an amino acid sequence according to SEQ ID NO: 256; or (v) a combination thereof. In some embodiments, a second polypeptide comprises one or more portions of the Plasmodium CSP C-terminal region, wherein the one or more portions collectively comprise or consist of: (i) an amino acid sequence according to SEQ ID NO: 244; (ii) an amino acid sequence according to SEQ ID NO: 248; (iii) an amino acid sequence according to SEQ ID NO: 262; and (iv) an amino acid sequence according to SEQ ID NO: 256. [0059] In some embodiments, an antigenic portion of a Plasmodium CSP C-terminal region comprises or consists of an amino acid sequence that is at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identical to the amino acid sequence of SEQ ID NO: 259. [0060] In some embodiments, a second polypeptide comprises a serine immediately following a Plasmodium CSP C-terminal region. In some embodiments, a second polypeptide comprises a serine-valine sequence immediately following a Plasmodium CSP C-terminal region. In some embodiments, one or more Plasmodium CSP polypeptide regions or portions thereof comprised in a second polypeptide comprise one or more Plasmodium CSP junction regions, portions thereof, or variants thereof. In some embodiments, one or more Plasmodium CSP polypeptide regions or portions thereof comprised in a second polypeptide comprise two or more Plasmodium CSP junction regions or portions thereof. In some embodiments, one or more Plasmodium CSP polypeptide regions or portions thereof comprised in a second polypeptide comprise exactly one Plasmodium CSP junction region. In some embodiments, one Plasmodium CSP junction region consists of an amino acid sequence according to SEQ ID NO: 272. [0061] In some embodiments, one or more Plasmodium CSP polypeptide regions or portions thereof comprised in a second polypeptide comprise one or more portions of a Plasmodium CSP junction region. [0062] In some embodiments, one or more portions of a Plasmodium CSP junction region comprise a deletion of K93, wherein the amino acid numbering is relative to SEQ ID NO: 1. In some embodiments, one or more portions of a Plasmodium CSP junction region comprise a deletion of L94, wherein the amino acid numbering is relative to SEQ ID NO: 1. In some embodiments, one or more portions of a Plasmodium CSP junction region comprise a deletion of K95, wherein the amino acid numbering is relative to SEQ ID NO: 1. In some embodiments, one or more portions of a Plasmodium CSP junction region comprise a deletion of Q96, wherein the amino acid numbering is relative to SEQ ID NO: 1. In some embodiments, one or more portions of a Plasmodium CSP junction region comprise a deletion of P97, wherein the amino acid numbering is relative to SEQ ID NO: 1. In some embodiments, one or more portions of a Plasmodium CSP junction region comprise a deletion of K93, L94, K95, Q96, P97, or a combination thereof, and wherein the amino acid numbering is relative to SEQ ID NO: 1. In some embodiments, one or more portions of a Plasmodium CSP junction region comprise a deletion of K93, L94, K95, and Q96, and wherein the amino acid numbering is relative to SEQ ID NO: 1. In some embodiments, one or more portions of a Plasmodium CSP junction region comprise a deletion of K93, L94, K95, Q96 and P97, and wherein the amino acid numbering is relative to SEQ ID NO: 1. [0063] In some embodiments, each portion of a Plasmodium CSP junction region comprises or consists of an amino acid sequence according to SEQ ID NO: 275. In some embodiments, each portion of a Plasmodium CSP junction region comprises or consists of an amino acid sequence according to SEQ ID NO: 277. In some embodiments, two or more Plasmodium CSP junction regions consist of an amino acid sequence according to SEQ ID NO: 272. [0064] In some embodiments, one or more Plasmodium CSP polypeptide regions or portions thereof comprised in a second polypeptide comprise two or more portions of a Plasmodium CSP junction region. In some embodiments, two or more portions of a Plasmodium CSP junction region comprise a deletion of K93, wherein the amino acid numbering is relative to SEQ ID NO: 1. In some embodiments, two or more portions of a Plasmodium CSP junction region comprise a deletion of L94, wherein the amino acid numbering is relative to SEQ ID NO: 1. In some embodiments, two or more portions of a Plasmodium CSP junction region comprise a deletion of K95, wherein the amino acid numbering is relative to SEQ ID NO: 1. In some embodiments, two or more portions of a Plasmodium CSP junction region comprise a deletion of Q96, wherein the amino acid numbering is relative to SEQ ID NO: 1. In some embodiments, two or more portions of a Plasmodium CSP junction region comprise a deletion of P97, wherein the amino acid numbering is relative to SEQ ID NO: 1. In some embodiments, two or more portions of a Plasmodium CSP junction region comprise a deletion of K93, L94, K95, Q96, P97, or a combination thereof, and wherein the amino acid numbering is relative to SEQ ID NO: 1. In some embodiments, two or more portions of a Plasmodium CSP junction region comprise a deletion of K93, L94, K95, and Q96, and wherein the amino acid numbering is relative to SEQ ID NO: 1. In some embodiments, two or more portions of a Plasmodium CSP junction region comprise a deletion of K93, L94, K95, Q96 and P97, and wherein the amino acid numbering is relative to SEQ ID NO: 1. [0065] In some embodiments, each portion of a Plasmodium CSP junction region comprises or consists of an amino acid sequence according to SEQ ID NO: 275. In some embodiments, each portion of a Plasmodium CSP junction region comprises or consists of an amino acid sequence according to SEQ ID NO: 277. [0066] In some embodiments, one or more Plasmodium CSP polypeptide regions or portions thereof comprised in a second polypeptide comprise one or more Plasmodium CSP junction region variants. In some embodiments, a Plasmodium CSP junction region variant comprises one or more substitution mutations. In some embodiments, one or more substitution mutations comprise a K93A mutation, wherein the amino acid numbering is relative to SEQ ID NO: 1. In some embodiments, one or more substitution mutations comprise a L94A mutation, wherein the amino acid numbering is relative to SEQ ID NO: 1. In some embodiments, one or more substitution mutations comprise a K93A mutation, an L94A mutation, or both, wherein the amino acid numbering is relative to SEQ ID NO: 1. In some embodiments, each Plasmodium CSP junction region variant comprises the amino acid sequence of AAKQ. [0067] In some embodiments, one or more Plasmodium CSP polypeptide regions or portions thereof comprised in a second polypeptide comprise one or more Plasmodium CSP N-terminal end regions or portions thereof. In some embodiments, one or more Plasmodium CSP polypeptide regions or portions thereof comprised in a second polypeptide comprise two or more Plasmodium CSP N-terminal end regions or portions thereof. In some embodiments, each Plasmodium CSP N-terminal end region consists of an amino acid sequence according to SEQ ID NO: 285. [0068] In some embodiments, a second polypeptide does not comprise a Plasmodium CSP N-terminal end region or any portion thereof. [0069] In some embodiments, one or more Plasmodium CSP polypeptide regions or portions thereof comprised in a second polypeptide comprise one or more Plasmodium CSP N-terminal regions or portions thereof. In some embodiments, one or more Plasmodium CSP polypeptide regions or portions thereof comprised in a second polypeptide comprise two or more Plasmodium CSP N-terminal regions or portions thereof. [0070] In some embodiments, each Plasmodium CSP N-terminal region comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 288. [0071] In some embodiments, one or more Plasmodium CSP polypeptide regions or portions thereof comprised in a second polypeptide comprise an antigenic portion of a Plasmodium CSP N-terminal region. In some embodiments, an antigenic portion of a Plasmodium CSP N-terminal region is a Plasmodium CSP N-terminal start region. In some embodiments, a Plasmodium CSP N-terminal start region comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 1010. [0072] In some embodiments, a second polypeptide does not comprise a Plasmodium CSP N-terminal region or any portion thereof. [0073] In some embodiments, one or more Plasmodium CSP polypeptide regions or portions thereof comprised in a second polypeptide comprise one or more Plasmodium CSP major repeat regions or portions thereof. In some embodiments, one or more Plasmodium CSP major repeat regions or portions thereof comprise the amino acid sequence NANPNA or NPNANP. In some embodiments, one or more Plasmodium CSP polypeptide regions or portions thereof comprised in a second polypeptide comprise at least two Plasmodium CSP major repeat region portions. In some embodiments, one or more Plasmodium CSP polypeptide regions or portions thereof comprised in a second polypeptide comprise at least two Plasmodium CSP major repeat region portions, wherein each CSP major repeat region portion comprises at least 4 and at most 7 repeats of the sequence NANP. In some embodiments, one or more Plasmodium CSP polypeptide regions or portions thereof comprised in a second polypeptide comprise two or three Plasmodium CSP major repeat region portions, wherein each CSP major repeat region portion comprises 6 repeats of the sequence NANP (SEQ ID NO: 230). In some embodiments, one or more Plasmodium CSP polypeptide regions or portions thereof comprised in a second polypeptide comprise two or three Plasmodium CSP major repeat region portions, wherein each CSP major repeat region portion comprises 6 repeats of the sequence NANP (SEQ ID NO: 230). In some embodiments, one or more Plasmodium CSP polypeptide regions or portions thereof comprised in a second polypeptide comprise exactly one Plasmodium CSP major repeat region or portion thereof, and the Plasmodium CSP major repeat region or portion thereof comprises a total of at least 2 and at most 35 repeats of the amino acid sequence NANP (SEQ ID NO: 230). [0074] In some embodiments, a Plasmodium CSP major repeat region or portion thereof comprises two contiguous stretches of repeats of the amino acid sequence NANP (SEQ ID NO: 230), and wherein the two contiguous stretches of repeats of the amino acid sequence NANP (SEQ ID NO: 230) flank an amino acid sequence of NVDP (SEQ ID NO:229). In some embodiments, a Plasmodium CSP major repeat region comprises, in N-terminus to C-terminus order, 17 repeats of the amino acid sequence NANP (SEQ ID NO: 230), an amino acid sequence of NVDP (SEQ ID NO:229), and 18 repeats of the amino acid sequence NANP (SEQ ID NO: 230). [0075] In some embodiments, a portion of a Plasmodium CSP major repeat region consists of at most 18 contiguous repeats of the amino acid sequence NANP (SEQ ID NO: 230). In some embodiments, a portion of the Plasmodium CSP major repeat region consists of 2 contiguous repeats of the amino acid sequence NANP (SEQ ID NO: 230). [0076] In some embodiments, a Plasmodium CSP major repeat region comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 305. [0077] In some embodiments, one or more Plasmodium CSP polypeptide regions or antigenic portions thereof comprises an antigenic portion of a Plasmodium CSP major repeat region. In some embodiments, an antigenic portion of a Plasmodium CSP major repeat region comprises at least six repeats of the amino acid sequence of NANP. In some embodiments, an antigenic portion of a Plasmodium CSP major repeat region further comprises an asparagine-alanine positioned immediately following of the six repeats of the amino acid sequence of NANP (SEQ ID NO: 230). In some embodiments, an antigenic portion of a Plasmodium CSP major repeat region comprises or consists of an amino acid sequence that is at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identical to the amino acid sequence of SEQ ID NO: 303. [0078] In some embodiments, an antigenic portion of a Plasmodium CSP major repeat region comprises eighteen repeats of the amino acid sequence of NANP (SEQ ID NO: 230). In some embodiments, an antigenic portion of a Plasmodium CSP major repeat region comprises or consists of an amino acid sequence that is at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identical to the amino acid sequence of SEQ ID NO: 308. [0079] In some embodiments, a second polypeptide does not comprise a Plasmodium CSP N-terminal region or any portion thereof. In some embodiments, a second polypeptide does not comprise a Plasmodium CSP C-terminal region or any portion thereof. In some embodiments, a second polypeptide does not comprise (i) a Plasmodium CSP N-terminal region or any portion thereof and/or (ii) a Plasmodium CSP C-terminal region or any portion thereof. [0080] In some embodiments, a second polypeptide does not comprise a Plasmodium CSP major repeat region or a portion of a Plasmodium CSP major repeat region comprising the amino acid sequence NPNA (SEQ ID NO: 228). [0081] In some embodiments, one or more Plasmodium CSP polypeptide regions or portions thereof, if present in a second polypeptide, are in the following N-terminus to C-terminus order: (i) one or more Plasmodium CSP N- terminal regions or portions thereof; (ii) one or more Plasmodium CSP N-terminal end regions or portions thereof; (iii) one or more Plasmodium CSP junction regions, portions thereof, or variants thereof; (iv) one or more repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223); (v) one or more Plasmodium CSP major repeat regions or portions thereof; and (vi) one or more Plasmodium CSP C-terminal regions or portions thereof. [0082] In some embodiments, one or more Plasmodium CSP polypeptide regions or portions thereof, if present in the second polypeptide, are in the following N-terminus to C-terminus order: (i) one Plasmodium CSP N-terminal region or portion thereof; (ii) one Plasmodium CSP N-terminal end region or portion thereof; (iii) one Plasmodium CSP junction region, portion thereof, or variant thereof; (iv) one or more repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223); (v) one Plasmodium CSP major repeat region or portion thereof; and (vi) one Plasmodium CSP C-terminal region or portion thereof. [0083] In some embodiments, a second polypeptide comprises one or more helper antigens. In some embodiments, one or more helper antigens comprise a Plasmodium antigen. In some embodiments, one or more helper antigens are Plasmodium 2-phospho-D-glycerate hydro-lyase antigen, Plasmodium liver stage antigen 1(a), (LSA-1(a)), Plasmodium liver stage antigen 1(b) (LSA-1(b)), Plasmodium thrombospondin-related anonymous protein (TRAP), Plasmodium liver stage associated protein 1 (LSAP1), Plasmodium liver stage associated protein 2 (LSAP2), Plasmodium UIS3, Plasmodium ETRAMP10.3, Plasmodium liver specific protein 1 (LISP-1), Plasmodium liver specific protein 2 (LISP-2), Plasmodium liver stage antigen 3 (LSA-3), Plasmodium EXP1, Plasmodium E140, Plasmodium reticulocyte-binding protein homolog 5 (Rh5), Plasmodium glutamic acid-rich protein (GARP), Plasmodium parasite- infected erythrocyte surface protein 2 (PIESP2), Plasmodium Cysteine-Rich Protective Antigen (CyRPA), Plasmodium Ripr, Plasmodium P113, or a combination thereof. [0084] In some embodiments, one or more helper antigens comprise or consist of a P. falciparum 2-phospho- D-glycerate hydro-lyase antigen. In some embodiments, a P. falciparum 2-phospho-D-glycerate hydro-lyase antigen comprises or consists of an amino acid sequence according to SEQ ID NO: 388. [0085] In some embodiments, one or more helper antigens comprise or consist of a P. falciparum liver-stage antigen 3. In some embodiments, a P. falciparum liver-stage antigen 3 comprises or consists of an amino acid sequence according to SEQ ID NO: 391. [0086] In some embodiments, one or more helper antigens comprise an Anopheles antigen. In some embodiments, a helper antigen comprises or consists of an Anopheles gambiae TRIO. In some embodiments, an Anopheles gambiae TRIO comprises or consists of an amino acid sequence according to SEQ ID NO: 393. [0087] In some embodiments, a second polypeptide comprises a secretory signal and the helper antigen immediately follows the secretory signal. In some embodiments, a second polypeptide comprises a helper antigen at the C-terminus of the second polypeptide. [0088] In some embodiments, a second polypeptide comprises a multimerization region. In some embodiments, a multimerization region comprises or consists of a trimerization region. In some embodiments, a trimerization region comprises or consists of a fibritin region. In some embodiments, a fibritin region comprises or consists of an amino acid sequence according to SEQ ID NO: 399. In some embodiments, a second polypeptide comprises a multimerization region at the N-terminus of the second polypeptide. [0089] In some embodiments, a second polypeptide comprises a self-aggregation region. In some embodiments, a self-aggregation region comprises or consists of a ferritin region. In some embodiments, a ferritin region comprises or consists of an amino acid sequence according to SEQ ID NO: 402. In some embodiments, a polypeptide comprises a self-aggregation region at the N-terminus of the polypeptide. [0090] In some embodiments, a second polypeptide comprises a secretory signal. In some embodiments, a secretory signal comprises or consists of a Plasmodium secretory signal. In some embodiments, a Plasmodium secretory signal comprises or consists of a Plasmodium CSP secretory signal. In some embodiments, a Plasmodium CSP secretory signal comprises or consists of an amino acid sequence according to SEQ ID NO: 332. In some embodiments, a secretory signal comprises or consists of a heterologous secretory signal. In some embodiments, a heterologous secretory signal comprises or consists of a non-human secretory signal. In some embodiments, a heterologous secretory signal comprises or consists of a viral secretory signal. In some embodiments, a viral secretory signal comprises or consists of an HSV secretory signal. In some embodiments, a HSV secretory signal comprises or consists of an HSV-1 or HSV-2 secretory signal. In some embodiments, a HSV secretory signal comprises or consists of an HSV glycoprotein D (gD) secretory signal. In some embodiments, a HSV gD secretory signal comprises or consists of an amino acid sequence according to SEQ ID NO: 314. In some embodiments, a HSV gD secretory signal comprises or consists of an amino acid sequence according to SEQ ID NO: 320. In some embodiments, a viral secretory signal comprises or consists of an Ebola virus secretory signal. In some embodiments, a Ebola virus secretory signal comprises or consists of an Ebola virus spike glycoprotein (SGP) secretory signal. In some embodiments, a Ebola virus SGP secretory signal comprises or consists of an amino acid sequence according to SEQ ID NO: 335. In some embodiments, a secretory signal is located at the N-terminus of a second polypeptide. In some embodiments, a second polypeptide does not comprise a secretory signal. [0091] In some embodiments, a second polypeptide comprises a transmembrane region. In some embodiments, a transmembrane region comprises or consists of a Plasmodium transmembrane region. In some embodiments, a Plasmodium transmembrane region comprises or consists of a Plasmodium CSP glycosylphosphatidylinositol (GPI) anchor region. In some embodiments, a Plasmodium CSP GPI anchor region comprises or consists of an amino acid sequence according to SEQ ID NO: 385. In some embodiments, a transmembrane region comprises or consists of a heterologous transmembrane region. In some embodiments, a heterologous transmembrane region does not comprise a hemagglutinin transmembrane region. In some embodiments, a heterologous transmembrane region comprises or consists of a non-human transmembrane region. In some embodiments, a heterologous transmembrane region comprises or consists of a viral transmembrane region. In some embodiments, a viral transmembrane region comprises or consists of an HSV transmembrane region. In some embodiments, a HSV transmembrane region comprises or consists of an HSV-1 or HSV-2 transmembrane region. In some embodiments, a HSV transmembrane region comprises or consists of an HSV gD transmembrane region. In some embodiments, a HSV gD transmembrane region comprises or consists of an amino acid sequence according to SEQ ID NO: 379. In some embodiments, a heterologous transmembrane region comprises or consists of a human transmembrane region. In some embodiments, a human transmembrane region comprises or consists of a human decay accelerating factor glycosylphosphatidylinositol (hDAF-GPI) anchor region. In some embodiments, a hDAF-GPI anchor region comprises or consists of an amino acid sequence according to SEQ ID NO: 382. In some embodiments, a second polypeptide does not comprise a transmembrane region. [0092] In some embodiments, a second polypeptide comprises one or more linkers. In some embodiments, one or more linkers comprise one or more glycine-serine linkers. In some embodiments, one or more linkers comprise or consist of an amino acid sequence according to SEQ ID NO: 404. In some embodiments, one or more linkers comprise or consist of an amino acid sequence according to SEQ ID NO: 411. In some embodiments, one or more linkers comprise or consist of an amino acid sequence according to SEQ ID NO: 408. In some embodiments, one or more linkers comprise or consist of an amino acid sequence according to SEQ ID NO: 412. [0093] In some embodiments, a second polypeptide comprises a linker between the C-terminal region or portion thereof and the transmembrane region. In some embodiments, a second polypeptide comprises a linker after an amino acid sequence of NANPNVDP (SEQ ID NO: 223). In some embodiments, a second polypeptide comprises a secretory signal. In some embodiments, a second polypeptide comprises one or more Plasmodium CSP junction regions, portions thereof, or variants thereof. In some embodiments, a second polypeptide comprises one or more repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223). In some embodiments, a second polypeptide comprises one or more Plasmodium CSP C-terminal regions or portions thereof. In some embodiments, a second polypeptide comprises a transmembrane region. In some embodiments, a second polypeptide does not comprise an amino acid sequence of NPNA (SEQ ID NO: 228). In some embodiments, a second polypeptide does not comprise a Plasmodium CSP N-terminal region or portion thereof. In some embodiments, a second polypeptide comprises: (i) a secretory signal; (ii) one or more Plasmodium CSP junction regions, portions thereof, or variants thereof; (iii) one or more repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223); (iv) one or more Plasmodium CSP C- terminal regions or portions thereof; and (v) a transmembrane region, and a second polypeptide does not comprise: (a) an amino acid sequence of NPNA (SEQ ID NO: 228); and (b) a Plasmodium CSP N-terminal region or portion thereof. In some embodiments, a second polypeptide does not comprise a Plasmodium CSP N-terminal end region. In some embodiments, a second polypeptide comprises one or more Plasmodium CSP N-terminal end regions or portions thereof. [0094] In some embodiments, a second polypeptide comprises: (i) a secretory signal; (ii) one or more Plasmodium CSP junction regions, portions thereof, or variants thereof; (iii) one or more repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223); and (iv) one or more Plasmodium CSP C-terminal regions or portions thereof. [0095] In some embodiments, a second polypeptide comprises a secretory signal. In some embodiments, a second polypeptide comprises three or more Plasmodium CSP junction regions, portions thereof, or variants thereof. In some embodiments, a second polypeptide comprises three or more repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223). In some embodiments, a second polypeptide comprises two or more Plasmodium CSP major repeat region portions. In some embodiments, a second polypeptide does not comprise a Plasmodium CSP N- terminal region or portion thereof. In some embodiments, a second polypeptide does not comprise a Plasmodium CSP C-terminal region or portion thereof. In some embodiments, a second polypeptide comprises: (i) a secretory signal; (ii) three or more Plasmodium CSP junction regions, portions thereof, or variants thereof; (iii) three or more repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223); and (iv) two or more Plasmodium CSP major repeat region portions, and a second polypeptide does not comprise: (a) a Plasmodium CSP N-terminal region or portion thereof; and (b) a Plasmodium CSP C-terminal region or portion thereof. In some embodiments, a second polypeptide comprises an amino acid sequence that has at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identity to a sequence of SEQ ID NO: 108. [0096] In some embodiments, a second polypeptide comprises: (i) a secretory signal; (ii) one or more Plasmodium CSP junction regions, portions thereof, or variants thereof; (iii) one or more repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223); (iv) one or more Plasmodium CSP C-terminal regions or portions thereof; and (v) a transmembrane region. [0097] In some embodiments, a second polypeptide comprises: (i) a secretory signal; (ii) one or more Plasmodium CSP junction regions, portions thereof, or variants thereof; (iii) one or more repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223); (iv) one or more Plasmodium CSP C-terminal regions or portions thereof; and (v) a transmembrane region. In some embodiments, a second polypeptide comprises: (i) a secretory signal; (ii) three or more Plasmodium CSP junction regions, portions thereof, or variants thereof; (iii) three or more repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223); (iv) two or more Plasmodium CSP major repeat region portions; and (v) a transmembrane region, and a second polypeptide does not comprise: (a) a Plasmodium CSP N- terminal region or portion thereof; and (b) a Plasmodium CSP C-terminal region or portion thereof. In some embodiments, a second polypeptide comprises an amino acid sequence that has at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identity to a sequence of SEQ ID NO: 107 or 109. [0098] In some embodiments, a second polypeptide comprises: (i) a secretory signal; (ii) three or more Plasmodium CSP junction regions, portions thereof, or variants thereof; (iii) three or more repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223); and (iv) two or more Plasmodium CSP major repeat region portions, wherein a second polypeptide does not comprise: (a) a Plasmodium CSP N-terminal region or portion thereof; and (b) a Plasmodium CSP C-terminal region or portion thereof. In some embodiments, a second polypeptide comprises an amino acid sequence that has at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to a sequence of SEQ ID NO: 110 or 111. [0099] In some embodiments, a second polypeptide comprises one or more helper antigens. [0100] In some embodiments, a second polypeptide comprises: (i) a secretory signal; (ii) a Plasmodium CSP N- terminal end region; (iii) a Plasmodium CSP junction region; (iv) nine repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223); (v) a Plasmodium CSP C-terminal region; and (vi) five antigenic repeat regions, wherein each antigenic repeat region comprises: (A) a linker; and (B) a helper antigen, and a second polypeptide does not comprise any of: (a) an amino acid sequence of NPNA (SEQ ID NO: 228); (b) a Plasmodium CSP N-terminal region or portion thereof; and (c) a transmembrane region. In some embodiments, a second polypeptide comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 36. [0101] In some embodiments, a second polypeptide comprises: (i) a secretory signal; (ii) a helper antigen; (iii) a linker; (iv) a Plasmodium CSP N-terminal end region; (v) a Plasmodium CSP junction region; (vi) nine repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223); (vii) a Plasmodium CSP C-terminal region; (viii) a serine- valine sequence immediately following the Plasmodium CSP C-terminal region; (ix) a linker; and (x) a transmembrane region, and a second polypeptide does not comprise any of: (a) an amino acid sequence of NPNA (SEQ ID NO: 228); and (b) a Plasmodium CSP N-terminal region or portion thereof. In some embodiments, a second polypeptide comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 39. [0102] In some embodiments, a second polypeptide comprises: (i) a secretory signal; (ii) a portion of a Plasmodium CSP junction region; (iii) three repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223); (iv) a Plasmodium CSP C-terminal region; (v) a serine-valine sequence immediately following the Plasmodium CSP C- terminal region; (vi) a linker; and (vii) a transmembrane region, and a second polypeptide does not comprise any of: (a) a Plasmodium CSP N-terminal region or portion thereof; (b) a Plasmodium CSP N-terminal end region or portion thereof; and (c) an amino acid sequence of NPNA (SEQ ID NO: 228). In some embodiments, a second polypeptide comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 57. [0103] In some embodiments, a second polypeptide comprises: (i) a secretory signal; (ii) a portion of a Plasmodium CSP junction region; (iii) nine repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223); (iv) a Plasmodium CSP C-terminal region; (v) a serine-valine sequence immediately following the Plasmodium CSP C- terminal region; (vi) a linker; and (vii) a transmembrane region, and a second polypeptide does not comprise any of: (a) a Plasmodium CSP N-terminal region or portion thereof; (b) a Plasmodium CSP N-terminal end region or portion thereof; (c) an amino acid sequence of NPNA (SEQ ID NO: 228). In some embodiments, a second polypeptide comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 60. [0104] In some embodiments, a second polypeptide comprises: (i) a secretory signal; (ii) a Plasmodium CSP junction region; (iii) three repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223); (iv) a Plasmodium CSP C-terminal region; (v) a serine-valine sequence immediately following the Plasmodium CSP C-terminal region; (vi) a linker; and (vii) a transmembrane region, and a second polypeptide does not comprise any of: (a) a Plasmodium CSP N-terminal region or portion thereof; (b) a Plasmodium CSP N-terminal end region or portion thereof; and (c) an amino acid sequence of NPNA (SEQ ID NO: 228). In some embodiments, a second polypeptide comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 63. [0105] In some embodiments, a second polypeptide comprises: (i) a secretory signal; (ii) a Plasmodium CSP junction region; (iii) nine repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223); (iv) a Plasmodium CSP C-terminal region; (v) a serine-valine sequence immediately following the Plasmodium CSP C-terminal region; (vi) a linker; and (vii) a transmembrane region, and a second polypeptide does not comprise any of: (a) a Plasmodium CSP N-terminal region or portion thereof; (b) a Plasmodium CSP N-terminal end region or portion thereof; and (c) an amino acid sequence of NPNA (SEQ ID NO: 228). In some embodiments, a second polypeptide comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 66. [0106] In some embodiments, a second polypeptide comprises: (i) a secretory signal; (ii) a Plasmodium CSP junction region variant; (iii) three repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223); (iv) a Plasmodium CSP C-terminal region; (v) a serine-valine sequence immediately following the Plasmodium CSP C- terminal region; (vi) a linker; and (vii) a transmembrane region, and a second polypeptide does not comprise any of: (a) a Plasmodium CSP N-terminal region or portion thereof; (b) a Plasmodium CSP N-terminal end region or portion thereof; and (c) an amino acid sequence of NPNA (SEQ ID NO: 228). In some embodiments, a second polypeptide comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 69. [0107] In some embodiments, a second polypeptide comprises: (i) a secretory signal; (ii) a Plasmodium CSP junction region variant; (iii) nine repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223); (iv) a Plasmodium CSP C-terminal region; (v) a serine-valine sequence immediately following the Plasmodium CSP C- terminal region; (vi) a linker; and (vii) a transmembrane region, and a second polypeptide does not comprise any of: (a) a Plasmodium CSP N-terminal region or portion thereof; (b) a Plasmodium CSP N-terminal end region or portion thereof; and (c) an amino acid sequence of NPNA (SEQ ID NO: 228). In some embodiments, a second polypeptide comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 72. [0108] In some embodiments, a second polypeptide comprises: (i) a secretory signal; (ii) a portion of a Plasmodium CSP junction region; (iii) three repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223); (iv) a Plasmodium CSP C-terminal region; (v) a serine-valine sequence immediately following the Plasmodium CSP C- terminal region; (vi) a linker; and (vii) a transmembrane region, and a second polypeptide does not comprise any of: (a) a Plasmodium CSP N-terminal region or portion thereof; (b) a Plasmodium CSP N-terminal end region or portion thereof; and (c) an amino acid sequence of NPNA (SEQ ID NO: 228). In some embodiments, a second polypeptide comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 75. [0109] In some embodiments, a second polypeptide comprises: (i) a secretory signal; (ii) a portion of a Plasmodium CSP junction region; (iii) nine repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223); (iv) a Plasmodium CSP C-terminal region; (v) a serine-valine sequence immediately following the Plasmodium CSP C- terminal region; (vi) a linker; and (vii) a transmembrane region, and a second polypeptide does not comprise any of: (a) a Plasmodium CSP N-terminal region or portion thereof; (b) a Plasmodium CSP N-terminal end region or portion thereof; and (c) an amino acid sequence of NPNA (SEQ ID NO: 228). In some embodiments, a second polypeptide comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 78. [0110] In some embodiments, second polypeptide comprises: (i) a secretory signal; (ii) a Plasmodium CSP N- terminal end region; (iii) a Plasmodium CSP junction region; (iv) nine repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223); (v) a Plasmodium CSP C-terminal region; (vi) a serine-valine sequence immediately following the Plasmodium CSP C-terminal region; (vii) a linker; and (viii) a transmembrane region, and a second polypeptide does not comprise any of: (a) a Plasmodium CSP N-terminal region or portion thereof; (b) an amino acid sequence of NPNA (SEQ ID NO: 228). In some embodiments, a second polypeptide comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 81. [0111] In some embodiments, a second polypeptide comprises: (i) a secretory signal; (ii) a Plasmodium CSP N- terminal end region; (iii) a Plasmodium CSP junction region variant; (iv) nine repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223); (v) a Plasmodium CSP C-terminal region; (vi) a serine-valine sequence immediately following the Plasmodium CSP C-terminal region; (vii) a linker; and (viii) a transmembrane region, and a second polypeptide does not comprise any of: (a) a Plasmodium CSP N-terminal region or portion thereof; and (b) an amino acid sequence of NPNA (SEQ ID NO: 228). In some embodiments, a second polypeptide comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 84. [0112] In some embodiments, a second polypeptide comprises: (i) a secretory signal; (ii) a Plasmodium CSP N- terminal end region; (iii) a Plasmodium CSP junction region; (iv) nine repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223); (v) a Plasmodium CSP C-terminal region; and (vi) a transmembrane region, and a second polypeptide does not comprise any of: (a) a Plasmodium CSP N-terminal region or portion thereof; and (b) an amino acid sequence of NPNA (SEQ ID NO: 228). In some embodiments, a second polypeptide comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 102. [0113] In some embodiments, a second polypeptide comprises: (i) a secretory signal; (ii) a Plasmodium CSP N- terminal end region; (iii) a Plasmodium CSP junction region; (iv) nine repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223); (v) a Plasmodium CSP C-terminal region; and (vi) a transmembrane region, and a second polypeptide does not comprise any of: (a) a Plasmodium CSP N-terminal region or portion thereof; (b) an amino acid sequence of NPNA (SEQ ID NO: 228). In some embodiments, a second polypeptide comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 105. [0114] In some embodiments, a second polypeptide comprises: (i) a secretory signal; (ii) two or more Plasmodium CSP neutralizing region repeats, wherein each Plasmodium CSP neutralizing region repeat comprises or consists of: (a) a Plasmodium CSP N-terminal end region; (b) a Plasmodium CSP junction region; (c) two repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223); and (d) a linker; (iii) a portion of a Plasmodium CSP major repeat region; (iv) a Plasmodium CSP C-terminal region; (v) a serine-valine sequence immediately following the Plasmodium CSP C-terminal region; (vi) a linker; and (vii) a transmembrane region, and a second polypeptide does not comprise a Plasmodium CSP N-terminal region or portion thereof. In some embodiments, a second polypeptide comprises exactly four Plasmodium CSP neutralizing region repeats. In some embodiments, a second polypeptide comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 87. [0115] In some embodiments, a second polypeptide comprises: (i) a secretory signal; (ii) one Plasmodium CSP junction region; (iii) three repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223); (iv) a Plasmodium CSP major repeat region; (v) one Plasmodium CSP C-terminal region; (vi) a serine-valine sequence immediately following the Plasmodium CSP C-terminal region; (vii) a linker; and (viii) a transmembrane region, and a second polypeptide does not comprise any of: (a) a Plasmodium CSP N-terminal region or portion thereof; and (b) a Plasmodium CSP N-terminal end region or portion thereof. In some embodiments, a second polypeptide comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 30. [0116] In some embodiments, a second polypeptide comprises: (i) a secretory signal; (ii) a Plasmodium CSP N- terminal region; (iii) a Plasmodium CSP N-terminal end region; (iv) a portion of a Plasmodium CSP junction region; (v) three repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223); (vi) a Plasmodium CSP major repeat region; (vii) a Plasmodium CSP C-terminal region; and (viii) a serine immediately following the Plasmodium CSP C- terminal region, and a second polypeptide does not comprise a transmembrane region. In some embodiments, a second polypeptide comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 27. [0117] In some embodiments, a second polypeptide comprises: (i) a secretory signal; (ii) a Plasmodium CSP N- terminal region; (iii) a Plasmodium CSP N-terminal end region; (iv) a Plasmodium CSP junction region; (v) three repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223); (vi) a Plasmodium CSP major repeat region; (vii) a Plasmodium CSP C-terminal region; and (viii) a serine immediately following the Plasmodium CSP C-terminal region, and a second polypeptide does not comprise a transmembrane region. In some embodiments, a second polypeptide comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 8. [0118] In some embodiments, a second polypeptide comprises: (i) a secretory signal; (ii) a Plasmodium CSP N- terminal region; (iii) a Plasmodium CSP N-terminal end region; (iv) a Plasmodium CSP junction region; (v) three repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223); (vi) a Plasmodium CSP major repeat region; (vii) a Plasmodium CSP C-terminal region; and (viii) a serine immediately following the Plasmodium CSP C-terminal region, and a second polypeptide does not comprise a transmembrane region. In some embodiments, a second polypeptide comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 24. [0119] In some embodiments, a second polypeptide comprises: (i) a secretory signal; (ii) a Plasmodium CSP N- terminal region; (iii) a Plasmodium CSP N-terminal end region; (iv) a Plasmodium CSP junction region; (v) three repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223); (vi) a Plasmodium CSP major repeat region; (vii) a Plasmodium CSP C-terminal region; and (viii) a serine-valine sequence immediately following the Plasmodium CSP C-terminal region, and a second polypeptide does not comprise a transmembrane region. In some embodiments, a second polypeptide comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 99. [0120] In some embodiments, a second polypeptide comprises: (i) a secretory signal; (ii) a Plasmodium CSP N- terminal region; (iii) a Plasmodium CSP N-terminal end region; (iv) a Plasmodium CSP junction region; (v) three repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223); (vi) a Plasmodium CSP major repeat region; (vii) a Plasmodium CSP C-terminal region; and (viii) a transmembrane region. In some embodiments, a second polypeptide comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 33. [0121] In some embodiments, a second polypeptide comprises: (i) a secretory signal; (ii) a Plasmodium CSP N- terminal region; (iii) a Plasmodium CSP N-terminal end region; (iv) a Plasmodium CSP junction region; (v) three repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223), (vi) a Plasmodium CSP major repeat region; (vii) a Plasmodium CSP C-terminal region; (viii) a serine-valine sequence immediately following the Plasmodium CSP C-terminal region; (ix) a linker; and (x) a multimerization region, and a second polypeptide does not comprise a transmembrane region. In some embodiments, a second polypeptide comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 42. [0122] In some embodiments, a second polypeptide comprises: (i) a secretory signal; (ii) a Plasmodium CSP N- terminal region; (iii) a Plasmodium CSP N-terminal end region; (iv) a Plasmodium CSP junction region; (v) three repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223), (vi) a Plasmodium CSP major repeat region; (vii) a Plasmodium CSP C-terminal region; (viii) a serine immediately following the Plasmodium CSP C-terminal region; (ix) a linker; and (x) a transmembrane region. In some embodiments, a second polypeptide comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 48. [0123] In some embodiments, a second polypeptide comprises: (i) a secretory signal; (ii) a Plasmodium CSP N- terminal region; (iii) a Plasmodium CSP N-terminal end region; (iv) a Plasmodium CSP junction region; (v) three repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223), (vi) a Plasmodium CSP major repeat region; (vii) a Plasmodium CSP C-terminal region; (viii) a serine-valine sequence immediately following the Plasmodium CSP C-terminal region; (ix) a linker; and (x) a transmembrane region. In some embodiments, a second polypeptide comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 90. [0124] In some embodiments, a second polypeptide comprises: (i) a secretory signal; (ii) a Plasmodium CSP N- terminal region; (iii) a Plasmodium CSP N-terminal end region; (iv) a Plasmodium CSP junction region; (v) three repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223), (vi) a Plasmodium CSP major repeat region; (vii) a Plasmodium CSP C-terminal region; (viii) a serine-valine sequence immediately following the Plasmodium CSP C-terminal region; (ix) a linker; and (x) a transmembrane region. In some embodiments, a second polypeptide comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 90. [0125] In some embodiments, a second polypeptide comprises: (i) a secretory signal; (ii) a Plasmodium CSP N- terminal region; (iii) a Plasmodium CSP N-terminal end region; (iv) a Plasmodium CSP junction region; (v) three repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223); (vi) a Plasmodium CSP major repeat region; (vii) a Plasmodium CSP C-terminal region; (viii) a serine immediately following the Plasmodium CSP C-terminal region; and (ix) a transmembrane region. In some embodiments, a second polypeptide comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 21. [0126] In some embodiments, a second polypeptide comprises: (i) a secretory signal; (ii) an antigenic portion of a Plasmodium CSP major repeat region; (iii) a Plasmodium CSP C-terminal region; and (iv) a serine-valine immediately following the Plasmodium CSP C-terminal region. In some embodiments, a second polypeptide comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 51. [0127] In some embodiments, a second polypeptide comprises: (i) a secretory signal; (ii) an antigenic portion of a Plasmodium CSP major repeat region; (iii) a Plasmodium CSP C-terminal region; (iv) a serine immediately following the Plasmodium CSP C-terminal region; (v) a linker; and (vi) a transmembrane region. In some embodiments, a second polypeptide comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 54. [0128] In some embodiments, one or more Plasmodium CSP polypeptide regions or portions thereof comprised in a second polypeptide comprise in N-terminus to C-terminus order: (i) three contiguous repeats of the amino acid sequence NANPNVDP (SEQ ID NO: 223); (ii) six contiguous repeats of the amino acid sequence NANP (SEQ ID NO: 230); (iii) three contiguous repeats of the amino acid sequence NANPNVDP (SEQ ID NO: 223); (iv) six contiguous repeats of the amino acid sequence NANP (SEQ ID NO: 230); and (v) three contiguous repeats of the amino acid sequence NANPNVDP (SEQ ID NO: 223). In some embodiments, a second polypeptide further comprises: (i) one or more Plasmodium CSP N-terminal regions or portions thereof; (ii) one or more Plasmodium CSP N-terminal end regions or portions thereof; (iii) one or more Plasmodium CSP junction regions, portions thereof, or variants thereof; (iv) one or more Plasmodium CSP C-terminal regions or portions thereof; or (v) a combination thereof. [0129] In some embodiments, one or more Plasmodium CSP polypeptide regions or portions thereof comprised in a second polypeptide comprise in N-terminus to C-terminus order: (i) a Plasmodium CSP N-terminal end region or portion thereof; (ii) a Plasmodium CSP R1 region or portion thereof; (iii) a Plasmodium CSP junction region or portion thereof; (iv) three contiguous repeats of the amino acid sequence NANPNVDP (SEQ ID NO: 223); (v) six contiguous repeats of the amino acid sequence NANP (SEQ ID NO: 230); (vi) three contiguous repeats of the amino acid sequence NANPNVDP (SEQ ID NO: 223); (vii) six contiguous repeats of the amino acid sequence NANP (SEQ ID NO: 230); (viii) three contiguous repeats of the amino acid sequence NANPNVDP (SEQ ID NO: 223); and (ix) a Plasmodium CSP C-terminal region or portion thereof. [0130] In some embodiments, a second polypeptide further comprises a Plasmodium CSP GPI domain. In some embodiments, a Plasmodium CSP C-terminal region or portion thereof comprised in the second polypeptide comprises a substitution at a fucosylation site. [0131] In some embodiments, one or more Plasmodium CSP polypeptide regions or portions thereof comprised in the second polypeptide comprise in N-terminus to C-terminus order three repeating domains. In some embodiments, one or more Plasmodium CSP polypeptide regions or portions thereof comprised in the second polypeptide comprise in N-terminus to C-terminus order three repeating domains, wherein each repeating domain comprises one or more Plasmodium CSP junction regions, portions thereof, or variants thereof. In some embodiments, one or more Plasmodium CSP polypeptide regions or portions thereof comprised in the second polypeptide comprise in N-terminus to C-terminus order three repeating domains, wherein each repeating domain comprises three contiguous repeats of the amino acid sequence NANPNVDP (SEQ ID NO: 223). In some embodiments, one or more Plasmodium CSP polypeptide regions or portions thereof comprised in the second polypeptide comprise in N-terminus to C-terminus order three repeating domains, wherein each repeating domain comprises six contiguous repeats of the amino acid sequence NANP (SEQ ID NO: 230). In some embodiments, one or more Plasmodium CSP polypeptide regions or portions thereof comprised in the second polypeptide comprise in N- terminus to C-terminus order three repeating domains, wherein each repeating domain comprises: (i) one or more Plasmodium CSP junction regions, portions thereof, or variants thereof; (ii) three contiguous repeats of the amino acid sequence NANPNVDP (SEQ ID NO: 223); and (iii) six contiguous repeats of the amino acid sequence NANP (SEQ ID NO: 230). [0132] In some embodiments, one or more Plasmodium CSP polypeptide regions or portions thereof comprised in the second polypeptide comprise in N-terminus to C-terminus order three repeating domains, wherein each repeating domain comprises one or more Plasmodium R1 regions or portions thereof. In some embodiments, one or more Plasmodium CSP polypeptide regions or portions thereof comprised in the second polypeptide comprise in N- terminus to C-terminus order three repeating domains, wherein each repeating domain comprises one or more Plasmodium CSP junction regions, portions thereof, or variants thereof. In some embodiments, one or more Plasmodium CSP polypeptide regions or portions thereof comprised in the second polypeptide comprise in N-terminus to C-terminus order three repeating domains, wherein each repeating domain comprises three contiguous repeats of the amino acid sequence NANPNVDP (SEQ ID NO: 223). In some embodiments, one or more Plasmodium CSP polypeptide regions or portions thereof comprised in the second polypeptide comprise in N-terminus to C-terminus order three repeating domains, wherein each repeating domain comprises six contiguous repeats of the amino acid sequence NANP (SEQ ID NO: 230). In some embodiments, one or more Plasmodium CSP polypeptide regions or portions thereof comprised in the second polypeptide comprise in N-terminus to C-terminus order three repeating domains, wherein each repeating domain comprises: (i) one or more Plasmodium R1 regions or portions thereof; (ii) one or more Plasmodium CSP junction regions, portions thereof, or variants thereof; (iii) three contiguous repeats of the amino acid sequence NANPNVDP (SEQ ID NO: 223); and (iv) six contiguous repeats of the amino acid sequence NANP (SEQ ID NO: 230). [0133] In some embodiments, a combination further comprises one or more linker sequences. In some embodiments, a linker is a glycine-serine linker. In some embodiments, a second polypeptide comprises a linker sequence following each six contiguous repeats of the amino acid sequence NANP. [0134] In some embodiments, a second polypeptide comprises: (i) a secretory signal; (ii) a Plasmodium CSP N- terminal region; (iii) a Plasmodium CSP N-terminal end region; (iv) a Plasmodium CSP junctional region; (v) a Plasmodium CSP minor repeat region; (vi) an antigenic portion of a Plasmodium CSP major repeat region; and (vii) a Plasmodium CSP C-terminal region. In some embodiments, an antigenic portion of a Plasmodium CSP major repeat region comprises or consists of eighteen repeats of the amino acid sequence of NANP. In some embodiments, a second polypeptide comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the amino acid sequence according to SEQ ID NO: 117. In some embodiments, an antigenic portion of a Plasmodium CSP major repeat region comprises of six repeats of the amino acid sequence of NANP (SEQ ID NO: 230). In some embodiments, an antigenic portion of a Plasmodium CSP major repeat region further comprises an asparagine-alanine positioned immediately following the six repeats of the amino acid sequence of NANP (SEQ ID NO: 230). In some embodiments, a second polypeptide comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the amino acid sequence according to SEQ ID NO: 122. [0135] In some embodiments, a second polypeptide comprises: (i) a secretory signal; (ii) a Plasmodium CSP N- terminal region; (iii) a Plasmodium CSP N-terminal end region; (iv) a Plasmodium CSP junctional region; (v) a Plasmodium CSP minor repeat region; (vi) an antigenic portion of a Plasmodium CSP major repeat region; (vii) a Plasmodium CSP C-terminal region; and (viii) a transmembrane region. In some embodiments, an antigenic portion of a Plasmodium CSP major repeat region comprises or consists of eighteen repeats of the amino acid sequence of NANP (SEQ ID NO: 230). In some embodiments, a second polypeptide comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the amino acid sequence according to SEQ ID NO: 112. [0136] In some embodiments, a second polypeptide comprises: (i) a secretory signal; (ii) a Plasmodium CSP N- terminal region; (iii) a Plasmodium CSP N-terminal end region; (iv) a linker; (v) a Plasmodium CSP junctional region; (vi) a Plasmodium CSP minor repeat region; (vii) an antigenic portion of a Plasmodium CSP major repeat region; (viii) a Plasmodium CSP C-terminal region; (ix) a linker; and (x) a transmembrane region. In some embodiments, an antigenic portion of a Plasmodium CSP major repeat region comprises or consists of eighteen repeats of the amino acid sequence of NANP. In some embodiments, a second polypeptide comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the amino acid sequence according to SEQ ID NO: 125. [0137] In some embodiments, a second polypeptide comprises: (i) a secretory signal; (ii) a Plasmodium CSP N- terminal region; (iii) a Plasmodium CSP N-terminal end region; (iv) a Plasmodium CSP junctional region; (v) a Plasmodium CSP minor repeat region; (vi) a Plasmodium CSP major repeat region; (vii) a linker; and (viii) a transmembrane region. In some embodiments, a second polypeptide comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the amino acid sequence according to SEQ ID NO: 130. [0138] In some embodiments, a second polypeptide comprises: (i) a secretory signal; (ii) a Plasmodium CSP junctional region; (iii) a Plasmodium CSP minor repeat region; (iv) an antigenic portion of a Plasmodium CSP major repeat region; (v) a linker; (vi) an antigenic portion of a Plasmodium CSP C-terminal region; (vii) a serine-valine; (viii) a linker; and (ix) a multimerization region. In some embodiments, an antigenic portion of a Plasmodium CSP major repeat region comprises of six repeats of the amino acid sequence of NANP. In some embodiments, an antigenic portion of a Plasmodium CSP major repeat region further comprises an asparagine-alanine positioned immediately following the six repeats of the amino acid sequence of NANP (SEQ ID NO: 230). In some embodiments, an antigenic portion of a Plasmodium CSP C-terminal region comprises or consists of an amino acid sequence that is at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identical to the amino acid sequence of SEQ ID NO: 259. In some embodiments, a second polypeptide comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the amino acid sequence according to SEQ ID NO: 135. [0139] In some embodiments, a second polypeptide comprises: (i) a secretory signal; (ii) a Plasmodium CSP junctional region; (iii) a Plasmodium CSP minor repeat region; (iv) an antigenic portion of a Plasmodium CSP major repeat region; (v) a linker; (vi) an antigenic portion of a Plasmodium CSP C-terminal region; (vii) a serine-valine; (viii) a linker; and (ix) a self-aggregation region. In some embodiments, an antigenic portion of a Plasmodium CSP major repeat region comprises of six repeats of the amino acid sequence of NANP (SEQ ID NO: 230). In some embodiments, an antigenic portion of a Plasmodium CSP major repeat region further comprises an asparagine- alanine positioned immediately following the six repeats of the amino acid sequence of NANP (SEQ ID NO: 230). In some embodiments, an antigenic portion of a Plasmodium CSP C-terminal region comprises or consists of an amino acid sequence that is at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%, at least 90%, at least 95%, at least 98%, or 100% identical to the amino acid sequence of SEQ ID NO: 259. In some embodiments, a second polypeptide comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the amino acid sequence according to SEQ ID NO: 138. [0140] In some embodiments, a second polypeptide comprises: (i) a secretory signal; (ii) a Plasmodium CSP junctional region; (iii) a Plasmodium CSP minor repeat region; (iv) an antigenic portion of a Plasmodium CSP major repeat region; (v) a linker; (vi) an antigenic portion of a Plasmodium CSP C-terminal region; (vii) a serine-valine; (viii) a linker; and (ix) a transmembrane region. In some embodiments, an antigenic portion of a Plasmodium CSP major repeat region comprises of six repeats of the amino acid sequence of NANP (SEQ ID NO: 230). In some embodiments, an antigenic portion of a Plasmodium CSP major repeat region further comprises an asparagine- alanine positioned immediately following the six repeats of the amino acid sequence of NANP (SEQ ID NO: 230). In some embodiments, an antigenic portion of a Plasmodium CSP C-terminal region comprises or consists of an amino acid sequence that is at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%, at least 90%, at least 95%, at least 98%, or 100% identical to the amino acid sequence of SEQ ID NO: 259. In some embodiments, a second polypeptide comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the amino acid sequence according to SEQ ID NO: 141. [0141] In some embodiments, a second polypeptide comprises: (i) a secretory signal; (ii) a Plasmodium CSP N- terminal region; (iii) a Plasmodium CSP N-terminal end region; (iv) a Plasmodium CSP junctional region; (v) a Plasmodium CSP minor repeat region; (vi) a Plasmodium CSP major repeat region; (vii) a Plasmodium CSP C-terminal region variant; and (viii) a transmembrane region. In some embodiments, a secretory signal comprises or consists of a Plasmodium secretory signal. In some embodiments, a Plasmodium secretory signal comprises or consists of a Plasmodium CSP secretory signal. In some embodiments, a Plasmodium CSP secretory signal comprises or consists of an amino acid sequence according to SEQ ID NO: 332. In some embodiments, a transmembrane region comprises or consists of a Plasmodium transmembrane region. In some embodiments, a Plasmodium transmembrane region comprises or consists of a Plasmodium CSP glycosylphosphatidylinositol (GPI) anchor region. In some embodiments, a Plasmodium CSP GPI anchor region comprises or consists of an amino acid sequence according to SEQ ID NO: 385. In some embodiments, a polypeptide comprises or consists of an amino acid sequence with at least 85% sequence identity to the amino acid sequence according to SEQ ID NO: 989. In some embodiments, a polypeptide comprises or consists of an amino acid sequence according to SEQ ID NO: 989. In some embodiments, a polyribonucleotide comprises or consists of a nucleic acid sequence with at least 85% sequence identity to the nucleic acid sequence according to SEQ ID NO: 991. In some embodiments, a polyribonucleotide comprises or consists of a nucleic acid sequence according to SEQ ID NO: 991. [0142] In some embodiments, a second polypeptide comprises: (i) a secretory signal; (ii) an antigenic portion of a Plasmodium CSP N-terminal region; (iii) a first linker; (iv) a Plasmodium CSP N-terminal end region; (v) a Plasmodium CSP junctional region; (vi) a Plasmodium CSP minor repeat region; (vii) an antigenic portion of a Plasmodium CSP major repeat region; (viii) a Plasmodium CSP C-terminal region; (ix) a serine-valine sequence; (x) a second linker; and (xi) a transmembrane region. In some embodiments, a secretory signal comprises or consists of a Plasmodium secretory signal. In some embodiments, a Plasmodium secretory signal comprises or consists of a Plasmodium CSP secretory signal. In some embodiments, a Plasmodium CSP secretory signal comprises or consists of an amino acid sequence according to SEQ ID NO: 332. In some embodiments, a transmembrane region comprises or consists of an HSV transmembrane region. In some embodiments, a HSV transmembrane region comprises or consists of an HSV-1 or HSV-2 transmembrane region. In some embodiments, a HSV transmembrane region comprises or consists of an HSV gD transmembrane region. In some embodiments, a HSV gD transmembrane region comprises or consists of an amino acid sequence according to SEQ ID NO: 379. In some embodiments, an antigenic portion of a Plasmodium CSP N-terminal region comprises or consists of an amino acid sequence that is at least 85%, at least 90%, at least 95%, at least 98%, or 100% identical to the amino acid sequence of according to SEQ ID NO: 1010. In some embodiments, an antigenic portion of a Plasmodium CSP major repeat region comprises or consists of eighteen repeats of the amino acid sequence of NANP. In some embodiments, a polypeptide comprises or consists of an amino acid sequence with at least 85% sequence identity to the amino acid sequence according to SEQ ID NO: 997. In some embodiments, a polypeptide comprises or consists of an amino acid sequence according to SEQ ID NO: 997. In some embodiments, a polyribonucleotide comprises or consists of a nucleic acid sequence with at least 85% sequence identity to the nucleic acid sequence according to SEQ ID NO: 999. In some embodiments, a polyribonucleotide comprises or consists of a nucleic acid sequence according to SEQ ID NO: 999. [0143] In some embodiments, second polypeptide comprises: (i) a secretory signal; (ii) an antigenic portion of a Plasmodium CSP N-terminal region; (iii) a first linker; (iv) a Plasmodium CSP N-terminal end region; (v) a Plasmodium CSP junctional region; (vi) a Plasmodium CSP minor repeat region; (vii) an antigenic portion of a Plasmodium CSP major repeat region; (viii) a second linker; (ix) an antigenic portion of a Plasmodium CSP C-terminal region; (x) a serine-valine sequence; (xi) a third linker; and (xii) a transmembrane region. In some embodiments, a secretory signal comprises or consists of a Plasmodium secretory signal. In some embodiments, a Plasmodium secretory signal comprises or consists of a Plasmodium CSP secretory signal. In some embodiments, a Plasmodium CSP secretory signal comprises or consists of an amino acid sequence according to SEQ ID NO: 332. In some embodiments, a transmembrane region comprises or consists of an HSV transmembrane region. In some embodiments, a HSV transmembrane region comprises or consists of an HSV-1 or HSV-2 transmembrane region. In some embodiments, a HSV transmembrane region comprises or consists of an HSV gD transmembrane region. In some embodiments, a HSV gD transmembrane region comprises or consists of an amino acid sequence according to SEQ ID NO: 379. In some embodiments, an antigenic portion of a Plasmodium CSP N-terminal region comprises or consists of an amino acid sequence that is at least 85%, at least 90%, at least 95%, at least 98%, or 100% identical to the amino acid sequence of according to SEQ ID NO: 1010. In some embodiments, an antigenic portion of a Plasmodium CSP C-terminal region comprises or consists of an amino acid sequence that is at least 85%, at least 90%, at least 95%, at least 98%, or 100% identical to the amino acid sequence of SEQ ID NO: 259. In some embodiments, an antigenic portion of a Plasmodium CSP major repeat region comprises or consists of eighteen repeats of the amino acid sequence of NANP. In some embodiments, a polypeptide comprises or consists of an amino acid sequence with at least 85% sequence identity to the amino acid sequence according to SEQ ID NO: 1000. In some embodiments, a polypeptide comprises or consists of an amino acid sequence according to SEQ ID NO: 1000. In some embodiments, a polyribonucleotide comprises or consists of a nucleic acid sequence with at least 85% sequence identity to the nucleic acid sequence according to SEQ ID NO: 1002. In some embodiments, a polyribonucleotide comprises or consists of a nucleic acid sequence according to SEQ ID NO: 1002. In some embodiments, an antigenic portion of a Plasmodium CSP major repeat region comprises six repeats of the amino acid sequence of NANP. In some embodiments, an antigenic portion of a Plasmodium CSP major repeat region further comprises an asparagine-alanine positioned immediately following the six repeats of the amino acid sequence of NANP. In some embodiments, a polypeptide comprises or consists of an amino acid sequence with at least 85% sequence identity to the amino acid sequence according to SEQ ID NO: 1003. In some embodiments, a polypeptide comprises or consists of an amino acid sequence according to SEQ ID NO: 1003. In some embodiments, a polyribonucleotide comprises or consists of a nucleic acid sequence with at least 85% sequence identity to the nucleic acid sequence according to SEQ ID NO: 1005. In some embodiments, a polyribonucleotide comprises or consists of a nucleic acid sequence according to SEQ ID NO: 1005. In some embodiments, when present, the features are in a second polypeptide in numerical order from the C-terminus to the N-terminus. [0144] In some embodiments, a combination comprises a first polypeptide that comprises: (i) an antigenic Plasmodium CSP polypeptide fragment; (ii) an antigenic Plasmodium TRAP polypeptide fragment; (iii) an antigenic Plasmodium UIS3 polypeptide fragment; (iv) an antigenic Plasmodium ETRAMP10.3 polypeptide fragment; and (v) an antigenic Plasmodium LSAP2 polypeptide fragment. In some embodiments, a combination comprises a second polypeptide that comprises: (i) a secretory signal; (ii) a Plasmodium CSP N-terminal region; (iii) a Plasmodium CSP N- terminal end region; (iv) a Plasmodium CSP junction region; (v) three repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223); (vi) a Plasmodium CSP major repeat region; (vii) a Plasmodium CSP C-terminal region; and (viii) a transmembrane region. In some embodiments, a combination comprises a first polypeptide that comprises: (i) an antigenic Plasmodium CSP polypeptide fragment; (ii) an antigenic Plasmodium TRAP polypeptide fragment; (iii) an antigenic Plasmodium UIS3 polypeptide fragment; (iv) an antigenic Plasmodium ETRAMP10.3 polypeptide fragment; and (v) an antigenic Plasmodium LSAP2 polypeptide fragment, and a second polypeptide that comprises: (i) a secretory signal; (ii) a Plasmodium CSP N-terminal region; (iii) a Plasmodium CSP N-terminal end region; (iv) a Plasmodium CSP junction region; (v) three repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223); (vi) a Plasmodium CSP major repeat region; (vii) a Plasmodium CSP C-terminal region; and (viii) a transmembrane region. [0145] In some embodiments, a first polypeptide comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 203. [0146] In some embodiments, a second polypeptide comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 33. [0147] In some embodiments, a combination further comprises a third pharmaceutical composition comprising a third polyribonucleotide, wherein the third polyribonucleotide encodes a third polypeptide, and the third polypeptide comprises: (i) an antigenic Plasmodium LSA-1(a) polypeptide fragment; (ii) an antigenic Plasmodium LSA-1(b) polypeptide fragment; (iii) an antigenic Plasmodium LISP-2 polypeptide fragment; and (iv) an antigenic Plasmodium LISP-1 polypeptide fragment. [0148] In some embodiments, a third polypeptide comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 209. [0149] In some embodiments, a combination comprises a first polypeptide that comprises: (i) an antigenic Plasmodium CSP polypeptide fragment; (ii) an antigenic Plasmodium TRAP polypeptide fragment; (iii) an antigenic Plasmodium UIS3 polypeptide fragment; (iv) an antigenic Plasmodium ETRAMP10.3 polypeptide fragment; and (v) an antigenic Plasmodium LSAP2 polypeptide fragment. In some embodiments, a combination comprises a second polypeptide that comprises: (i) a secretory signal; (ii) a Plasmodium CSP N-terminal end region; (iii) a Plasmodium CSP junction region; (iv) nine repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223); (v) a Plasmodium CSP C-terminal region; (vi) a serine-valine sequence immediately following the Plasmodium CSP C- terminal region; (vii) a linker; and (viii) a transmembrane region, and a second polypeptide does not comprise any of: (a) a Plasmodium CSP N-terminal region or portion thereof; and (b) an amino acid sequence of NPNA (SEQ ID NO: 228). In some embodiments, a combination comprises a first polypeptide that comprises: (i) an antigenic Plasmodium CSP polypeptide fragment; (ii) an antigenic Plasmodium TRAP polypeptide fragment; (iii) an antigenic Plasmodium UIS3 polypeptide fragment; (iv) an antigenic Plasmodium ETRAMP10.3 polypeptide fragment; and (v) an antigenic Plasmodium LSAP2 polypeptide fragment, and a second polypeptide that comprises: (i) a secretory signal; (ii) a Plasmodium CSP N-terminal end region; (iii) a Plasmodium CSP junction region; (iv) nine repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223); (v) a Plasmodium CSP C-terminal region; (vi) a serine-valine sequence immediately following the Plasmodium CSP C-terminal region; (vii) a linker; and (viii) a transmembrane region, and a second polypeptide does not comprise any of: (a) a Plasmodium CSP N-terminal region or portion thereof; and (b) an amino acid sequence of NPNA (SEQ ID NO: 228). [0150] In some embodiments, a first polypeptide comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 203. [0151] In some embodiments, a second polypeptide comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 81. [0152] In some embodiments, a combination comprises a first polypeptide that comprises: (i) an antigenic Plasmodium LSA-1(a) polypeptide fragment; (ii) an antigenic Plasmodium LSA-1(b) polypeptide fragment; (iii) an antigenic Plasmodium LISP-2 polypeptide fragment; and (iv) an antigenic Plasmodium LISP-1 polypeptide fragment. In some embodiments, a combination comprises a second polypeptide that comprises: (i) a secretory signal; (ii) a Plasmodium CSP N-terminal region; (iii) a Plasmodium CSP N-terminal end region; (iv) a Plasmodium CSP junction region; (v) three repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223); (vi) a Plasmodium CSP major repeat region; (vii) a Plasmodium CSP C-terminal region; and (viii) a transmembrane region. In some embodiments, a combination comprises a first polypeptide that comprises: (i) an antigenic Plasmodium LSA-1(a) polypeptide fragment; (ii) an antigenic Plasmodium LSA-1(b) polypeptide fragment; (iii) an antigenic Plasmodium LISP-2 polypeptide fragment; and (iv) an antigenic Plasmodium LISP-1 polypeptide fragment, and a second polypeptide that comprises: (i) a secretory signal; (ii) a Plasmodium CSP N-terminal region; (iii) a Plasmodium CSP N-terminal end region; (iv) a Plasmodium CSP junction region; (v) three repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223); (vi) a Plasmodium CSP major repeat region; (vii) a Plasmodium CSP C-terminal region; and (viii) a transmembrane region. [0153] In some embodiments, a first polypeptide comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 209. [0154] In some embodiments, a second polypeptide comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 33. [0155] In some embodiments, a combination comprises a first polypeptide that comprises: (i) an antigenic Plasmodium LSA-1(a) polypeptide fragment; (ii) an antigenic Plasmodium LSA-1(b) polypeptide fragment; (iii) an antigenic Plasmodium LISP-2 polypeptide fragment; and (iv) an antigenic Plasmodium LISP-1 polypeptide fragment. In some embodiments, a combination comprises a second polypeptide that comprises: (i) a secretory signal; (ii) a Plasmodium CSP N-terminal end region; (iii) a Plasmodium CSP junction region; (iv) nine repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223); (v) a Plasmodium CSP C-terminal region; (vi) a serine-valine sequence immediately following the Plasmodium CSP C-terminal region; (vii) a linker; and (viii) a transmembrane region, and a second polypeptide does not comprise any of: (a) a Plasmodium CSP N-terminal region or portion thereof; and (b) an amino acid sequence of NPNA (SEQ ID NO: 228). In some embodiments, a combination comprises a first polypeptide that comprises: (i) an antigenic Plasmodium LSA-1(a) polypeptide fragment; (ii) an antigenic Plasmodium LSA-1(b) polypeptide fragment; (iii) an antigenic Plasmodium LISP-2 polypeptide fragment; and (iv) an antigenic Plasmodium LISP-1 polypeptide fragment, and a second polypeptide that comprises: (i) a secretory signal; (ii) a Plasmodium CSP N-terminal end region; (iii) a Plasmodium CSP junction region; (iv) nine repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223); (v) a Plasmodium CSP C-terminal region; (vi) a serine-valine sequence immediately following the Plasmodium CSP C-terminal region; (vii) a linker; and (viii) a transmembrane region, and a second polypeptide does not comprise any of: (a) a Plasmodium CSP N-terminal region or portion thereof; and (b) an amino acid sequence of NPNA (SEQ ID NO: 228). [0156] In some embodiments, a first polypeptide comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 209. [0157] In some embodiments, a second polypeptide comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 81. [0158] In some embodiments, Plasmodium is Plasmodium falciparum. In some embodiments, one or more Plasmodium CSP polypeptide regions or portions thereof are one or more P. falciparum CSP polypeptide regions or portions thereof. [0159] In some embodiments, one or more Plasmodium T-cell antigens are one or more P. falciparum T-cell antigens. In some embodiments, Plasmodium falciparum is Plasmodium falciparum isolate 3D7. [0160] In some embodiments, a first polyribonucleotide and/or second polyribonucleotide is an isolated polyribonucleotide. In some embodiments, a third polyribonucleotide is an isolated polyribonucleotide. In some embodiments, a first polyribonucleotide and/or second polyribonucleotide is an engineered polyribonucleotide. In some embodiments, a third polyribonucleotide is an engineered polyribonucleotide. [0161] In some embodiments, a first polyribonucleotide and/or second polyribonucleotide is a codon-optimized polyribonucleotide. In some embodiments, a third polyribonucleotide is a codon-optimized polyribonucleotide. [0162] The present disclosure further provides RNA constructs. In some embodiments, a first polyribonucleotide is comprised in a first RNA construct, wherein the first RNA construct comprises in 5' to 3' order: (i) a 5' UTR; (ii) the first polyribonucleotide; (iii) a 3' UTR; and (iv) a polyA tail sequence. In some embodiments, second polyribonucleotide is comprised in a second RNA construct, wherein the second RNA construct comprises in 5' to 3' order: (i) a 5' UTR; (ii) the second polyribonucleotide; (iii) a 3' UTR; and (iv) a polyA tail sequence. [0163] In some embodiments, a 5' UTR of a first and/or second RNA construct comprises or consists of a modified human alpha-globin 5'-UTR. In some embodiments, a 5' UTR of a first and/or second RNA construct consists of a ribonucleic acid sequence according to SEQ ID NO: 565. [0164] In some embodiments, a 3' UTR of a first and/or second RNA construct comprises or consists of a first sequence from the amino terminal enhancer of split (AES) messenger RNA and a second sequence from the mitochondrial encoded 12S ribosomal RNA. In some embodiments, a 3' UTR of a first and/or second RNA construct consists of a ribonucleic acid sequence according to SEQ ID NO: 567. [0165] In some embodiments, a 5' UTR of a first and/or second RNA construct comprises or consists of a modified human alpha-globin 5'-UTR and a 3' UTR of a first and/or second RNA construct comprises or consists of a first sequence from the amino terminal enhancer of split (AES) messenger RNA and a second sequence from the mitochondrial encoded 12S ribosomal RNA. [0166] In some embodiments, a polyA tail sequence of a first and/or second RNA construct is a split polyA tail sequence. In some embodiments, a split polyA tail sequence consists of a ribonucleic acid sequence according to SEQ ID NO: 569. [0167] In some embodiments, a first and/or second RNA construct further comprise a 5' cap. In some embodiments, a first and/or second RNA construct comprise a cap proximal sequence comprising positions +1, +2, +3, +4, and +5 of the polyribonucleotide. In some embodiments, a 5' cap comprises or consists of m7(3’OMeG)(5')ppp(5')(2'OMeA1)pG2, wherein A1 is position +1 of the polyribonucleotide, and G2 is position +2 of the polyribonucleotide. In some embodiments, a cap proximal sequence comprises A₁ and G₂ of the Cap1 structure, and a sequence comprising: A₃A₄U₅ (SEQ ID NO: 571) at positions +3, +4 and +5 respectively of the polyribonucleotide. [0168] In some embodiments, a first and/or second RNA construct includes modified uridines in place of all uridines. In some embodiments, modified uridines are each N1-methyl-pseudouridine. [0169] The present disclosure further provides pharmaceutical compositions, including pharmaceutical compositions for use in combinations described herein. In some embodiments, a first and/or second pharmaceutical composition further comprises lipid nanoparticles, polyplexes (PLX), lipidated polyplexes (LPLX), or liposomes. In some embodiments, a first and/or second polyribonucleotide is fully or partially encapsulated within the lipid nanoparticles, polyplexes (PLX), lipidated polyplexes (LPLX), or liposomes. [0170] In some embodiments, a first and/or second pharmaceutical composition further comprises lipid nanoparticles. In some embodiments, a first polyribonucleotide is encapsulated within the lipid nanoparticles. In some embodiments, a second polyribonucleotide is encapsulated within the lipid nanoparticles. [0171] In some embodiments, a first and/or second pharmaceutical composition comprises at least one pharmaceutically acceptable excipient. [0172] In some embodiments, a combination is for use in the treatment of a malaria infection. In some embodiments, a combination is for use in the prevention of a malaria infection. [0173] The present disclosure also provides methods. methods. In some embodiments, a method comprises administering a combination described herein to a subject. In some embodiments, a method described herein is a method of treating a malaria infection. In some embodiments, a method described herein is a method of preventing a malaria infection. [0174] In some embodiments, a subject has or is at risk of developing a malaria infection. In some embodiments, a subject is a human. [0175] In some embodiments, administration induces an anti-malaria immune response in a subject. [0176] Provided herein are also uses. In some embodiments, use of a combination as described herein can be for treatment of a malaria infection. In some embodiments, use of a combination as described herein can be for prevention of a malaria injection. BRIEF DESCRIPTION OF THE DRAWING [0177] FIG.1 presents an overview of the Plasmodium life cycle. [0178] FIGS.2A-2B show antigenic fragments of malarial proteins. Specifically, FIG.2A depicts epitopes observed from MAS1 and MAS2 strings mapped onto MAS3a and MAS4f. FIG.2B shows antigenic fragments of malarial protein LSA-3. [0179] FIG.3 presents a schematic representation of exemplary malarial T cell peptide string constructs containing antigens, as described herein. [0180] FIG.4 depicts transfection of a combination including MAS3a and MAS4f into cells to generate detectable protein product. Relative protein expression 24 h after co-transfecting 2.5 μg each drug product into HEK293T cell lines are shown. [0181] FIGS.5A-5F depict activation of T-cells, as assessed by secretion of IFN-γ. FIGS.5A-5D show an assessment of IFN-γ secretion using isolated splenocytes (from mice immunized with different T cell peptide string constructs) incubated with construct specific antigen peptide pools (15mers, 11aa overlap across antigen). FIG.5E depicts a comparison of isolated splenocytes (from mice in group 2 and 3, and splenocytes isolated from mice in group 4) response to specific antigen peptide pools. FIG.5F depicts a comparison of isolated splenocytes (from mice in group 2 and splenocytes isolated from mice in group 1) response to specific antigen peptide pools. [0182] FIGS.6A-6H depict activation of T-cells, as assessed by secretion of IFN-γ. FIGS.6A-6H show an assessment of IFN-γ secretion using isolated splenocytes (from mice immunized with different T cell peptide string constructs) incubated with construct specific antigen peptide pools (15mers, 11aa overlap across antigen). [0183] FIGS.7A-7B depict assessment of activation of T-cells, as assessed by secretion of IFN-γ using isolated splenocytes (from mice immunized with T cell peptide string constructs individually or with T cell strings constructs in combination). [0184] FIGS.8A-8B depict assessment of activation of T-cells, as assessed by secretion of IFN-γ using isolated splenocytes (from mice immunized with shorter T cell peptide string constructs or a longer T cell peptide string with the same antigenic content). [0185] FIGS.9A-9B depict in vitro expression of non-formulated RNA constructs encoding different malarial polypeptide constructs in HEK293T cells. FIG.9A shows transfection rate as measured by percentage of total HEK293T population that is positive for presence of expressed protein. FIG.9B shows total expression as measured by median fluorescence intensity of the total HEK293T population for both transfected and non-transfected cells. Permeabilized cells show total protein expressed (black bar, intracellular staining) and non-permeabilized cells show only surface expressed protein (grey bar, surface staining). Each sample was stained in triplicate, bar is a representation of mean with SD; NT, non-transfected. [0186] FIGS.10A-10C depict in vitro expression of formulated RNA constructs in HEK293T cells. FIG.10A shows transfection rate as measured by percentage of total HEK293T population that is positive for presence of expressed protein. FIG.10B shows total expression as measured by median fluorescence intensity of the total HEK293T population for both transfected and non-transfected cells. Permeabilized cells show total protein expressed (black bar, intracellular staining) and non-permeabilized cells show only surface expressed protein (grey bar, surface staining). Each sample was stained in triplicate, bar is a representation of mean with SD. FIG.10C shows amount of protein detected in culture supernatant where each data point represents a triplicate repeat; NT, non-transfected. [0187] FIGS.11A-11B depict immunogenicity induced in mice by formulated RNA constructs. FIG.11A shows antibodies to Plasmodium falciparum (Pf) CSP full length protein (“PfCSP-FL”). FIG.11B shows antibodies to PfCSP C-terminal domain (“PfCSP-C term”). Each data point is representative of one mouse and the bar denotes mean with SEM. LDL, lower detection limit. [0188] FIGS.12A-12B depict binding of antibodies generated from mice immunized with formulated RNA constructs to various epitopes. FIG.12A shows a visual summary of the data in form of a heatmap. FIG.12B shows bars that are representative of the area under the curve (AUC) created when plotting dilution steps versus ECL signal. [0189] FIGS.13A-13B depict binding specificity of antibodies generated from mice immunized with formulated RNA constructs to CSP protein in Plasmodium falciparum sporozoite lysates. FIG.13A shows binding between antibodies and CSP protein in the sporozoite (spz) lysates, represented as area under the curve (AUC), as assessed by luminescence. FIG.13B shows binding of murine anti-Pfs25 mAb32F81 used as negative control and murine anti-CSP mAb3SP2 used as a positive control. [0190] FIGS.14A-14B depict assessment of antibodies generated from mice immunized with formulated RNA constructs for ability to inhibit P. falciparum sporozoite traversal. FIG.14A shows results as the dilution at which the % of traversal is reduced by 50% (mean with SEM). FIG.14B shows the percentage of traversed cells for the negative control (serum from vehicle mice) and the percentage of inhibition of traversal for the positive control (mAb317, an antibody that binds to NANP (SEQ ID NO: 230) repeats of the major repeat region and is known to inhibit traversal), with 002, 003, 005, 012, 014, and 018 indicating different experimental runs. [0191] FIGS.15A-15B depict assessment of antibodies generated from mice immunized with formulated RNA constructs for ability to inhibit P. falciparum sporozoite infection of primary human hepatocytes. FIG.15A shows results as percentage of inhibition of infection activity (mean with SEM) in comparison to the average of the vehicle control, which was set as 0% inhibition for three different dilutions of the immune serum. FIG.15B shows the percentage of infected cells from negative control (serum from vehicle mice) and the percentage of inhibition of the positive control (mAb317, an antibody known to inhibit hepatocyte infection). [0192] FIG.16 depicts activation of T-cells, as assessed by secretion of IFN-γ. IFN-γ secretion was assessed using isolated splenocytes (from mice immunized with formulated RNA constructs) treated with overlapping peptide pools covering the full length CSP protein (PfCSP_FL_pep), peptides of epitopes predicted to be presented on MHC-I, on MHC-II, or controls (e.g., negative control: gp70-AH1 (SPSYVYHQF [SEQ ID NO: 595]), 4 μg/mL; positive control: concanavalin A, 2 μg/mL). Samples were measured in triplicate and negative control was measured in duplicate; each data point represents a single mouse and bars represent the group mean spot-forming units (SFU) ± SD per 5x10⁵ splenocytes; ve, vehicle. [0193] FIG.17 depicts activation of T-cells, as assessed by secretion of TNF-α. TNF-α secretion was assessed using isolated splenocytes (from mice immunized formulated RNA constructs) treated with overlapping peptide pools covering the full length CSP protein (PfCSP_FL_pep), peptides of epitopes predicted to be presented on MHC-I, on MHC-II, or controls (e.g., negative control: gp70-AH1 (SPSYVYHQF [SEQ ID NO: 595]), 4 μg/mL; positive control: concanavalin A, 2 μg/mL). Samples were measured in triplicate and negative control was measured in duplicate; each data point represents a single mouse and bars represent the group mean spot-forming units (SFU) ± SD per 5x10⁵ splenocytes; ve, vehicle. [0194] FIG.18 depicts activation of T-cells, as assessed by secretion of IL-2. IL-2 secretion was assessed using isolated splenocytes (from mice immunized with formulated RNA constructs) treated with overlapping peptide pools covering the full length CSP protein (PfCSP_FL_pep), peptides of epitopes predicted to be presented on MHC-I, on MHC-II, or controls (e.g., negative control: gp70-AH1 (SPSYVYHQF [SEQ ID NO: 595]), 4 μg/mL; positive control: concanavalin A, 2 μg/mL). Samples were measured in triplicate and negative control was measured in duplicate; each data point represents a single mouse and bars represent the group mean spot-forming units (SFU) ± SD per 5x10⁵ splenocytes; ve, vehicle. [0195] FIG.19 depicts activation of T-cells, as assessed by secretion of IL-2 and IFN-γ. IL-2 and IFN-γ secretion was assessed using isolated splenocytes (from mice immunized with formulated RNA constructs) treated with overlapping peptide pools covering the full length CSP protein (PfCSP_FL_pep), peptides of epitopes predicted to be presented on MHC-I, on MHC-II, or controls (e.g., negative control: gp70-AH1 (SPSYVYHQF [SEQ ID NO: 595]), 4 μg/mL; positive control: concanavalin A, 2 μg/mL). Samples were measured in triplicate and negative control was measured in duplicate; each data point represents a single mouse and bars represent the group mean spot-forming units (SFU) ± SD per 5x10⁵ splenocytes; ve, vehicle. [0196] FIG.20 depicts activation of T-cells, as assessed by secretion of TNF-α and IFN-γ. TNF-α and IFN-γ secretion was assessed using isolated splenocytes (from mice immunized with formulated RNA constructs) treated with overlapping peptide pools covering the full length CSP protein (PfCSP_FL_pep), peptides of epitopes predicted to be presented on MHC-I, on MHC-II, or controls (e.g., negative control: gp70-AH1 (SPSYVYHQF [SEQ ID NO: 595]), 4 μg/mL; positive control: concanavalin A, 2 μg/mL). Samples were measured in triplicate and negative control was measured in duplicate; each data point represents a single mouse and bars represent the group mean spot-forming units (SFU) ± SD per 5x10⁵ splenocytes; ve, vehicle. [0197] FIG.21 depicts activation of T-cells, as assessed by secretion of TNF-α and IL-2. TNF-α and IL-2 secretion was assessed using splenocytes (isolated from mice immunized with formulated RNA constructs) treated with overlapping peptide pools covering the full length CSP protein (PfCSP_FL_pep), peptides of epitopes predicted to be presented on MHC-I, on MHC-II, or controls (e.g., negative control: gp70-AH1 (SPSYVYHQF [SEQ ID NO: 595]), 4 μg/mL; positive control: concanavalin A, 2 μg/mL). Samples were measured in triplicate and negative control was measured in duplicate; each data point represents a single mouse and bars represent the group mean spot-forming units (SFU) ± SD per 5x10⁵ splenocytes; ve, vehicle. [0198] FIG.22 depicts activation of T-cells, as assessed by secretion of TNF-α, IL-2 and IFN-γ. TNF-α, IL-2 and IFN-γ secretion was assessed using isolated splenocytes (from mice immunized with formulated RNA constructs) treated with overlapping peptide pools covering the full length CSP protein (PfCSP_FL_pep), peptides of epitopes predicted to be presented on MHC-I, on MHC-II, or controls (e.g., negative control: gp70-AH1 (SPSYVYHQF [SEQ ID NO: 595]), 4 μg/mL; positive control: concanavalin A, 2 μg/mL). Samples were measured in triplicate and negative control was measured in duplicate; each data point represents a single mouse and bars represent the group mean spot-forming units (SFU) ± SD per 5x10⁵ splenocytes; ve, vehicle. [0199] FIGS.23A-23C depict protection of mice immunized with formulated RNA constructs against a challenge with PfCSP-expressing P. berghei sporozoites as well as immunogenicity induced by this immunization. FIG.23A depicts percentage of protected mice up to 11 days after challenge with PfCSP-expressing P. berghei sporozoites, for mice immunized with formulated RNA constructs, vehicle, or positive control. Mice that received 100 μg of the 2A10 monoclonal antibody 24 h before the challenge were used as positive control (2A10, a monoclonal antibody that targets the major repeats). FIG.23B and FIG.23C depict endpoint titers against full length PfCSP two weeks after the boost (day 35, FIG.23B) and one day before the challenge (day 49, FIG.23C) for mice immunized with formulated RNA constructs and mice injected with the vehicle only. Mean ± SEM and individual animal values are shown. [0200] FIGS.24A-24B depict protection of mice immunized with formulated RNA constructs against a challenge with PfCSP-expressing P. berghei sporozoites as well as immunogenicity induced by this immunization from three separate experiments. FIG.24A depicts percentage of protected mice up to 11 days after challenge with PfCSP-expressing P. berghei sporozoites, for mice immunized with formulated RNA constructs, vehicle (saline), or positive control. Mice that received 100 μg of the 2A10 monoclonal antibody 24 h before the challenge were used as positive control in Experiment 1 and mice immunized with Mosquirix were used as positive control in Experiment 2 and 3. FIG.24B depicts endpoint titers against full length PfCSP two weeks after the boost (day 35) and one day before the challenge (day 49) for mice immunized with formulated RNA constructs and mice injected with the vehicle only. Mean ± SEM and individual animal values are shown. Mice immunized twice IM with 5 μg of Mosquirix were used as positive control in Experiments 2 and 3. Mice injected with the vehicle were used as negative controls in all experiments. [0201] FIGS.25A-25J depict assessment of antibodies generated from mice immunized with a formulated RNA construct for ability to recognize native PfCSP on sporozoites and inhibit sporozoite viability and motility. FIG. 25A shows log of anti-sporozoite endpoint titers using fixed PfCSP-expressing P. berghei sporozoites. Symbols represent the mean ± SEM using serum from individual mice. FIG.25B shows inhibition of sporozoite gliding speed. Circles represent the mean ± SEM of duplicates of pooled serum samples from each group. FIG.25C shows estimated length of the circumsporozoite precipitation reaction (CSPR) elicited by serum samples from immunized mice as measured by flow cytometry (Forward Scatter Width (FSC-W)). Symbols represent the mean ± SEM using serum from individual mice. FIG.25D shows cytotoxicity of serum samples from immunized mice against sporozoites in suspension (PBS). Symbols represent the mean ± SEM using serum from individual mice. FIG.25E shows cytotoxicity in 3D (Matrigel). Symbols represent the mean ± SEM using serum from individual mice. FIG.25F depicts 3 experiments and shows log of anti-sporozoite endpoint titers using fixed PfCSP-expressing P. berghei sporozoites. Bars represent the mean ± SEM using serum from individual mice. 2A10, positive antibody control; Mos, Mosquirix® positive control; IFA, Immunofluorescence assay. FIG.25G depicts assessment of antibodies generated from mice immunized with formulated RNA of 5 priority constructs for ability to inhibit sporozoite gliding motility. Each graph represents a different experiment and shows sporozoite gliding speed (μm/s). Bars represent the mean ± SEM of duplicates (in Experiment 1) or single replicates (Experiments 2 and 3) of pooled serum samples from each group. 2A10, positive antibody control; Mos, Mosquirix® positive control; Veh, vehicle. FIG.25H depicts assessment of antibodies generated from mice immunized with formulated RNA for ability to bind and crosslink native PfCSP on the sporozoite surface. Each graph represents a different experiment and shows the estimated length of the circumsporozoite Precipitation Reaction (CSPR) elicited by 17% immune sera as measured by flow cytometry (Forward Scatter Width (FSC-W)). Symbols represent the mean ± SEM using serum from individual mice. 2A10, positive antibody control; Mos, Mosquirix® positive control; Veh, vehicle. FIG.25I depicts the cytotoxicity of 17% immune sera measured against PfCSP-expressing P. berghei sporozoites in suspension and is presented as percentage of viable sporozoites. FIG.25J depicts cytotoxicity of 17% immune sera against PfCSP-expressing P. berghei sporozoites measured in a 3D Matrigel and normalized to vehicle group (viability = 100%). For FIGS.25F- 25J, each graph represents an independent challenge experiment (designated Experiment 1, Experiment 2 and Experiment 3). Bars represent the mean ± SEM using serum from individual mice. 2A10, positive antibody control; Mosquirix® positive control; Veh, vehicle; PBS, phosphate buffer saline. [0202] FIGS.26A- 26B depict in vitro expression of non-formulated RNA constructs encoding different malarial peptide constructs in HEK293T cells. FIG.26A shows transfection rate as measured by percentage of total HEK293T population that is positive for presence of expressed protein. FIG.26B shows total expression as measured by median fluorescence intensity of the total HEK293T population for both transfected and non-transfected cells. [0203] FIGS.27A-27B depict in vitro expression of formulated RNA constructs encoding different malarial peptide constructs in HEK293T cells. FIG.27A shows transfection rate as measured by percentage of total HEK293T population that is positive for presence of expressed protein. FIG.27B shows total expression as measured by median fluorescence intensity of the total HEK293T population for both transfected and non-transfected cells. [0204] FIGS.28A-28B depict immunogenicity induced in mice by formulated RNA constructs at day 21 after immunization. FIG.28A shows antibodies to an exemplary Plasmodium falciparum (Pf) CSP full length protein (“PfCSP-FL”). FIG.28B shows antibodies to an exemplary PfCSP C-terminal domain (“PfCSP-C term (3D7)”). Each data point is representative of one mouse and the bar denotes mean with SEM. LDL, lower detection limit. [0205] FIGS.29A-29B depict immunogenicity induced in mice by formulated RNA constructs at day 35 after immunization. FIG.29A shows antibodies to an exemplary Plasmodium falciparum (Pf) CSP full length protein (“PfCSP-FL”). FIG.29B shows antibodies to an exemplary PfCSP C-terminal domain (“PfCSP-C term (3D7)”). Each data point is representative of one mouse and the bar denotes mean with SEM. LDL, lower detection limit. [0206] FIGS.30A-30K depict binding of antibodies generated from mice immunized with formulated RNA constructs to various epitopes. FIG.30A shows a visual summary of the data in FIGS.30B-30K in the form of a heatmap. FIGS.30B-30K show bars that are representative of the area under the curve (AUC) created when plotting dilution steps versus ECL signal. [0207] FIGS.31A-31B depict binding specificity of antibodies generated from mice immunized with formulated RNA constructs to CSP protein in Plasmodium falciparum sporozoite lysates. FIG.31A shows binding between antibodies in the sera of immunized mice and CSP protein in the sporozoite (spz) lysates represented as area under the curve (AUC) created when plotting dilution steps versus luminescence signal. FIG.31B shows binding of murine anti-CSP mAb3SP2 used as a positive control. [0208] FIGS.32A-32C depict activation of T-cells, as assessed by secretion of IFN-γ. IFN-γ secretion was assessed using isolated splenocytes (from mice immunized with formulated RNA constructs) treated with overlapping peptide pools covering a full length CSP protein (FIG.32A) or controls (e.g., negative control: Trp1, 2 μg/mL (FIG. 32B); positive control: concanavalin A, 2 μg/mL (FIG.32C)). Samples were measured in triplicate and negative control was measured in duplicate; each data point represents a single mouse and bars represent the group mean spot-forming units (SFU) ± SD per 5x10⁵ splenocytes. Each data point in the medium and ConA controls represents the mean of triplicates of a pool of splenocytes from all mice. [0209] FIGS.33A-33C depict activation of T-cells, as assessed by secretion of IL-2. IL-2 secretion was assessed using isolated splenocytes (from mice immunized with formulated RNA constructs) treated with overlapping peptide pools covering a full length CSP protein (FIG.33A) or controls (e.g., negative control: Trp1, 2 μg/mL (FIG. 33B); positive control: concanavalin A, 2 μg/mL (FIG.33C)). Samples were measured in triplicate and negative control was measured in duplicate; each data point represents a single mouse and bars represent the group mean spot-forming units (SFU) ± SD per 5x10⁵ splenocytes. Each data point in the medium and ConA controls represents the mean of triplicates of a pool of splenocytes from all mice. [0210] FIGS.34A-34C depict activation of T-cells, as assessed by secretion of TNF-α. TNF-α secretion was assessed using isolated splenocytes (from mice immunized with formulated RNA constructs) treated with overlapping peptide pools covering a full length CSP protein (FIG.34A) or controls (e.g., negative control: Trp1, 2 μg/mL (FIG. 34B); positive control: concanavalin A, 2 μg/mL (FIG.34C)). Samples were measured in triplicate and negative control was measured in duplicate; each data point represents a single mouse and bars represent the group mean spot-forming units (SFU) ± SD per 5x10⁵ splenocytes. Each data point in the medium and ConA controls represents the mean of triplicates of a pool of splenocytes from all mice. [0211] FIGS.35A-35C depict activation of T-cells, as assessed by secretion of both IFN-γ and IL-2. IFN-γ+IL- 2 secretion was assessed using isolated splenocytes (from mice immunized with formulated RNA constructs) treated with overlapping peptide pools covering a full length CSP protein (FIG.35A) or controls (e.g., negative control: Trp1, 2 μg/mL (FIG.35B); positive control: concanavalin A, 2 μg/mL (FIG.35C)). Samples were measured in triplicate and negative control was measured in duplicate; each data point represents a single mouse and bars represent the group mean spot-forming units (SFU) ± SD per 5x10⁵ splenocytes. Each data point in the medium and ConA controls represents the mean of triplicates of a pool of splenocytes from all mice. [0212] FIGS.36A-36C depict activation of T-cells, as assessed by secretion of both IFN-γ and TNF-α. IFN-γ+ TNF-α secretion was assessed using isolated splenocytes (from mice immunized with formulated RNA constructs) treated with overlapping peptide pools covering a full length CSP protein (FIG.36A) or controls (e.g., negative control: Trp1, 2 μg/mL (FIG.36B); positive control: concanavalin A, 2 μg/mL (FIG.36C)). Samples were measured in triplicate and negative control was measured in duplicate; each data point represents a single mouse and bars represent the group mean spot-forming units (SFU) ± SD per 5x10⁵ splenocytes. Each data point in the medium and ConA controls represents the mean of triplicates of a pool of splenocytes from all mice. [0213] FIGS.37A-37C depict activation of T-cells, as assessed by secretion of both IL-2 and TNF-α. IL-2+ TNF-α secretion was assessed using isolated splenocytes (from mice immunized with formulated RNA constructs) treated with overlapping peptide pools covering a full length CSP protein (FIG.37A) or controls (e.g., negative control: Trp1, 2 μg/mL (FIG.37B); positive control: concanavalin A, 2 μg/mL (FIG.37C)). Samples were measured in triplicate and negative control was measured in duplicate; each data point represents a single mouse and bars represent the group mean spot-forming units (SFU) ± SD per 5x10⁵ splenocytes. Each data point in the medium and ConA controls represents the mean of triplicates of a pool of splenocytes from all mice. [0214] FIGS.38A-38C depict activation of T-cells, as assessed by secretion of IFN-γ, IL-2 and TNF-α. IFN- γ+IL-2+TNF-α secretion was assessed using isolated splenocytes (from mice immunized with formulated RNA constructs) treated with overlapping peptide pools covering a full length CSP protein (FIG.38A) or controls (e.g., negative control: Trp1, 2 μg/mL (FIG.38B); positive control: concanavalin A, 2 μg/mL (FIG.38C)). Samples were measured in triplicate and negative control was measured in duplicate; each data point represents a single mouse and bars represent the group mean spot-forming units (SFU) ± SD per 5x10⁵ splenocytes. Each data point in the medium and ConA controls represents the mean of triplicates of a pool of splenocytes from all mice. [0215] FIGS.39A-39D depict activation of CD4 T cells only, as assessed by secretion of IFN-γ. IFN-γ secretion was assessed by a fluorospot assay after using MACS separation to isolate CD4+ T cells (from pools of splenocytes from mice immunized with each of the formulated RNA constructs). Cells were then incubated with overlapping peptide pools covering a full length CSP protein (FIG.39A) or controls (e.g., negative control: Trp1, 2 μg/mL (FIG.39B); positive control: concanavalin A, 2 μg/mL (FIG.39C); medium control (FIG.39D)). Pooled samples were measured in triplicate and negative control was measured in duplicate; data points and bars represent the group mean spot-forming units (SFU) ± SD per 1x10⁵ CD4 T cells. [0216] FIGS.40A-40D depict activation of CD4 T cells only, as assessed by secretion of IL-2. IL-2 secretion was assessed by a fluorospot assay after using MACS separation to isolate CD4+ T cells (from pools of splenocytes from mice immunized with each of the formulated RNA constructs). Cells were then incubated with overlapping peptide pools covering a full length CSP protein (FIG.40A) or controls (e.g., negative control: Trp1, 2 μg/mL (FIG. 40B); positive control: concanavalin A, 2 μg/mL (FIG.40C); medium control (FIG.40D)). Pooled samples were measured in triplicate and negative control was measured in duplicate; data points and bars represent the group mean spot-forming units (SFU) ± SD per 1x10⁵ CD4 T cells. [0217] FIGS.41A-41D depict activation of CD4 T cells only, as assessed by secretion of TNF-α. TNF-α secretion was assessed by a fluorospot assay after using MACS separation to isolate CD4+ T cells (from pools of splenocytes from mice immunized with each of the formulated RNA constructs). Cells were then incubated with overlapping peptide pools covering a full length CSP protein (FIG.41A) or controls (e.g., negative control: Trp1, 2 μg/mL (FIG.41B); positive control: concanavalin A, 2 μg/mL (FIG.41C); medium control (FIG.41D)). Pooled samples were measured in triplicate and negative control was measured in duplicate; data points and bars represent the group mean spot-forming units (SFU) ± SD per 1x10⁵ CD4 T cells. [0218] FIGS.42A-42D depict activation of CD4 T cells only, as assessed by secretion of both IFN-γ and IL-2. IFN-γ+IL-2 secretion was assessed by a fluorospot assay after using MACS separation to isolate CD4+ T cells (from pools of splenocytes from mice immunized with each of the formulated RNA constructs). Cells were then incubated with overlapping peptide pools covering a full length CSP protein (FIG.42A) or controls (e.g., negative control: Trp1, 2 μg/mL (FIG.42B); positive control: concanavalin A, 2 μg/mL (FIG.42C); medium control (FIG.42D)). Pooled samples were measured in triplicate and negative control was measured in duplicate; data points and bars represent the group mean spot-forming units (SFU) ± SD per 1x10⁵ CD4 T cells. [0219] FIGS.43A-43D depict activation of CD4 T cells only, as assessed by secretion of both IFN-γ and TNF-α. IFN-γ+TNF-α secretion was assessed by a fluorospot assay after using MACS separation to isolate CD4+ T cells (from pools of splenocytes from mice immunized with each of the formulated RNA constructs). Cells were then incubated with overlapping peptide pools covering a full length CSP protein (FIG.43A) or controls (e.g., negative control: Trp1, 2 μg/mL (FIG.43B); positive control: concanavalin A, 2 μg/mL (FIG.43C); medium control (FIG. 43D)). Pooled samples were measured in triplicate and negative control was measured in duplicate; data points and bars represent the group mean spot-forming units (SFU) ± SD per 1x10⁵ CD4 T cells. [0220] FIGS.44A-44D depict activation of CD4 T cells only, as assessed by secretion of both IL-2 and TNF-α. IL-2+TNF-α secretion was assessed by a fluorospot assay after using MACS separation to isolate CD4+ T cells (from pools of splenocytes from mice immunized with each of the formulated RNA constructs). Cells were then incubated with overlapping peptide pools covering a full length CSP protein (FIG.44A) or controls (e.g., negative control: Trp1, 2 μg/mL (FIG.44B); positive control: concanavalin A, 2 μg/mL (FIG.44C); medium control (FIG.44D)). Pooled samples were measured in triplicate and negative control was measured in duplicate; data points and bars represent the group mean spot-forming units (SFU) ± SD per 1x10⁵ CD4 T cells. [0221] FIGS.45A-45D depict activation of CD4 T cells only, as assessed by secretion of IFN-γ, IL-2 and TNF- α. IFN-γ+IL-2+TNF-α secretion was assessed by a fluorospot assay after using MACS separation to isolate CD4+ T cells (from pools of splenocytes from mice immunized with each of the formulated RNA constructs). Cells were then incubated with overlapping peptide pools covering a full length CSP protein (FIG.45A) or controls (e.g., negative control: Trp1, 2 μg/mL (FIG.45B); positive control: concanavalin A, 2 μg/mL (FIG.45C); medium control (FIG. 45D)). Pooled samples were measured in triplicate and negative control was measured in duplicate; data points and bars represent the group mean spot-forming units (SFU) ± SD per 1x10⁵ CD4 T cells. [0222] FIGS.46A-46D depict activation of CD8 T cells only, as assessed by secretion of IFN-γ. IFN-γ secretion was assessed by a fluorospot assay after using MACS separation to isolate CD8+ T cells (from pools of splenocytes from mice immunized with each of the formulated RNA constructs). Cells were then incubated with overlapping peptide pools covering a full length CSP protein (FIG.46A) or controls (e.g., negative control: Trp1, 2 μg/mL (FIG.46B); positive control: concanavalin A, 2 μg/mL (FIG.46C); medium control (FIG.46D)). Pooled samples were measured in triplicate and negative control was measured in duplicate; data points and bars represent the group mean spot-forming units (SFU) ± SD per 1x10⁵ CD8 T cells. [0223] FIGS.47A-47D depict activation of CD8 T cells only, as assessed by secretion of IL-2. IL-2 secretion was assessed by a fluorospot assay after using MACS separation to isolate CD8+ T cells (from pools of splenocytes from mice immunized with each of the formulated RNA constructs). Cells were then incubated with overlapping peptide pools covering a full length CSP protein (FIG.47A) or controls (e.g., negative control: Trp1, 2 μg/mL (FIG. 47B); positive control: concanavalin A, 2 μg/mL (FIG.47C); medium control (FIG.47D)). Pooled samples were measured in triplicate and negative control was measured in duplicate; data points and bars represent the group mean spot-forming units (SFU) ± SD per 1x10⁵ CD8 T cells. [0224] FIGS.48A-48D depict activation of CD8 T cells only, as assessed by secretion of TNF-α. TNF-α secretion was assessed by a fluorospot assay after using MACS separation to isolate CD8+ T cells (from pools of splenocytes from mice immunized with each of the formulated RNA constructs). Cells were then incubated with overlapping peptide pools covering a full length CSP protein (FIG.48A) or controls (e.g., negative control: Trp1, 2 μg/mL (FIG.48B); positive control: concanavalin A, 2 μg/mL (FIG.48C); medium control (FIG.48D)). Pooled samples were measured in triplicate and negative control was measured in duplicate; data points and bars represent the group mean spot-forming units (SFU) ± SD per 1x10⁵ CD8 T cells. [0225] FIGS.49A-49D depict activation of CD8 T cells only, as assessed by secretion of both IFN-γ and IL-2. IFN-γ+IL-2 secretion was assessed by a fluorospot assay after using MACS separation to isolate CD8+ T cells (from pools of splenocytes from mice immunized with each of the formulated RNA constructs). Cells were then incubated with overlapping peptide pools covering a full length CSP protein (FIG.49A) or controls (e.g., negative control: Trp1, 2 μg/mL (FIG.49B); positive control: concanavalin A, 2 μg/mL (FIG.49C); medium control (FIG.49D)). Pooled samples were measured in triplicate and negative control was measured in duplicate; data points and bars represent the group mean spot-forming units (SFU) ± SD per 1x10⁵ CD8 T cells. [0226] FIGS.50A-50D depict activation of CD8 T cells only, as assessed by secretion of both IFN-γ and TNF- α. IFN-γ+TNF-α secretion was assessed by a fluorospot assay after using MACS separation to isolate CD8+ T cells (from pools of splenocytes from mice immunized with each of the formulated RNA constructs). Cells were then incubated with overlapping peptide pools covering a full length CSP protein (FIG.50A) or controls (e.g., negative control: Trp1, 2 μg/mL (FIG.50B); positive control: concanavalin A, 2 μg/mL (FIG.50C); medium control (FIG. 50D)). Pooled samples were measured in triplicate and negative control was measured in duplicate; data points and bars represent the group mean spot-forming units (SFU) ± SD per 1x10⁵ CD8 T cells. [0227] FIGS.51A-51D depict activation of CD8 T cells only, as assessed by secretion of both IL-2 and TNF-α. IL-2+TNF-α secretion was assessed by a fluorospot assay after using MACS separation to isolate CD8+ T cells (from pools of splenocytes from mice immunized with each of the formulated RNA constructs). Cells were then incubated with overlapping peptide pools covering a full length CSP protein (FIG.51A) or controls (e.g., negative control: Trp1, 2 μg/mL (FIG.51B); positive control: concanavalin A, 2 μg/mL (FIG.51C); medium control (FIG.51D)). Pooled samples were measured in triplicate and negative control was measured in duplicate; data points and bars represent the group mean spot-forming units (SFU) ± SD per 1x10⁵ CD8 T cells. [0228] FIGS.52A-52D depict activation of CD8 T cells only, as assessed by secretion of IFN-γ, IL-2 and TNF- α. IFN-γ+IL-2+TNF-α secretion was assessed by a fluorospot assay after using MACS separation to isolate CD8+ T cells (from pools of splenocytes from mice immunized with each of the formulated RNA constructs). Cells were then incubated with overlapping peptide pools covering a full length CSP protein (FIG.52A) or controls (e.g., negative control: Trp1, 2 μg/mL (FIG.52B); positive control: concanavalin A, 2 μg/mL (FIG.52C); medium control (FIG. 52D). Pooled samples were measured in triplicate and negative control was measured in duplicate; data points and bars represent the group mean spot-forming units (SFU) ± SD per 1x10⁵ CD8 T cells. [0229] FIGS.53A-53C depict in vitro expression of ERMA 23-7 RNA construct in HEK293T cells. FIG.53A shows transfection rate as measured by percentage of total HEK293T population that is positive for presence of expressed protein. FIG.53B shows total expression as measured by median fluorescence of the total HEK293T population for both transfected and non-transfected cells. FIG.53C shows percentage of viable cells that are positive for presence of expressed protein, with non-transfected cells serving as a control. [0230] FIGS.54A-54B depict titers of antibodies elicited against PfCSP after immunization of mice with a pharmaceutical composition comprising ERMA 23-7. FIG.54A shows endpoint titers against full-length PfCSP on day 21, pre-boost. FIG.54B shows endpoint titers against full-length PfCSP on day 35 after boost. [0231] FIGS.55A-55B depict epitope specificity of antibodies elicited upon immunization of mice with a pharmaceutical composition comprising ERMA 23-7. FIG.55A shows a diagram depicting localization of peptides using in multiplex assay in central region of PfCSP sequence. FIG.55B shows binding to epitopes by calculating AUC of 8-point dilution of immune serum samples. [0232] FIGS.56A-56C depict pro-inflammatory response from T cells after immunization of mice with a pharmaceutical composition comprising ERMA 23-7. FIG.56A shows production of IFNɣ in mouse splenocytes after immunization with a pharmaceutical composition comprising ERMA 23-7 and stimulation with PfCSP peptides. FIG. 56B shows production of IFNɣ in combination with IL-2 in mouse splenocytes after immunization with a pharmaceutical composition comprising ERMA 23-7 and stimulation with PfCSP peptides. FIG.56C shows production of IFNɣ in combination with IL-2 and TNFα in mouse splenocytes after immunization with a pharmaceutical composition comprising ERMA 23-7 and stimulation with PfCSP peptides. [0233] FIGS.57A-57B depict titers of antibodies elicited against PfCSP after immunization of mice with a pharmaceutical composition comprising ERMA 23-7 or with Composition 1, 2, and 3 comprising ERMA 23-7, MAS3a and MAS4f. FIG.57A shows endpoint titers (reciprocal serum titer) against full-length PfCSP pre-boost on Day 21. FIG.57B shows endpoint titers (reciprocal serum titer) against full-length PfCSP after boost on Day 35. [0234] FIG.58 depicts epitope specificity of antibodies elicited upon immunization of mice with a pharmaceutical composition comprising ERMA 23-7 or with Compositions 1, 2 and 3 comprising ERMA 23-7, MAS3a and MAS4f. [0235] FIG.59 depicts T-cell induction following immunization with Composition 3 comprising 1 μg ERMA 23- 7, 2 μg MAS3a and 2 μg MAS4f. [0236] FIGS.60A-60B depict T-cell induction following immunization. FIG.60A shows the results for a combination of two T-cell string constructs by comparing the effects of a pharmaceutical composition comprising 2 μg MAS3a and 2 μg MAS4f (black dots) and Composition 3 comprising 1 μg ERMA 23-7, 2 μg MAS3a and 2 μg MAS4f (red dots). FIG.60B shows the results for a CSP construct by comparing the effects of a pharmaceutical composition comprising 1 μg ERMA 23-7 (black dots) and Composition 3 comprising 1 μg ERMA 23-7, 2 μg MAS3a and 2 μg MAS4f (red dots). [0237] FIGS.61A-61K depict an assessment of antibodies generated from mice immunized with formulated RNA constructs for their ability to inhibit P. falciparum sporozoite infection of primary human hepatocytes. Percentage of inhibition of infection activity (mean with SEM) in comparison to a control (medium only) is shown for a 1:40 dilution (FIGS.61A and 61E), a 1:160 dilution (FIGS.61B and 61F), a 1:640 dilution (FIGS.61C and 61G), and a 1:2560 dilution (FIGS.61D and 61H). Inhibition of antibodies in sera of immunized mice in ILSDA is represented as area under the curve (AUC) created when plotting dilution steps versus percentage inhibition of infection (FIGS. 61I and 61J). ILSDA results for a positive control (mAb317, an antibody reported to inhibit hepatocyte infection) are also shown (FIG.61K). [0238] FIGS. 62A-62F depict an assessment of binding and disassociation of antibodies generated from mice immunized with formulated RNA constructs and exposed to full length PfCSP, a peptide with a junction region and minor repeats (Junction + Minor repeats), or a peptide with major repeats (Major repeats). Serum samples from all treated mice were pooled prior to analysis. Level of antibody binding to a respective binding partner is shown in resonance units (RU) (FIGS.62A, 62C, and 62E). Percentage of antibody:antigen complexes still measurable after 15 minutes of dissociation (Residual Response) is calculated from initial binding (FIGS.62B, 62D, and 62F). [0239] FIGS.63A-63D depict T-cell induction following immunization with 1 μg of Mas3a or a codon- optimized version (Mas3a-2, Mas3a-3) and 1 μg Mas4f or a codon-optimized version (Mas4f-2, Mas4f-3). Antigen specific T-cell induction 7 days after immunization is shown for the combination of 1 μg Mas3a and 1 μg Mas4f (FIG. 63A), and the combination of 1 μg Mas3a-3 and 1 μg Mas4f-3 (FIG.63B). Antigen specific T-cell induction 35 days after immunization is shown for the combination of 1 μg Mas3a and 1 μg Mas4f (FIG.63C), and the combination of 1 μg Mas3a-3 and 1 μg Mas4f-3 (FIG.63D). [0240] FIGS.64A-64D depict antigen-specific IFNɣ and IL-2 T-cell responses following immunization with 1 μg of Mas3a or a codon-optimized version (Mas3a-2, Mas3a-3) and 1 μg Mas4f or a codon-optimized version (Mas4f- 2, Mas4f-3). Antigen-specific IFNɣ responses after immunization for the combination of 1 μg Mas3a and 1 μg Mas4f is compared to the combination of 1 μg Mas3a-3 and 1 μg Mas4f-3 (FIG.64A) and Mas3a-2 and 1 μg Mas4f-2 (FIG. 64C). Antigen-specific IL-2 responses after immunization for the combination of 1 μg Mas3a and 1 μg Mas4f is compared to the combination of 1 μg Mas3a -3 and 1 μg Mas4f-3 (FIG.64B) and Mas3a-2 and 1 μg Mas4f-2 (FIG. 64D). [0241] FIGS.65A-65H depict assessment of antibodies generated from mice immunized with formulated RNA constructs for ability to inhibit P. falciparum sporozoite traversal in HC-04 hepatoma cells. Percentage of inhibition of traversal activity (mean with SEM) in comparison to a medium control, which was set as 0% inhibition, is shown for a 1:20 dilution (FIG.65A), a 1:40 dilution (FIG.65B), a 1:80 dilution (FIG.65C), a 1:160 dilution (FIG. 65D), a 1:320 dilution (FIG.65E), and a 1:640 dilution (FIG.65F). Inhibition of antibodies in sera of immunized mice in traversal assays is represented as area under the curve (AUC) created when plotting dilution steps versus % inhibition of traversal (FIG.65G). Traversal assay results for a positive control (mAb317, an antibody known to inhibit sporozoite traversal) are also shown (FIG.65H). [0242] FIGS.66A-66G depict assessment of antibodies generated from mice immunized with formulated RNA constructs for ability to inhibit P. falciparum sporozoite traversal in HC-04 hepatoma cells. Percentage of inhibition of traversal activity (mean with SEM) in comparison to a medium control, which was set as 0% inhibition, is shown for a 1:20 dilution (FIG.66A), a 1:40 dilution (FIG.66B), a 1:80 dilution (FIG.66C), a 1:160 dilution (FIG.66D), a 1:320 dilution (FIG.66E), and a 1:640 dilution (FIG.66F). Inhibition of antibodies in sera of immunized mice in traversal assays is represented as area under the curve (AUC) created when plotting dilution steps versus % inhibition of traversal (FIG.66G). [0243] FIGS.67A-67B depict in vitro expression of non-formulated RNA constructs 91, 100 and 104 encoding different Plasmodium polypeptides in HEK293T cells. FIG.67A shows transfection rate as measured by percentage of total HEK293T population that is positive for presence of expressed protein. FIG.67B shows total expression as measured by median fluorescence of the total HEK293T population for both transfected and non-transfected cells. Permeabilized cells show total protein expressed (black bar, intracellular staining) and non-permeabilized cells show only surface expressed protein (grey bar, surface staining). Protein was detected using anti-PfCSP L9 antibody. Each sample was stained in triplicate, bar is a representation of mean with SD; NT, non-transfected. [0244] FIGS.68A-68B depict in vitro expression of non-formulated RNA constructs 87 and 88 encoding different Plasmodium polypeptides in HEK293T cells. FIG.68A shows transfection rate as measured by percentage of total HEK293T population that is positive for presence of expressed protein. FIG.68B shows total expression as measured by median fluorescence of the total HEK293T population for both transfected and non-transfected cells. Permeabilized cells show total protein expressed (black bar, intracellular staining) and non-permeabilized cells show only surface expressed protein (grey bar, surface staining). Protein was detected using anti-PfCSP L9 antibody. Each sample was stained in triplicate, bar is a representation of mean with SD; NT, non-transfected. [0245] FIGS.69A-69B depict in vitro expression of formulated RNA constructs 87, 88, 91, 100 and 104 encoding different Plasmodium polypeptides in HEK293T cells. FIG.69A shows transfection rate as measured by percentage of total HEK293T population that is positive for presence of expressed protein. FIG.69B shows total expression as measured by median fluorescence of the total HEK293T population for both transfected and non- transfected cells. Permeabilized cells show total protein expressed (black bar, intracellular staining) and non- permeabilized cells show only surface expressed protein (grey bar, surface staining). Protein was detected using anti- PfCSP L9 antibody. Each sample was stained in triplicate, bar is a representation of mean with SD; NT, non- transfected. [0246] FIGS.70A-70B depict immunogenicity induced in mice by formulated RNA constructs 87, 88, 91, 100 and 104. FIG.70A shows antibodies to Plasmodium falciparum (Pf) CSP full length protein (“PfCSP-FL”). FIG.70B shows antibodies to PfCSP C-terminal domain (“PfCSP-C term (3D7)”). Each data point is representative of one mouse and the bar denotes mean with SEM. LDL, lower detection limit. [0247] FIG.71 depicts binding of antibodies generated from mice immunized with formulated RNA constructs 87, 88, 91, 104, and 100 during challenge studies to various epitopes in a heatmap format. [0248] FIGS.72A-72J depict binding of antibodies generated from mice immunized with formulated RNA constructs to various epitopes. FIGS.72A-72J each show bars that are representative of the area under the curve (AUC) created when plotting dilution steps versus ECL signal. [0249] FIGS.73A-73C depict activation of T-cells, as assessed by secretion of IFN-γ. IFN-γ secretion was assessed using isolated splenocytes (from mice immunized with formulated RNA constructs) treated with overlapping peptide pools covering the full length CSP protein (FIG.73A) or controls (e.g., negative control: Trp1, 2 μg/mL (FIG.73B); positive control: concanavalin A, 2 μg/mL (FIG.73C)). Samples were measured in triplicate and negative control was measured in duplicate; each data point represents a single mouse and bars represent the group mean spot-forming units (SFU) ± SD per 5x10⁵ splenocytes. Each data point in the medium and ConA controls represents the mean of triplicates of a pool of splenocytes from all mice. ve, vehicle. [0250] FIGS.74A-74C depicts activation of T-cells, as assessed by secretion of IL-2. IL-2 secretion was assessed using isolated splenocytes (from mice immunized with formulated RNA constructs) treated with overlapping peptide pools covering the full length CSP protein (FIG.74A) or controls (e.g., negative control: Trp1, 2 μg/mL (FIG.74B); positive control: concanavalin A, 2 μg/mL (FIG.74C)). Samples were measured in triplicate and negative control was measured in duplicate; each data point represents a single mouse and bars represent the group mean spot-forming units (SFU) ± SD per 5x10⁵ splenocytes. Each data point in the medium and ConA controls represents the mean of triplicates of a pool of splenocytes from all mice. ve, vehicle. [0251] FIGS.75A-75C depicts activation of T-cells, as assessed by secretion of TNF-α. TNF-α secretion was assessed using isolated splenocytes (from mice immunized with formulated RNA constructs) treated with overlapping peptide pools covering the full length CSP protein (FIG.75A) or controls (e.g., negative control: Trp1, 2 μg/mL (FIG.75B); positive control: concanavalin A, 2 μg/mL (FIG.75C)). Samples were measured in triplicate and negative control was measured in duplicate; each data point represents a single mouse and bars represent the group mean spot-forming units (SFU) ± SD per 5x10⁵ splenocytes. Each data point in the medium and ConA controls represents the mean of triplicates of a pool of splenocytes from all mice. ve, vehicle. [0252] FIGS.76A-76C depicts activation of T-cells, as assessed by secretion of both IFN-γ and IL-2. IFN- γ+IL-2 secretion was assessed using isolated splenocytes (from mice immunized with formulated RNA constructs) treated with overlapping peptide pools covering the full length CSP protein (FIG.76A) or controls (e.g., negative control: Trp1, 2 μg/mL (FIG.76B); positive control: concanavalin A, 2 μg/mL (FIG.76C)). Samples were measured in triplicate and negative control was measured in duplicate; each data point represents a single mouse and bars represent the group mean spot-forming units (SFU) ± SD per 5x10⁵ splenocytes. Each data point in the medium and ConA controls represents the mean of triplicates of a pool of splenocytes from all mice. ve, vehicle. [0253] FIGS.77A-77C depicts activation of T-cells, as assessed by secretion of both IFN-γ and TNF-α. IFN- γ+ TNF-α secretion was assessed using isolated splenocytes (from mice immunized with formulated RNA constructs) treated with overlapping peptide pools covering the full length CSP protein (FIG.77A) or controls (e.g., negative control: Trp1, 2 μg/mL (FIG.77B); positive control: concanavalin A, 2 μg/mL (FIG.77C)). Samples were measured in triplicate and negative control was measured in duplicate; each data point represents a single mouse and bars represent the group mean spot-forming units (SFU) ± SD per 5x10⁵ splenocytes. Each data point in the medium and ConA controls represents the mean of triplicates of a pool of splenocytes from all mice. ve, vehicle. [0254] FIGS.78A-78C depicts activation of T-cells, as assessed by secretion of both IL-2 and TNF-α. IL-2+ TNF-α secretion was assessed using isolated splenocytes (from mice immunized with formulated RNA constructs) treated with overlapping peptide pools covering the full length CSP protein (FIG.78A) or controls (e.g., negative control: Trp1, 2 μg/mL (FIG.78B); positive control: concanavalin A, 2 μg/mL (FIG.78C)). Samples were measured in triplicate and negative control was measured in duplicate; each data point represents a single mouse and bars represent the group mean spot-forming units (SFU) ± SD per 5x10⁵ splenocytes. Each data point in the medium and ConA controls represents the mean of triplicates of a pool of splenocytes from all mice. ve, vehicle. [0255] FIGS.79A-79C depicts activation of T-cells, as assessed by secretion of IFN-γ, IL-2 and TNF-α. IFN- γ+IL-2+TNF-α secretion was assessed using isolated splenocytes (from mice immunized with formulated RNA constructs) treated with overlapping peptide pools covering the full length CSP protein (FIG.79A) or controls (e.g., negative control: Trp1, 2 μg/mL (FIG.79B); positive control: concanavalin A, 2 μg/mL (FIG.79C)). Samples were measured in triplicate and negative control was measured in duplicate; each data point represents a single mouse and bars represent the group mean spot-forming units (SFU) ± SD per 5x10⁵ splenocytes. Each data point in the medium and ConA controls represents the mean of triplicates of a pool of splenocytes from all mice. ve, vehicle. [0256] FIGS.80A-80D depicts activation of CD4 T cells only, as assessed by secretion of IFN-γ. IFN-γ secretion was assessed by a fluorospot assay after using MACS separation to isolate CD4+ T cells (from pools of splenocytes from mice immunized with formulated RNA constructs). Cells were then incubated with overlapping peptide pools covering the full length CSP protein (FIG.80A) or controls (e.g., negative control: Trp1, 2 μg/mL (FIG.80B); positive control: concanavalin A, 2 μg/mL (FIG.80C); medium control (FIG.80D)). Pooled samples were measured in triplicate and negative control was measured in duplicate; data points and bars represent the group mean spot-forming units (SFU) ± SD per 1x10⁵ CD4 T cells; ve, vehicle. [0257] FIGS.81A-81D depicts activation of CD4 T cells only, as assessed by secretion of IL-2. IL-2 secretion was assessed by a fluorospot assay after using MACS separation to isolate CD4+ T cells (from pools of splenocytes from mice immunized with formulated RNA constructs). Cells were then incubated with overlapping peptide pools covering the full length CSP protein (FIG.81A) or controls (e.g., negative control: Trp1, 2 μg/mL (FIG.81B); positive control: concanavalin A, 2 μg/mL (FIG.81C); medium control (FIG.81D)). Pooled samples were measured in triplicate and negative control was measured in duplicate; data points and bars represent the group mean spot- forming units (SFU) ± SD per 1x10⁵ CD4 T cells; ve, vehicle. [0258] FIGS.82A-82D depicts activation of CD4 T cells only, as assessed by secretion of TNF-α. TNF-α secretion was assessed by a fluorospot assay after using MACS separation to isolate CD4+ T cells (from pools of splenocytes from mice immunized with formulated RNA constructs). Cells were then incubated with overlapping peptide pools covering the full length CSP protein (FIG.82A) or controls (e.g., negative control: Trp1, 2 μg/mL (FIG.82B); positive control: concanavalin A, 2 μg/mL (FIG.82C); medium control (FIG.82D)). Pooled samples were measured in triplicate and negative control was measured in duplicate; data points and bars represent the group mean spot-forming units (SFU) ± SD per 1x10⁵ CD4 T cells; ve, vehicle. [0259] FIGS.83A-83D depicts activation of CD4 T cells only, as assessed by secretion of both IFN-γ and IL- 2. IFN-γ+IL-2 secretion was assessed by a fluorospot assay after using MACS separation to isolate CD4+ T cells (from pools of splenocytes from mice immunized with formulated RNA constructs). Cells were then incubated with overlapping peptide pools covering the full length CSP protein (FIG.83A) or controls (e.g., negative control: Trp1, 2 μg/mL (FIG.83B); positive control: concanavalin A, 2 μg/mL (FIG.83C); medium control (FIG.83D)). Pooled samples were measured in triplicate and negative control was measured in duplicate; data points and bars represent the group mean spot-forming units (SFU) ± SD per 1x10⁵ CD4 T cells; ve, vehicle. [0260] FIGS.84A-84D depicts activation of CD4 T cells only, as assessed by secretion of both IFN-γ and TNF-α. IFN-γ+TNF-α secretion was assessed by a fluorospot assay after using MACS separation to isolate CD4+ T cells (from pools of splenocytes from mice immunized with formulated RNA constructs). Cells were then incubated with overlapping peptide pools covering the full length CSP protein (FIG.84A) or controls (e.g., negative control: Trp1, 2 μg/mL (FIG.84B); positive control: concanavalin A, 2 μg/mL (FIG.84C); medium control (FIG.84D)). Pooled samples were measured in triplicate and negative control was measured in duplicate; data points and bars represent the group mean spot-forming units (SFU) ± SD per 1x10⁵ CD4 T cells; ve, vehicle. [0261] FIGS.85A-85D depicts activation of CD4 T cells only, as assessed by secretion of both IL-2 and TNF- α. IL-2+TNF-α secretion was assessed by a fluorospot assay after using MACS separation to isolate CD4+ T cells (from pools of splenocytes from mice immunized with formulated RNA constructs). Cells were then incubated with overlapping peptide pools covering the full length CSP protein (FIG.85A) or controls (e.g., negative control: Trp1, 2 μg/mL (FIG.85B); positive control: concanavalin A, 2 μg/mL (FIG.85C); medium control (FIG.85D)). Pooled samples were measured in triplicate and negative control was measured in duplicate; data points and bars represent the group mean spot-forming units (SFU) ± SD per 1x10⁵ CD4 T cells; ve, vehicle. [0262] FIGS.86A-86D depicts activation of CD4 T cells only, as assessed by secretion of IFN-γ, IL-2 and TNF-α. IFN-γ+IL-2+TNF-α secretion was assessed by a fluorospot assay after using MACS separation to isolate CD4+ T cells (from pools of splenocytes from mice immunized with formulated RNA constructs). Cells were then incubated with overlapping peptide pools covering the full length CSP protein (FIG.86A) or controls (e.g., negative control: Trp1, 2 μg/mL (FIG.86B); positive control: concanavalin A, 2 μg/mL (FIG.86C); medium control (FIG.86D)). Pooled samples were measured in triplicate and negative control was measured in duplicate; data points and bars represent the group mean spot-forming units (SFU) ± SD per 1x10⁵ CD4 T cells; ve, vehicle. [0263] FIGS.87A-87D depicts activation of CD8 T cells only, as assessed by secretion of IFN-γ. IFN-γ secretion was assessed by a fluorospot assay after using MACS separation to isolate CD8+ T cells (from pools of splenocytes from mice immunized with formulated RNA constructs). Cells were then incubated with overlapping peptide pools covering the full length CSP protein (FIG.87A) or controls (e.g., negative control: Trp1, 2 μg/mL (FIG.87B); positive control: concanavalin A, 2 μg/mL (FIG.87C); medium control (FIG.87D)). Pooled samples were measured in triplicate and negative control was measured in duplicate; data points and bars represent the group mean spot-forming units (SFU) ± SD per 1x10⁵ CD8 T cells; ve, vehicle. [0264] FIGS.88A-88D depicts activation of CD8 T cells only, as assessed by secretion of IL-2. IL-2 secretion was assessed by a fluorospot assay after using MACS separation to isolate CD8+ T cells (from pools of splenocytes from mice immunized with formulated RNA constructs). Cells were then incubated with overlapping peptide pools covering the full length CSP protein (FIG.88A) or controls (e.g., negative control: Trp1, 2 μg/mL (FIG.88B); positive control: concanavalin A, 2 μg/mL (FIG.88C); medium control (FIG.88D)). Pooled samples were measured in triplicate and negative control was measured in duplicate; data points and bars represent the group mean spot- forming units (SFU) ± SD per 1x10⁵ CD8 T cells; ve, vehicle. [0265] FIGS.89A-89D depicts activation of CD8 T cells only, as assessed by secretion of TNF-α. TNF-α secretion was assessed by a fluorospot assay after using MACS separation to isolate CD8+ T cells (from pools of splenocytes from mice immunized with formulated RNA constructs). Cells were then incubated with overlapping peptide pools covering the full length CSP protein (FIG.89A) or controls (e.g., negative control: Trp1, 2 μg/mL (FIG.89B); positive control: concanavalin A, 2 μg/mL (FIG.89C); medium control (FIG.89D)). Pooled samples were measured in triplicate and negative control was measured in duplicate; data points and bars represent the group mean spot-forming units (SFU) ± SD per 1x10⁵ CD8 T cells; ve, vehicle. [0266] FIGS.90A-90D depicts activation of CD8 T cells only, as assessed by secretion of both IFN-γ and IL- 2. IFN-γ+IL-2 secretion was assessed by a fluorospot assay after using MACS separation to isolate CD8+ T cells (from pools of splenocytes from mice immunized with formulated RNA constructs). Cells were then incubated with overlapping peptide pools covering the full length CSP protein (FIG.90A) or controls (e.g., negative control: Trp1, 2 μg/mL (FIG.90B); positive control: concanavalin A, 2 μg/mL (FIG.90C); medium control (FIG.90D)). Pooled samples were measured in triplicate and negative control was measured in duplicate; data points and bars represent the group mean spot-forming units (SFU) ± SD per 1x10⁵ CD8 T cells; ve, vehicle. [0267] FIGS.91A-91D depicts activation of CD8 T cells only, as assessed by secretion of both IFN-γ and TNF-α. IFN-γ+TNF-α secretion was assessed by a fluorospot assay after using MACS separation to isolate CD8+ T cells (from pools of splenocytes from mice immunized with formulated RNA constructs). Cells were then incubated with overlapping peptide pools covering the full length CSP protein (FIG.91A) or controls (e.g., negative control: Trp1, 2 μg/mL (FIG.91B); positive control: concanavalin A, 2 μg/mL (FIG.91C); medium control (FIG.91D)). Pooled samples were measured in triplicate and negative control was measured in duplicate; data points and bars represent the group mean spot-forming units (SFU) ± SD per 1x10⁵ CD8 T cells; ve, vehicle. [0268] FIGS.92A-92D depicts activation of CD8 T cells only, as assessed by secretion of both IL-2 and TNF- α. IL-2+TNF-α secretion was assessed by a fluorospot assay after using MACS separation to isolate CD8+ T cells (from pools of splenocytes from mice immunized with formulated RNA constructs). Cells were then incubated with overlapping peptide pools covering the full length CSP protein (FIG.92A) or controls (e.g., negative control: Trp1, 2 μg/mL (FIG.92B); positive control: concanavalin A, 2 μg/mL (FIG.92C); medium control (FIG.92D)). Pooled samples were measured in triplicate and negative control was measured in duplicate; data points and bars represent the group mean spot-forming units (SFU) ± SD per 1x10⁵ CD8 T cells; ve, vehicle. [0269] FIGS.93A-93D depicts activation of CD8 T cells only, as assessed by secretion of IFN-γ, IL-2 and TNF-α. IFN-γ+IL-2+TNF-α secretion was assessed by a fluorospot assay after using MACS separation to isolate CD8+ T cells (from pools of splenocytes from mice immunized with formulated RNA constructs). Cells were then incubated with overlapping peptide pools covering the full length CSP protein (FIG.93A) or controls (e.g., negative control: Trp1, 2 μg/mL (FIG.93B); positive control: concanavalin A, 2 μg/mL (FIG.93C); medium control (FIG.93D)). Pooled samples were measured in triplicate and negative control was measured in duplicate; data points and bars represent the group mean spot-forming units (SFU) ± SD per 1x10⁵ CD8 T cells; ve, vehicle. [0270] FIG.94 shows binding between antibodies in the sera of immunized mice and CSP protein in the sporozoite (spz) lysates represented as area under the curve (AUC) created when plotting dilution steps versus luminescence signal. DEFINITIONS [0271] Compounds of this disclosure include those described generally above and are further illustrated by the classes, subclasses, and species disclosed herein. As used herein, the following definitions shall apply unless otherwise indicated. For purposes of this disclosure, the chemical elements are identified in accordance with the Periodic Table of Elements, CAS version, Handbook of Chemistry and Physics, 75th Ed. Additionally, general principles of organic chemistry are described in “Organic Chemistry”, Thomas Sorrell, University Science Books, Sausalito: 1999, and “March’s Advanced Organic Chemistry”, 5th Ed., Ed.: Smith, M.B. and March, J., John Wiley & Sons, New York: 2001, the entire contents each of which are hereby incorporated by reference. [0272] Unless otherwise stated, structures depicted herein are meant to include all stereoisomeric (e.g., enantiomeric or diastereomeric) forms of the structure, as well as all geometric or conformational isomeric forms of the structure. For example, the R and S configurations of each stereocenter are contemplated as part of the disclosure. Therefore, single stereochemical isomers, as well as enantiomeric, diastereomeric, and geometric (or conformational) mixtures of provided compounds are within the scope of the disclosure. For example, in some cases, provided compounds show one or more stereoisomers of a compound, and unless otherwise indicated, represents each stereoisomer alone and/or as a mixture. Unless otherwise stated, all tautomeric forms of provided compounds are within the scope of the disclosure. [0273] Unless otherwise indicated, structures depicted herein are meant to include compounds that differ only in the presence of one or more isotopically enriched atoms. For example, compounds having the present structures including replacement of hydrogen by deuterium or tritium, or replacement of a carbon by 13C- or 14C-enriched carbon are within the scope of this disclosure. [0274] About: The term “about”, when used herein in reference to a value, refers to a value that is similar, in context to the referenced value. In general, those skilled in the art, familiar with the context, will appreciate the relevant degree of variance encompassed by “about” in that context. For example, in some embodiments, the term “about” may encompass a range of values that within 25%, 20%, 19%, 18%, 17%, 16%, 15%, 14%, 13%, 12%, 11%, 10%, 9%, 8%, 7%, 6%, 5%, 4%, 3%, 2%, 1%, or less of the referred value. [0275] Agent: As used herein, the term “agent,” may refer to a physical entity. In some embodiments, an agent may be characterized by a particular feature and/or effect. For example, as used herein, the term “therapeutic agent” refers to a physical entity has a therapeutic effect and/or elicits a desired biological and/or pharmacological effect. In some embodiments, an agent may be a compound, molecule, or entity of any chemical class including, for example, a small molecule, polypeptide, nucleic acid, saccharide, lipid, metal, or a combination or complex thereof. [0276] Amino acid: In its broadest sense, as used herein, the term “amino acid” refers to a compound and/or substance that can be, is, or has been incorporated into a polypeptide chain, e.g., through formation of one or more polypeptide bonds. In some embodiments, an amino acid has the general structure H2N–C(H)(R)–COOH. In some embodiments, an amino acid is a naturally-occurring amino acid. In some embodiments, an amino acid is a non- natural amino acid; in some embodiments, an amino acid is a D-amino acid; in some embodiments, an amino acid is an L-amino acid. “Standard amino acid” refers to any of the twenty standard L-amino acids commonly found in naturally occurring polypeptides. “Nonstandard amino acid” refers to any amino acid, other than the standard amino acids, regardless of whether it is prepared synthetically or obtained from a natural source. In some embodiments, an amino acid, including a carboxy- and/or amino-terminal amino acid in a polypeptide, can contain a structural modification as compared with the general structure above. For example, in some embodiments, an amino acid may be modified by methylation, amidation, acetylation, pegylation, glycosylation, phosphorylation, and/or substitution (e.g., of the amino group, the carboxylic acid group, one or more protons, and/or the hydroxyl group) as compared with the general structure. In some embodiments, such modification may, for example, alter the circulating half-life of a polypeptide containing the modified amino acid as compared with one containing an otherwise identical unmodified amino acid. In some embodiments, such modification does not significantly alter a relevant activity of a polypeptide containing the modified amino acid, as compared with one containing an otherwise identical unmodified amino acid. As will be clear from context, in some embodiments, the term “amino acid” may be used to refer to a free amino acid; in some embodiments it may be used to refer to an amino acid residue of a polypeptide. [0277] Antigen: The term “antigen”, as used herein, refers to an agent that elicits an immune response; and/or (ii) an agent that binds to a T cell receptor (e.g., when presented by an MHC molecule) or to an antibody. In the context of the present disclosure, the terms “malaria antigen” and “Plasmodium antigen” are understood to refer to an antigen from a Plasmodium species, where the Plasmodium species can cause malaria in a subject. [0278] Anti-malaria immune response: The term “anti-malaria immune response”, as used herein, refers to an immune response produced through pre-exposure to one or more Plasmodium antigens, e.g., through administration (e.g., vaccination) of the constructs as described herein directed to Plasmodium. [0279] Associated: Two events or entities are “associated” with one another, as that term is used herein, if the presence, level, degree, type and/or form of one is correlated with that of the other. For example, a particular entity (e.g., polypeptide, genetic signature, metabolite, microbe, etc.) is considered to be associated with a particular disease, disorder, or condition, if its presence, level and/or form correlates with incidence of, susceptibility to, severity of, stage of, etc. the disease, disorder, or condition (e.g., across a relevant population). In some embodiments, two or more entities are physically “associated” with one another if they interact, directly or indirectly, so that they are and/or remain in physical proximity with one another. In some embodiments, two or more entities that are physically associated with one another are covalently linked to one another; in some embodiments, two or more entities that are physically associated with one another are not covalently linked to one another but are non- covalently associated, for example by means of hydrogen bonds, van der Waals interaction, hydrophobic interactions, magnetism, and combinations thereof. [0280] C-terminal domain: The term “C-terminal domain”, as used herein, refers to a region of a CSP polypeptide that corresponds to amino acids 273-397 of wild-type CSP sequence of Plasmodium falciparum (isolate 3D7) (SEQ ID NO: 1). [0281] C-terminal region: The term “C-terminal region”, as used herein, refers to a region of a CSP polypeptide that corresponds to amino acids 273-375 of wild-type CSP sequence (SEQ ID NO: 1). In some embodiments, a serine follows immediately after the C-terminal region. In some embodiments, a serine and a valine follow immediately after the C-terminal region. [0282] C-terminal region variant: The term “C-terminal region variant”, as used herein, refers to a C- terminal region that comprises one or more mutations as compared to amino acids 273-375 of wild-type CSP sequence (SEQ ID NO: 1). In some embodiments, one or more mutations are one or more substitution mutations. In some embodiments, one or more mutations comprise an indel. [0283] Central domain: The term “central domain”, as used herein, refers to a region of a CSP polypeptide that corresponds to amino acids 105-272 of wild-type CSP sequence (SEQ ID NO: 1). [0284] Characteristic portion: As used herein, the term “characteristic portion”, in the broadest sense, refers to a portion of a polypeptide or region thereof whose presence (or absence) correlates with presence (or absence) of a particular feature, attribute, or activity of the polypeptide or region thereof. In some embodiments, a characteristic portion of a polypeptide or region thereof is a portion that is found in the polypeptide or region thereof and in related polypeptide or region thereof that share the particular feature, attribute or activity, but not in those that do not share the particular feature, attribute or activity. In certain embodiments, a characteristic portion shares at least one functional characteristic with the intact polypeptide or region thereof. For example, in some embodiments, a “characteristic portion” of a polypeptide or region thereof is one that contains a continuous stretch of amino acids, or a collection of continuous stretches of amino acids, that together are characteristic of the polypeptide or region thereof. In some embodiments, each such continuous stretch generally contains at least 2, 5, 10, 15, 20, 50, or more amino acids. In general, a characteristic portion of a polypeptide or region thereof (e.g., CSP, its N terminal domain, its major repeat region etc.) is one that, in addition to the sequence and/or structural identity specified above, shares at least one functional characteristic with the relevant intact polypeptide or region thereof. In some embodiments, a characteristic portion may be biologically active. In some embodiments, a fragment as described herein can be a portion. Accordingly, in some embodiments, a characteristic fragment can be a “characteristic portion.” [0285] Combination therapy: As used herein, the term “combination therapy” refers to those situations in which a subject is simultaneously exposed to two or more therapeutic regimens (e.g., two or more therapeutic agents (e.g., two or more antibody agents)). In some embodiments, the two or more regimens may be administered simultaneously; in some embodiments, such regimens may be administered sequentially (e.g., all “doses” of a first regimen are administered prior to administration of any doses of a second regimen); in some embodiments, such agents are administered in overlapping dosing regimens. In some embodiments, administration of combination therapy may involve administration of one or more agent(s) or modality(ies) to a subject receiving the other agent(s) or modality(ies) in the combination. For clarity, combination therapy does not require that individual agents be administered together in a single composition (or even necessarily at the same time), although in some embodiments, two or more agents, or active moieties thereof, may be administered together in a combination composition. [0286] Comparable: As used herein, the term “comparable” refers to two or more agents, entities, situations, sets of conditions, etc., that may not be identical to one another but that are sufficiently similar to permit comparison there between so that one skilled in the art will appreciate that conclusions may reasonably be drawn based on differences or similarities observed. In some embodiments, comparable sets of conditions, circumstances, individuals, or populations are characterized by a plurality of substantially identical features and one or a small number of varied features. Those of ordinary skill in the art will understand, in context, what degree of identity is required in any given circumstance for two or more such agents, entities, situations, sets of conditions, etc. to be considered comparable. For example, those of ordinary skill in the art will appreciate that sets of circumstances, individuals, or populations are comparable to one another when characterized by a sufficient number and type of substantially identical features to warrant a reasonable conclusion that differences in results obtained or phenomena observed under or with different sets of circumstances, individuals, or populations are caused by or indicative of the variation in those features that are varied. [0287] Corresponding to: As used herein, the term “corresponding to” refers to a relationship between two or more entities. For example, the term “corresponding to” may be used to designate the position/identity of a structural element in a compound or composition relative to another compound or composition (e.g., to an appropriate reference compound or composition). For example, in some embodiments, a monomeric residue in a polymer (e.g., an amino acid residue in a polypeptide or a nucleic acid residue in a polynucleotide) may be identified as “corresponding to” a residue in an appropriate reference polymer. For example, those of ordinary skill will appreciate that, for purposes of simplicity, residues in a polypeptide are often designated using a canonical numbering system based on a reference related polypeptide, so that an amino acid “corresponding to” a residue at position 190, for example, need not actually be the 190th amino acid in a particular amino acid chain but rather corresponds to the residue found at 190 in the reference polypeptide; those of ordinary skill in the art readily appreciate how to identify “corresponding” amino acids. For example, those skilled in the art will be aware of various sequence alignment strategies, including software programs such as, for example, BLAST, CS-BLAST, CUSASW++, DIAMOND, FASTA, GGSEARCH/GLSEARCH, Genoogle, HMMER, HHpred/HHsearch, IDF, Infernal, KLAST, USEARCH, parasail, PSI-BLAST, PSI-Search, ScalaBLAST, Sequilab, SAM, SSEARCH, SWAPHI, SWAPHI-LS, SWIMM, or SWIPE that can be utilized, for example, to identify “corresponding” residues in polypeptide and/or nucleic acids in accordance with the present disclosure. Those of skill in the art will also appreciate that, in some instances, the term “corresponding to” may be used to describe an event or entity that shares a relevant similarity with another event or entity (e.g., an appropriate reference event or entity). To give but one example, a gene or protein in one organism may be described as “corresponding to” a gene or protein from another organism in order to indicate, in some embodiments, that it plays an analogous role or performs an analogous function and/or that it shows a particular degree of sequence identity or homology, or shares a particular characteristic sequence element. [0288] Dosing regimen: Those skilled in the art will appreciate that the term “dosing regimen” (or “therapeutic regimen”) may be used to refer to a set of unit doses (typically more than one) that are administered individually to a subject, typically separated by periods of time. In some embodiments, a given therapeutic agent has a recommended dosing regimen, which may involve one or more doses. [0289] Encode: As used herein, the term “encode” or “encoding” refers to sequence information of a first molecule that guides production of a second molecule having a defined sequence of nucleotides (e.g., a polyribonucleotide) or a defined sequence of amino acids. For example, a DNA molecule can encode an RNA molecule (e.g., by a transcription process that includes a DNA-dependent RNA polymerase enzyme). An RNA molecule can encode a polypeptide (e.g., by a translation process). Thus, a gene, a cDNA, or an RNA molecule encodes a polypeptide if transcription and translation of RNA corresponding to that gene produces the polypeptide in a cell or other biological system. In some embodiments, a coding region of a polyribonucleotide encoding a target antigen refers to a coding strand, the nucleotide sequence of which is identical to the polyribonucleotide sequence of such a target antigen. In some embodiments, a coding region of a polyribonucleotide encoding a target antigen refers to a non-coding strand of such a target antigen, which may be used as a template for transcription of a gene or cDNA. [0290] Expression: As used herein, the term “expression” of a nucleic acid sequence refers to the generation of a gene product from the nucleic acid sequence. In some embodiments, a gene product can be a transcript, e.g., a polyribonucleotide as provided herein. In some embodiments, a gene product can be a polypeptide. In some embodiments, expression of a nucleic acid sequence involves one or more of the following: (1) production of an RNA template from a DNA sequence (e.g., by transcription); (2) processing of an RNA transcript (e.g., by splicing, editing, etc.); (3) translation of an RNA into a polypeptide or protein; and/or (4) post-translational modification of a polypeptide or protein. [0291] Helper antigen: As used herein, the term “helper antigen” refers to an antigen that is included in a polypeptide comprising one or more CSP polypeptide regions or portion thereof, where the antigen is not derived from a CSP polypeptide. [0292] Heterologous: As used herein, the term “heterologous”, with respect to secretory signal or transmembrane region, refers to a secretory signal or transmembrane region from a virus or an organism other than Plasmodium. [0293] Homology: As used herein, the term “homology” or “homolog” refers to the overall relatedness between polynucleotide molecules (e.g., DNA molecules and/or RNA molecules) and/or between polypeptide molecules. In some embodiments, polynucleotide molecules (e.g., DNA molecules and/or RNA molecules) and/or polypeptide molecules are considered to be “homologous” to one another if their sequences are at least 15%, 20%, 25%, 30%, 35%, 40%, 45%, 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85%, 90%, 95%, or 99% identical. In some embodiments, polynucleotide molecules (e.g., DNA molecules and/or RNA molecules) and/or polypeptide molecules are considered to be “homologous” to one another if their sequences are at least 25%, 30%, 35%, 40%, 45%, 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85%, 90%, 95%, or 99% similar (e.g., containing residues with related chemical properties at corresponding positions). For example, as is well known by those of ordinary skill in the art, certain amino acids are typically classified as similar to one another as “hydrophobic” or “hydrophilic” amino acids, and/or as having “polar” or “non-polar” side chains. Substitution of one amino acid for another of the same type may often be considered a “homologous” substitution. [0294] Identity: As used herein, the term “identity” refers to the overall relatedness between polynucleotide molecules (e.g., DNA molecules and/or RNA molecules) and/or between polypeptide molecules. In some embodiments, polynucleotide molecules (e.g., DNA molecules and/or RNA molecules) and/or between polypeptide molecules are considered to be “substantially identical” to one another if their sequences are at least 80%, 85%, 90%, 95%, 96%, 97%, 98%, or 99% identical. Calculation of the percent identity of two nucleic acid or polypeptide sequences, for example, can be performed by aligning the two sequences for optimal comparison purposes (e.g., gaps can be introduced in one or both of a first and a second sequence for optimal alignment and non-identical sequences can be disregarded for comparison purposes). In certain embodiments, the length of a sequence aligned for comparison purposes is at least 30%, at least 40%, at least 50%, at least 60%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or substantially 100% of the length of a reference sequence. The nucleotides at corresponding positions are then compared. When a position in the first sequence is occupied by the same residue (e.g., nucleotide or amino acid) as the corresponding position in the second sequence, then the molecules are identical at that position. The percent identity between the two sequences is a function of the number of identical positions shared by the sequences, taking into account the number of gaps, and the length of each gap, which needs to be introduced for optimal alignment of the two sequences. The comparison of sequences and determination of percent identity between two sequences can be accomplished using a mathematical algorithm. For example, the percent identity between two nucleotide sequences can be determined using the algorithm of Meyers and Miller, 1989, which has been incorporated into the ALIGN program (version 2.0). In some exemplary embodiments, nucleic acid sequence comparisons made with the ALIGN program use a PAM120 weight residue table, a gap length penalty of 12 and a gap penalty of 4. The percent identity between two nucleotide sequences can, alternatively, be determined using the GAP program in the GCG software package using an NWSgapdna.CMP matrix. [0295] Increased, Induced, or Reduced: As used herein, these terms or grammatically comparable comparative terms, indicate values that are relative to a comparable reference measurement. For example, in some embodiments, an assessed value achieved with a provided composition (e.g., a pharmaceutical composition) may be “increased” relative to that obtained with a comparable reference composition. Alternatively or additionally, in some embodiments, an assessed value achieved in a subject may be “increased” relative to that obtained in the same subject under different conditions (e.g., prior to or after an event; or presence or absence of an event such as administration of a composition (e.g., a pharmaceutical composition) as described herein, or in a different, comparable subject (e.g., in a comparable subject that differs from the subject of interest in prior exposure to a condition, e.g., absence of administration of a composition (e.g., a pharmaceutical composition) as described herein.). In some embodiments, comparative terms refer to statistically relevant differences (e.g., that are of a prevalence and/or magnitude sufficient to achieve statistical relevance). Those skilled in the art will be aware, or will readily be able to determine, in a given context, a degree and/or prevalence of difference that is required or sufficient to achieve such statistical significance. In some embodiments, the term “reduced” or equivalent terms refers to a reduction in the level of an assessed value by at least 5%, at least 10%, at least 20%, at least 50%, at least 75% or higher, as compared to a comparable reference. In some embodiments, the term “reduced” or equivalent terms refers to a complete or essentially complete inhibition, i.e., a reduction to zero or essentially to zero. In some embodiments, the term “increased” or “induced” refers to an increase in the level of an assessed value by at least 10%, at least 20%, at least 30%, at least 40%, at least 50%, at least 80%, at least 100%, at least 200%, at least 500%, or higher, as compared to a comparable reference. [0296] In order: As used herein with reference to a polynucleotide or polyribonucleotide, “in order” refers to the order of features from 5' to 3' along the polynucleotide or polyribonucleotide. As used herein with reference to a polypeptide, “in order” refers to the order of features moving from the N-terminal-most of the features to the C- terminal-most of the features along the polypeptide. “In order” does not mean that no additional features can be present among the listed features. For example, if Features A, B, and C of a polynucleotide are described herein as being “in order, Feature A, Feature B, and Feature C,” this description does not exclude, e.g., Feature D being located between Features A and B. [0297] Isolated: The term “isolated” means altered or removed from the natural state. For example, a nucleic acid or a polypeptide naturally present in a living animal is not “isolated,” but the same nucleic acid or polypeptide partially or completely separated from the coexisting materials of its natural state is “isolated.” An isolated nucleic acid or protein can exist in substantially purified form, or can exist in a non-native environment such as, for example, a host cell. [0298] Junction: The term “junction”, as used herein, refers to a region of a CSP polypeptide that corresponds to amino acids 98-104 of wild-type CSP sequence (SEQ ID NO: 1). [0299] Junction region: The term “junction region”, as used herein, refers to a region of a CSP polypeptide that corresponds to amino acids 93-104 of wild-type CSP sequence (SEQ ID NO: 1). Typically, a junction region includes an R1 region (amino acids 93-97) and a junction (SEQ ID NO: 277) at positions 98-104. [0300] Junction region variant: The term “junction region variant”, as used herein, refers to a junction region that comprises one or more mutations as compared to amino acids 93-104 of wild-type CSP sequence (SEQ ID NO: 1). In some embodiments, one or more mutations are one or more substitution mutations. In some embodiments, one or more mutations comprise an indel. [0301] Linker: As used herein, the term “linker” refers to a portion of a polypeptide that connects different regions, portions, or antigens to one another. [0302] Lipid: As used herein, the terms “lipid” and “lipid-like material” are broadly defined as molecules which comprise one or more hydrophobic moieties or groups and optionally also one or more hydrophilic moieties or groups. Molecules comprising hydrophobic moieties and hydrophilic moieties are also typically denoted as amphiphiles. [0303] Major repeat region: As used herein, the term “major repeat region” refers to a region of a CSP polypeptide that corresponds to amino acids 129-272 of wild-type CSP sequence (SEQ ID NO: 1) and contains 35 repeats of the amino acid sequence NANP (SEQ ID NO: 230). The 35 repeats of the amino acid sequence NANP (SEQ ID NO: 230) are separated into two contiguous stretches, the first stretch containing 17 repeats of the amino acid sequence NANP (SEQ ID NO: 230) and second stretch containing 18 repeats of the amino acid sequence NANP (SEQ ID NO: 230) which flank an amino acid sequence of NVDP (SEQ ID NO: 229). A portion of the major repeat region contains at least the amino acid sequence NPNA (SEQ ID NO: 228). Preferably a portion of the major repeat region contains at least the amino acid sequences NANPNA (SEQ ID NO: 232) and NPNANP (SEQ ID NO: 231). As used herein, “repeat” in reference to sequence A refers to sequence A being present once, and “one or more repeats” of sequence A refers to sequence A being present one or more times. [0304] Merozoite stage specific Plasmodium antigen: As used herein, the term “merozoite stage specific Plasmodium antigen” refers to an antigen that is expressed during the merozoite stage of the Plasmodium life cycle. [0305] Minor repeat region: As used herein, the term “minor repeat region” refers to a region of a CSP polypeptide that corresponds to amino acids 105-128 of wild-type CSP sequence (SEQ ID NO: 1) and contains 3 repeats of the amino acid sequence NANPNVDP (SEQ ID NO: 223). A minor repeat region does not contain the amino acid sequence NPNA (SEQ ID NO: 228), and does not contain the amino acid sequence NANPNA (SEQ ID NO: 232) or NPNANP (SEQ ID NO: 231). As used herein, “repeat” in reference to sequence A refers to sequence A being present once, and three repeats of sequence A refers to sequence A being present three times. [0306] Multimerization region: As used herein, the term “multimerization region” refers to a region that directs assembly of multimers into a complex, where each multimer comprises a polypeptide associated with the multimerization region. [0307] N-terminal domain: As used herein, the term “N-terminal domain” refers to a region of a CSP polypeptide that corresponds to amino acids 19-104 of wild-type CSP sequence (SEQ ID NO: 1). [0308] N-terminal start region: As used herein, the term “N-terminal start region” refers to a region of a CSP polypeptide that corresponds to amino acids 19-31 of wild-type CSP sequence (SEQ ID NO:1). [0309] N-terminal end region: As used herein, the term “N-terminal end region” refers to a region of a CSP polypeptide that corresponds to amino acids 81-92 of wild-type CSP sequence (SEQ ID NO: 1). [0310] N-terminal region: As used herein, the term “N-terminal region” refers to a region of a CSP polypeptide that corresponds to amino acids 19-80 of wild-type CSP sequence (SEQ ID NO: 1). [0311] R1: The term “R1”, as used herein, refers to a region of a CSP polypeptide that corresponds to amino acids 93-97 of wild-type CSP sequence (SEQ ID NO: 1). [0312] RNA lipid nanoparticle: As used herein, the term “RNA lipid nanoparticle” refers to a nanoparticle comprising at least one lipid and RNA molecule(s), e.g., one or more polyribonucleotides as provided herein. In some embodiments, an RNA lipid nanoparticle comprises at least one cationic amino lipid. In some embodiments, an RNA lipid nanoparticle comprises at least one cationic amino lipid, at least one helper lipid, and at least one polymer- conjugated lipid (e.g., PEG-conjugated lipid). In various embodiments, RNA lipid nanoparticles as described herein can have an average size (e.g., Z-average) of about 100 nm to 1000 nm, or about 200 nm to 900 nm, or about 200 nm to 800 nm, or about 250 nm to about 700 nm. In some embodiments of the present disclosure, RNA lipid nanoparticles can have a particle size (e.g., Z-average) of about 30 nm to about 200 nm, or about 30 nm to about 150 nm, about 40 nm to about 150 nm, about 50 nm to about 150 nm, about 60 nm to about 130 nm, about 70 nm to about 110 nm, about 70 nm to about 100 nm, about 80 nm to about 100 nm, about 90 nm to about 100 nm, about 70 to about 90 nm, about 80 nm to about 90 nm, or about 70 nm to about 80 nm. In some embodiments, an average size of lipid nanoparticles is determined by measuring the average particle diameter. In some embodiments, RNA lipid nanoparticles may be prepared by mixing lipids with RNA molecules described herein. [0313] Neutralization: As used herein, the term “neutralization” refers to an event in which binding agents such as antibodies bind to a biological active site of a parasite such as a receptor binding protein, thereby inhibiting the parasitic infection of cells. In some embodiments, the term “neutralization” refers to an event in which binding agents eliminate or significantly reduce ability of infecting cells. [0314] Nucleic acid/ Polynucleotide: As used herein, the term “nucleic acid” refers to a polymer of at least 10-nucleotides or more. In some embodiments, a nucleic acid is or comprises DNA. In some embodiments, a nucleic acid is or comprises RNA. In some embodiments, a nucleic acid is or comprises polypeptide nucleic acid (PNA). In some embodiments, a nucleic acid is or comprises a single stranded nucleic acid. In some embodiments, a nucleic acid is or comprises a double-stranded nucleic acid. In some embodiments, a nucleic acid comprises both single and double-stranded portions. In some embodiments, a nucleic acid comprises a backbone that comprises one or more phosphodiester linkages. In some embodiments, a nucleic acid comprises a backbone that comprises both phosphodiester and non-phosphodiester linkages. For example, in some embodiments, a nucleic acid may comprise a backbone that comprises one or more phosphorothioate or 5'-N-phosphoramidite linkages and/or one or more polypeptide bonds, e.g., as in a “polypeptide nucleic acid”. In some embodiments, a nucleic acid comprises one or more, or all, natural residues (e.g., adenine, cytosine, deoxyadenosine, deoxycytidine, deoxyguanosine, deoxythymidine, guanine, thymine, uracil). In some embodiments, a nucleic acid comprises on or more, or all, non- natural residues. In some embodiments, a non-natural residue comprises a nucleoside analog (e.g., 2- aminoadenosine, 2-thiothymidine, inosine, pyrrolo-pyrimidine, 3 -methyl adenosine, 5-methylcytidine, C-5 propynyl- cytidine, C-5 propynyl-uridine, 2-aminoadenosine, C5-bromouridine, C5-fluorouridine, C5-iodouridine, C5-propynyl- uridine, C5 -propynyl-cytidine, C5-methylcytidine, 2-aminoadenosine, 7-deazaadenosine, 7-deazaguanosine, 8- oxoadenosine, 8-oxoguanosine, 6-O-methylguanine, 2-thiocytidine, methylated bases, intercalated bases, and combinations thereof). In some embodiments, a non-natural residue comprises one or more modified sugars (e.g., 2'-fluororibose, ribose, 2'-deoxyribose, arabinose, and hexose) as compared to those in natural residues. In some embodiments, a nucleic acid has a nucleotide sequence that encodes a functional gene product such as an RNA or polypeptide. In some embodiments, a nucleic acid has a nucleotide sequence that comprises one or more introns. In some embodiments, a nucleic acid may be prepared by isolation from a natural source, enzymatic synthesis (e.g., by polymerization based on a complementary template, e.g., in vivo or in vitro), reproduction in a recombinant cell or system, or chemical synthesis. In some embodiments, a nucleic acid is at least 3, 4, 5, 6, 7, 8, 9, 10, 15, 20, 25, 30, 35, 40, 45, 50, 55, 60, 65, 70, 75, 80, 85, 90, 95, 100, 110, 120, 130, 140, 150, 160, 170, 180, 190, 200, 225, 250, 275, 300, 325, 350, 375, 400, 425, 450, 475, 500, 600, 700, 800, 900, 1000, 1500, 2000, 2500, 3000, 3500, 4000, 4500, 5000, 5500, 6000, 6500, 7000, 7500, 8000, 8500, 9000, 9500, 10,000, 10,500, 11,000, 11,500, 12,000, 12,500, 13,000, 13,500, 14,000, 14,500, 15,000, 15,500, 16,000, 16,500, 17,000, 17,500, 18,000, 18,500, 19,000, 19,500, or 20,000 or more residues or nucleotides long. [0315] Pharmaceutically effective amount: The term “pharmaceutically effective amount” or “therapeutically effective amount” refers to the amount which achieves a desired reaction or a desired effect alone or together with further doses. In the case of the treatment of a particular disease (e.g., malaria), a desired reaction in some embodiments relates to inhibition of the course of the disease (e.g., malaria). In some embodiments, such inhibition may comprise slowing down the progress of a disease (e.g., malaria) and/or interrupting or reversing the progress of the disease (e.g., malaria). In some embodiments, a desired reaction in a treatment of a disease (e.g., malaria) may be or comprise delay or prevention of the onset of a disease (e.g., malaria) or a condition (e.g., a malaria associated condition). An effective amount of a composition (e.g., a pharmaceutical composition) described herein will depend, for example, on disease (e.g., malaria) or a condition (e.g., a malaria associated condition) to be treated, the severity of such a disease (e.g., malaria) or a condition (e.g., a malaria associated condition), individual parameters of the patient, including, e.g., age, physiological condition, size and weight, the duration of treatment, the type of an accompanying therapy (if present), the specific route of administration and similar factors. Accordingly, doses of a composition (e.g., a pharmaceutical composition) described herein may depend on various of such parameters. In the case that a reaction in a patient is insufficient with an initial dose, higher doses (or effectively higher doses achieved by a different, more localized route of administration) may be used. [0316] Polypeptide: As used herein, the term “polypeptide” refers to a polymeric chain of amino acids. In some embodiments, a polypeptide has an amino acid sequence that occurs in nature. In some embodiments, a polypeptide has an amino acid sequence that does not occur in nature. In some embodiments, a polypeptide has an amino acid sequence that is engineered in that it is designed and/or produced through action of the hand of man. In some embodiments, a polypeptide may comprise or consist of natural amino acids, non-natural amino acids, or both. In some embodiments, a polypeptide may comprise or consist of only natural amino acids or only non-natural amino acids. In some embodiments, a polypeptide may comprise D-amino acids, L-amino acids, or both. In some embodiments, a polypeptide may comprise only D-amino acids. In some embodiments, a polypeptide may comprise only L-amino acids. In some embodiments, a polypeptide may include one or more pendant groups or other modifications, e.g., modifying or attached to one or more amino acid side chains, at the polypeptide’s N-terminus, at the polypeptide’s C-terminus, or any combination thereof. In some embodiments, such pendant groups or modifications comprise acetylation, amidation, lipidation, methylation, pegylation, etc., including combinations thereof. In some embodiments, a polypeptide may be cyclic, and/or may comprise a cyclic portion. In some embodiments, a polypeptide is not cyclic and/or does not comprise any cyclic portion. In some embodiments, a polypeptide is linear. In some embodiments, a polypeptide may be or comprise a stapled polypeptide. In some embodiments, the term “polypeptide” may be appended to a name of a reference polypeptide, activity, or structure; in such instances it is used herein to refer to polypeptide that share the relevant activity or structure and thus can be considered to be members of the same class or family of polypeptide. For each such class, the present specification provides and/or those skilled in the art will be aware of exemplary polypeptide within the class whose amino acid sequences and/or functions are known; in some embodiments, such exemplary polypeptide are reference polypeptide for the polypeptide class or family. In some embodiments, a member of a polypeptide class or family shows significant sequence homology or identity with, shares a common sequence motif (e.g., a characteristic sequence element) with, and/or shares a common activity (in some embodiments at a comparable level or within a designated range) with a reference polypeptide of the class; in some embodiments with all polypeptide within the class). For example, in some embodiments, a member polypeptide shows an overall degree of sequence homology or identity with a reference polypeptide that is at least about 30-40%, and is often greater than about 50%, 60%, 70%, 80%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or more and/or includes at least one region (e.g., a conserved region that may in some embodiments be or comprise a characteristic sequence element) that shows very high sequence identity, often greater than 90% or even 95%, 96%, 97%, 98%, or 99%. Such a conserved region usually encompasses at least 3-4 and often up to 35 or more amino acids; in some embodiments, a conserved region encompasses at least one stretch of at least 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35 or more contiguous amino acids. In some embodiments, a relevant polypeptide may comprise or consist of a fragment of a parent polypeptide. In some embodiments, a polypeptide is a Plasmodium polypeptide construct described herein. A Plasmodium polypeptide construct is a polypeptide that includes one or more Plasmodium proteins, or one or more portions thereof. In some embodiments, a Plasmodium polypeptide construct described herein includes at least one region of Plasmodium CSP or a portion thereof. In some embodiments, a Plasmodium polypeptide construct additionally includes one or more additional amino acid sequences, such as a secretory signal (e.g., a heterologous secretory signal), a transmembrane region (e.g., a heterologous transmembrane region), a helper antigen, a multimerization region, and/or a linker, as described herein. [0317] Prevent: As used herein, the term “prevent” or “prevention” when used in connection with the occurrence of a disease, disorder, and/or condition, refers to reducing the risk of developing the disease, disorder and/or condition and/or to delaying onset of one or more characteristics or symptoms of the disease, disorder or condition. Prevention may be considered complete when onset of a disease, disorder or condition has been delayed for a predefined period of time. In some embodiments, prevention refers to reducing the risk of developing clinical malaria. [0318] Reference: As used herein, the term “reference” describes a standard or control relative to which a comparison is performed. For example, in some embodiments, an agent, animal, individual, population, sample, sequence or value of interest is compared with a reference or control agent, animal, individual, population, sample, sequence or value. In some embodiments, a reference or control is tested and/or determined substantially simultaneously with the testing or determination of interest. In some embodiments, a reference or control is a historical reference or control, optionally embodied in a tangible medium. Typically, as would be understood by those skilled in the art, a reference or control is determined or characterized under comparable conditions or circumstances to those under assessment. Those skilled in the art will appreciate when sufficient similarities are present to justify reliance on and/or comparison to a particular possible reference or control. [0319] Ribonucleic acid (RNA) or Polyribonucleotide: As used herein, the term “ribonucleic acid,” “RNA,” or “polyribonucleotide” refers to a polymer of ribonucleotides. In some embodiments, an RNA is single stranded. In some embodiments, an RNA is double stranded. In some embodiments, an RNA comprises both single and double stranded portions. In some embodiments, an RNA can comprise a backbone structure as described in the definition of “Nucleic acid / Polynucleotide” above. An RNA can be a regulatory RNA (e.g., siRNA, microRNA, etc.), or a messenger RNA (mRNA). In some embodiments, an RNA is a mRNA. In some embodiments, where an RNA is a mRNA, an RNA typically comprises at its 3' end a poly(A) region. In some embodiments, where an RNA is a mRNA, an RNA typically comprises at its 5' end an art-recognized cap structure, e.g., for recognizing and attachment of a mRNA to a ribosome to initiate translation. In some embodiments, an RNA is a synthetic RNA. Synthetic RNAs include RNAs that are synthesized in vitro (e.g., by enzymatic synthesis methods and/or by chemical synthesis methods). In some embodiments, a polyribonucleotide encodes a polypeptide, which is preferably is a Plasmodium polypeptide construct. [0320] Ribonucleotide: As used herein, the term “ribonucleotide” encompasses unmodified ribonucleotides and modified ribonucleotides. For example, unmodified ribonucleotides include the purine bases adenine (A) and guanine (G), and the pyrimidine bases cytosine (C) and uracil (U). Modified ribonucleotides may include one or more modifications including, but not limited to, for example, (a) end modifications, e.g., 5' end modifications (e.g., phosphorylation, dephosphorylation, conjugation, inverted linkages, etc.), 3' end modifications (e.g., conjugation, inverted linkages, etc.), (b) base modifications, e.g. , replacement with modified bases, stabilizing bases, destabilizing bases, or bases that base pair with an expanded repertoire of partners, or conjugated bases, (c) sugar modifications (e.g., at the 2' position or 4' position) or replacement of the sugar, and (d) internucleoside linkage modifications, including modification or replacement of the phosphodiester linkages. The term “ribonucleotide” also encompasses ribonucleotide triphosphates including modified and non-modified ribonucleotide triphosphates. [0321] Secretory signal: As used herein, the term “secretory signal” refers to an amino acid sequence motif that targets associated polypeptide for translocation to a secretory pathway. [0322] Subject: As used herein, the term “subject” refers to an organism to be administered with a composition described herein, e.g., for experimental, diagnostic, prophylactic, and/or therapeutic purposes. Typical subjects include animals (e.g., mammals such as mice, rats, rabbits, non-human primates, domestic pets, etc.) and humans. In preferred embodiments, a subject is a human subject. In some embodiments, a subject is suffering from a disease, disorder, or condition (e.g., malaria and/or a malaria-associated condition). In some embodiments, a subject is susceptible to a disease, disorder, or condition (e.g., malaria and/or a malaria-associated condition). In some embodiments, a subject displays one or more symptoms or characteristics of a disease, disorder, or condition (e.g., malaria and/or a malaria-associated condition). In some embodiments, a subject displays one or more non- specific symptoms of a disease, disorder, or condition (e.g., malaria and/or a malaria-associated condition). In some embodiments, a subject does not display any symptom or characteristic of a disease, disorder, or condition (e.g., malaria and/or a malaria-associated condition). In some embodiments, a subject is someone with one or more features characteristic of susceptibility to or risk of a disease, disorder, or condition (e.g., malaria and/or a malaria- associated condition). In some embodiments, a subject is a patient. In some embodiments, a subject is an individual to whom diagnosis and/or therapy is and/or has been administered. [0323] Suffering from: An individual who is “suffering from” a disease, disorder, and/or condition (e.g., malaria and/or a malaria-associated condition) has been diagnosed with and/or displays one or more symptoms of a disease, disorder, and/or condition. [0324] Susceptible to: An individual who is “susceptible to” a disease, disorder, and/or condition (e.g., malaria and/or a malaria-associated condition) is one who has a higher risk of developing the disease, disorder, and/or condition (e.g., malaria and/or a malaria-associated condition) than does a member of the general public. In some embodiments, an individual who is susceptible to a disease, disorder and/or condition (e.g., malaria and/or a malaria-associated condition) may not have been diagnosed with the disease, disorder, and/or condition (e.g., malaria and/or a malaria-associated condition). In some embodiments, an individual who is susceptible to a disease, disorder, and/or condition (e.g., malaria and/or a malaria-associated condition) may exhibit symptoms of the disease, disorder, and/or condition (e.g., malaria and/or a malaria-associated condition). In some embodiments, an individual who is susceptible to a disease, disorder, and/or condition (e.g., malaria and/or a malaria-associated condition) may not exhibit symptoms of the disease, disorder, and/or condition (e.g., malaria and/or a malaria-associated condition). In some embodiments, an individual who is susceptible to a disease, disorder, and/or condition (e.g., malaria and/or a malaria-associated condition) will develop the disease, disorder, and/or condition (e.g., malaria and/or a malaria- associated condition). In some embodiments, an individual who is susceptible to a disease, disorder, and/or condition (e.g., malaria and/or a malaria-associated condition) will not develop the disease, disorder, and/or condition (e.g., malaria and/or a malaria-associated condition). [0325] Therapy: The term “therapy” refers to an administration or delivery of an agent or intervention that has a therapeutic effect and/or elicits a desired biological and/or pharmacological effect (e.g., has been demonstrated to be statistically likely to have such effect when administered to a relevant population). In some embodiments, a therapeutic agent or therapy is any substance that can be used to alleviate, ameliorate, relieve, inhibit, prevent, delay onset of, reduce severity of, and/or reduce incidence of one or more symptoms or features of a disease, disorder, and/or condition (e.g., malaria and/or a malaria-associated condition). In some embodiments, a therapeutic agent or therapy is a medical intervention that can be performed to alleviate, relieve, inhibit, present, delay onset of, reduce severity of, and/or reduce incidence of one or more symptoms or features of a disease, disorder, and/or condition. [0326] Transmembrane region: As used herein, the term “transmembrane region” refers to a region of a polypeptide that spans a biological membrane, such as the plasma membrane of a cell. [0327] Treat: As used herein, the term “treat,” “treatment,” or “treating” refers to any method used to partially or completely alleviate, ameliorate, relieve, inhibit, prevent, delay onset of, reduce severity of, and/or reduce incidence of one or more symptoms or features of a disease, disorder, and/or condition (e.g., malaria and/or a malaria-associated condition). Treatment may be administered to a subject who does not exhibit signs of a disease, disorder, and/or condition (e.g., malaria and/or a malaria-associated condition). In some embodiments, treatment may be administered to a subject who exhibits only early signs of the disease, disorder, and/or condition (e.g., malaria and/or a malaria-associated condition), for example for the purpose of decreasing the risk of developing pathology associated with the disease, disorder, and/or condition. In some embodiments, treatment may be administered to a subject at a later-stage of disease, disorder, and/or condition (e.g., malaria and/or a malaria- associated condition). [0328] Variant: As used herein, the term “variant” refers to a molecule that shows significant structural (e.g., primary or secondary) identity with a reference molecule but differs structurally from the reference molecule. For example, a variant polypeptide or nucleic acid may differ from a reference polypeptide or nucleic acid as a result of one or more differences in amino acid or nucleotide sequence and/or one or more differences in chemical moieties (e.g., carbohydrates, lipids, phosphate groups) that are covalently components of the polypeptide or nucleic acid (e.g., that are attached to the polypeptide or nucleic acid backbone). DETAILED DESCRIPTION OF CERTAIN EMBODIMENTS I. Malaria [0329] Malaria is a mosquito-borne infectious disease caused by single-celled eukaryotic Plasmodium parasites that are transmitted by the bite of Anopheles spp. mosquitoes (Phillips, M., et al. Malaria. Nat Rev Dis Primers 3, 17050, 2017, which is incorporated herein by reference in its entirety). Mosquitoes that transmit malaria must have been infected through a previous blood meal taken from an infected subject (e.g., a human). When a mosquito bites an infected subject a small amount of blood is taken in containing malaria parasites. The infected mosquito can then subsequently bite a non-infected subject, infecting the subject. [0330] Malaria remains one of the most serious infectious diseases, causing approximately 200 million clinical cases and 500,000-600,000 deaths annually. Although significant effort has been invested in developing therapeutic treatments for malaria, many malaria parasites have developed resistance to available therapeutics. According to Malaria Eradication Research Agenda Initiative, malaria eradication will only be achievable through effective vaccination. [0331] In 2015, the European Medicines Agency gave a positive review to a malaria vaccine candidate known as “RTS,S,” a milestone in malaria vaccine development. In 2019, the World Health Organization launched pilot programs that provide RTS,S to children at least 5 months of age in parts of three sub-Saharan African countries. RTS,S/AS01 is an adjuvanted protein subunit vaccine that consists of a portion of the major repeat region and the C- terminus of CSP from Plasmodium falciparum fused to the Hepatitis B surface antigen (HBsAg). The vaccine is a mix of this PfCSP-HBsAg compound with HBsAg that forms virus-like particles (RTS,S/AS01; Mosquirix™). RTS,S is administered according to a regimen that requires four doses: an initial 3-dose schedule given at least 1 month apart, and a 4th dose 15-18 months after dose 3 (see, for example, Vandoolaeghe & Schuerman Expert Rev Vaccines. 15:1481, 2016; PATH_MVI_RTSS_Fact Sheet_042019, each of which is incorporated herein by reference in its entirety). Reports indicate that RTS,S protects approximately 30% to 50% of children from clinical disease over 18 months. RTS,S has been reported to induce protective antibody and CD4+ T-cell responses, but only negligible CD8+ T cell responses (see, for example, Moris et al. Hum Vaccin Immunother 14:17, 2018, which is incorporated herein by reference in its entirety). Phase III studies of RTS,S delivered as a three-dose series with a booster after 1 yr (year) showed moderate vaccine efficacy in children aged 5 to 17 months preventing 36% of clinical malaria cases over the full study period with a median follow-up of 4 yrs, with a range of 20% in high to 66% in low transmission settings. Furthermore, published literature suggests that protection wanes over time including reports of potential negative efficacy after 5 yrs in children with high malaria exposure (Olotu et al. 2016, N. Engl. J. Med. 374:2519-29, which is incorporated herein by reference in its entirety). Thus, an effective malaria vaccine remains an unmet medical need of critical importance for global health. A. Life Cycle [0332] During a blood meal, infected mosquitos inject, along with their anticoagulating saliva, sporozoites known as the liver stage of Plasmodium spp. Sporozoites journey through the skin to the lymphatics and into hepatocytes of the liver. This journey happens very quickly; it can be complete within only a few minutes (Sinnis et al., Parasitol Int. 2007 Sep;56(3):171-8, which is incorporated herein by reference in its entirety). This is a time known to be a bottleneck of Malaria infection most favorable for therapeutic intervention, as only a small number (thought to be a few hundred at maximum) of sporozoites are injected by the mosquito, with only fraction of that number establishing infection in the liver and developing into mature live-stage parasites (Flores-Garcia et al., mBio. 2018 Nov 20;9(6):e02194-18, which is incorporated herein by reference in its entirety). Thus, a subject whose immune system is primed to clear sporozoites before they enter hepatocytes can efficiently clear an infection. [0333] One particular challenge associated with clearing a malarial infection during this bottleneck is that the most abundant and immunogenic protein on the sporozoite surface, the circumsporozoite protein (CSP), is only exposed to the immune system in small quantities and for short duration of time due to the variably low inoculum from the mosquito and the kinetics of hepatocyte infection after inoculation. After liver infection is established, the parasite differentiates into a stage which no longer expresses CSP and instead has a different mosaic of surface antigens. Furthermore, due to the density and close proximity of neighboring CSPs on the surface of the parasite coupled with the bi-valency of antibodies, binding of antibodies to CSP can produce a phenomenon referred to as CSP precipitation reaction, whereby antibodies can crosslink neighboring CSP and cause them to precipitate and shed from the parasite surface, leaving a trail of precipitated antibody bound CSP that the parasite can replace through its normal CSP translocation process (Livingstone et al., Sci Rep 11, 5318 (2021); Steward et al., J Protozool. 1991 Jul- Aug; 38(4):411-21, each of which is incorporated herein by reference in its entirety). [0334] When moving from an inoculation site in the skin to the liver, sporozoites traverse host cells (Mota et al., Science 2001 Jan 5;291(5501):141-4). Sporozoites traverse different types of host cells at the dermis, including fibroblasts and phagocytes (Amino et al., Cell Host Microbe.2008 Feb 14;3(2):88-96, which is incorporated herein by reference in its entirety), and the liver sinusoidal barrier, containing liver endothelial cells and Kupffer cells (Frevert et al., PLoS Biol 3(6): e192.2005, which is incorporated herein by reference in its entirety) and sinusoidal endothelial cells (Tavares et al., J Exp Med 2013 May 6;210(5):905-15, which is incorporated herein by reference in its entirety), in order to gain access to hepatocytes. Sporozoites preferentially traverse cells with low-sulfated heparin sulfate proteoglycans (HSPGs) but preferentially invade cells with high-sulfated HSPGs (Coppi et al., Cell Host & Microbe 2, 316–327, November 2007, which is incorporated herein by reference in its entirety). [0335] Cell traversal was first observed as non-phagocytic entry of P. berghei sporozoites into macrophages followed by “escape” from these cells (Vanderberg et al., J. Euk. Microbiol.37:528-536, 1990, which is incorporated herein by reference in its entirety). The biochemical, biophysical, and stepwise processes of traversal are still being explored. However, it has been suggested by electron microscopy that host cell rupture occurs upon entry and exit from the host cell (Mota et al., 2001; Tavares et al., 2013, each of which is incorporated herein by reference in its entirety). It has also been shown that P. yoelii sporozoites can enter hepatocytes via a transient vacuole and that host membrane rupture occurs upon cell exit rather than cell entry (Risco-Castillo et al., Cell Host Microbe 2015 Nov 11;18(5):593-603, which is incorporated herein by reference in its entirety). [0336] Sporozoites also traverse hepatocytes before establishing a productive hepatocyte infection (Mota et al., 2001, which is incorporated herein by reference in its entirety). Several possibilities emerged as to why this occurs. The first hypothesis suggested that migration through hepatocytes primes parasites for invasion by activating apical exocytosis (Mota et al., Nat Med 2002 Nov;8(11):1318-22, which is incorporated herein by reference in its entirety). The second theory suggested that traversal releases hepatocyte growth factor (HGF), making neighboring hepatocytes more susceptible to infection (Carrolo et al., Nat Med.2003 Nov;9(11):1363-9, which is incorporated herein by reference in its entirety). Lastly, other studies suggest that it takes some time for sporozoites to switch off the machinery for traversal and activate invasion machinery (Amino et al., 2008, Coppi et al., 2007, each of which is incorporated herein by reference in its entirety), and that traversal primarily functions to penetrate cell barriers and avoid phagocytosis en route to the liver (Amino et al., 2008, Coppi et al., 2007, Tavares et al., 2013, each of which is incorporated herein by reference in its entirety). [0337] Although it has been shown that sporozoites traverse human cells (Behet et al., Malar J 2014 Apr 5;13:136; Cha et al., J Exp Med 2015 Aug 24;212(9):1391-403; Dumoulin et al., PLoS One 2015 Jun 12;10(6):e0129623; van Schaijk et al., PLoS ONE, 3 (10). e35492008, each of which is incorporated herein by reference in its entirety), the molecular basis for the traversal process is largely unstudied. Antibodies against circumsporozoite protein (CSP) impair traversal (Dumoulin et al., 2015, which is incorporated herein by reference in its entirety), but this is likely due to inhibition of motility rather than a direct effect (Cha et al., J Exp Med 2016 Sep 19;213(10):2099-112, which is incorporated herein by reference in its entirety). Furthermore, antibodies induced by chloroquine prophylaxis with sporozoites interfere with cell traversal, and these may also target CSP (Behet et al., 2014, which is incorporated herein by reference in its entirety). Recently it was shown that glyceraldehyde 3- phosphate dehydrogenase (GAPDH) on the parasite surface interacts with CD68 on Kupffer cells during traversal (Cha et al., 2015, Cha et al., 2016, each of which is incorporated herein by reference in its entirety). [0338] In rodent malaria parasites such as P. berghei, two sporozoite microneme proteins have been identified that appear to be essential for cell traversal: sporozoite microneme protein essential for cell traversal 1 (SPECT1) (Ishino et al., PLoS Biol., 2 (2004), pp. 77-84, which is incorporated herein by reference in its entirety) and sporozoite microneme protein essential for cell traversal 2 (SPECT2) (Ishino et al., Cell. Microbiol., 7 (2005), pp. 199- 208, which is incorporated herein by reference in its entirety). SPECT2 can also be called perforin-like protein 1 (PLP1) (Kaiser et al., Mol. Biochem. Parasitol., 133 (2004), pp.15-26, which is incorporated herein by reference in its entirety). Even though genetic disruption of SPECT1 or SPECT2 rendered sporozoites unable to traverse murine cells, sporozoites still invaded hepatocytes in vitro (Ishino et al., 2004, Ishino et al., 2005, each of which is incorporated herein by reference in its entirety). When injected into rodents, sporozoites lacking SPECT1 or SPECT2 were impaired for liver infection, but a small number of sporozoites could still establish liver infection that resulted in subsequent patency. However, depletion of Kupffer cells allowed mutants to establish liver infection at levels comparable with wild-type parasites (Ishino et al., 2004, Ishino et al., 2005, each of which is incorporated herein by reference in its entirety). This data suggests that traversal by rodent-infecting sporozoites is important for navigating through the sinusoidal layer, but not for hepatocyte invasion, malarial exoerythrocytic forms development, or growth within erythrocytes (Ishino et al., 2004, Ishino et al., 2005, each of which is incorporated herein by reference in its entirety). [0339] The ortholog of SPECT2 in P. yoelii, PLP1, has been shown to play a role in cell traversal. Although this protein is not required for hepatocyte entry, it plays a role in egress from transient vacuoles during traversal (Risco- Castillo et al., 2015, each of which is incorporated herein by reference in its entirety). Thus, sporozoites that infect rodents can traverse host cells by generating a vacuole at the entry step and use a perforin-like protein (e.g., SPECT2/PLP1) to escape from this compartment and/or a host cell, during cell exit. [0340] Once sporozoites have invaded liver cells, they differentiate into merozoites, a replicative form of the parasite capable of lysing hepatocytes after multiple rounds of replication. Within a few days, a few hundred sporozoites can become hundreds of thousands of merozoites. When infected liver cells rupture, they release the merozoites into the bloodstream, where they invade red blood cells and begin the asexual reproductive stage, which is the symptomatic stage of the disease. Within a small number of days, millions of merozoites can be present in blood. [0341] Malaria symptoms typically develop 4-8 days after initial red blood cell invasion. Replication cycle of merozoites within the red blood cells continues for 36-72 hours, until hemolysis, releasing the merozoites for another round of red blood cell infection. Thus, in synchronous infections (infections that originate from a single infectious bite), fever occurs every 36–72 hours, when infected red blood cells lyse and release endotoxins en masse. [0342] Plasmodium spp. parasites gain entry into red blood cells through specific ligand–receptor interactions mediated by proteins on the surface of the parasite that interact with receptors on the host erythrocyte (mature red blood cell) or reticulocyte (immature red blood cell), whereas P. falciparum can invade and replicate in erythrocytes and reticulocytes, P. vivax and other species predominantly invade reticulocytes, which are less abundant than erythrocytes. Most of the erythrocyte-binding proteins or reticulocyte-binding proteins that have been associated with invasion are redundant or are expressed as a family of variant forms; however, for P. falciparum, two essential red blood cell receptors (basigin and complement decay-accelerating factor (also known as CD55)) have been identified. [0343] Plasmodium vivax and Plasmodium ovale can also enter a dormant state in the liver, the hypnozoite. [0344] Merozoites released from red blood cells can invade other red blood cells and continue to replicate, or in some cases, they differentiate into male or female gametocytes. Gametocytes concentrate in skin capillaries and are then taken up by the mosquito vector in another blood meal. In the gut of the mosquito, each male gametocyte produces eight microgametes after three rounds of mitosis; the female gametocyte matures into a macrogamete. Male microgametes are motile forms with flagellae and seek the female macrogamete. The male and female gametocytes fuse, forming a diploid zygote, which elongates into an ookinete; this motile form secretes a chitinase in order to enter the peritrophic membrane and traverse the midgut epithelium to the basal lateral side of the midgut, establishing itself in the basal lamina as an oocyst. Oocysts mature over 14-15 days, undergoing cycles of replication to form sporozoites that are ultimately liberated into the hemocoel, an environment rich in sugars and substrates beneficial to the parasite’s survival. Thousands of sporozoites can form from a single oocyst and become randomly distributed throughout the hemocoel. These sporozoites are motile and rapidly destroy the hemolymph, with only approximately 20% successfully invading the salivary gland. Following invasion of the salivary gland, sporozoites are re-programmed via an unknown mechanism to prepare for liver invasion. Evidence of this reprogramming has been demonstrated by the inability of midgut sporozoites (directly from oocysts) to invade hepatocytes, and also by the fact that sporozoites which have successfully invaded a salivary gland are unable to do re-invade another salivary gland if presented one. Salivary gland sporozoites alter mosquito behavior and salivary gland function, as less saliva is produced resulting in an increase in mosquito probing behavior, increasing the chances of transmission to a human host via a mosquito bite. [0345] Some drugs that prevent Plasmodium spp. invasion or proliferation in the liver have prophylactic activity, drugs that block the red blood cell stage are required for the treatment of the symptomatic phase of the disease, and compounds that inhibit the formation of gametocytes or their development in the mosquito (including drugs that kill mosquitoes feeding on blood) are transmission-blocking agents (Phillips, et al. Malaria. Nat Rev Dis Primers 3, 17050 (2017), which is incorporated herein by reference in its entirety). [0346] Some proteins that are expressed exclusively by the parasite in specific phases of its life cycle, while other proteins are expressed and may play a role in multiple life cycle phases. B. Genome [0347] Since completion of the first sequence of P. falciparum 3D7 genome in 2002, genomic research on malaria parasites has rapidly advanced. Except for a short diploid phase after fertilization in the mosquito midgut, Plasmodium parasites are haploid throughout their life cycle. The genomes of different species range from 20 to 35 megabases, contain 1 4 chromosomes, a circular plastid genome of approximately 35 kilobases, and multiple copies of a 6 kilobase mitochondrial DNA. Comparison of genomes from different species showed that homologous genes are often found in synthetic blocks arranged in different orders among different chromosomes. [0348] The adenine-thymine (AT) content of Plasmodium spp. can also be very different, e.g., ^80% AT in P. falciparum, P. reichenowi, and P. gallinaceum; ^75% AT in rodent malaria parasites; and ^60% AT in P. vivax, P. knowlesi, and P. cynomolgi. AT content is often higher in introns and intergenic noncoding regions than in protein- coding exons, with an average of 80.6% AT for the whole P. falciparum genome versus 86.5% for noncoding sequences. The high AT content of P. falciparum reflects large numbers of low-complexity regions, simple sequence repeats, and microsatellites, as well as a highly skewed codon usage bias. Polymorphisms of AT-rich repeats provide abundant markers for linkage mapping of drug resistance genes and for tracing the evolution and structure of parasite populations. [0349] Malaria parasite genomes carry multigene families that serve important roles in parasite interactions with their hosts, including, for example, antigenic variation, signaling, protein trafficking, and adhesion. Among the gene families, genes encoding P. falciparum erythrocyte membrane protein 1 (PfEMP1) have been studied most extensively. Each individual P. falciparum parasite carries a unique set of 50 to 150 copies of the var gene in its genome, where switches of gene expression can produce antigenic variation. PfEMP1 plays an important role in the pathogenesis of clinical developments such as in cerebral and placental malaria, in which it mediates the cytoadherence of infected red blood cells (iRBCs; infected erythrocytes) in the deep tissues. Different PfEMP1 molecules bind to various host molecules, including α2-macroglobulin, CD36, chondroitin sulfate A (CSA), complement 1q, CR1, E-selectins and P-selectins, endothelial protein C receptor (EPCR), heparan sulfate, ICAM1, IgM, IgG, PECAM1, thrombospondin (TSP), and VCAM1. Such binding leads to activation of various host inflammatory responses. Hemoglobinopathies, including the hemoglobin C and hemoglobin S trait conditions, interfere with PfEMP1 display in knob structures of the iRBCs. This poor display of PfEMP1 on the host cell surface offers protection against malaria by reducing the cytoadherence and activation of inflammatory processes that promote the development of severe disease. [0350] Members of the large Plasmodium interspersed repeat (pir) multigene family are named differently by parasite species, for example, yir in P. yoelii, bir in P. berghei, vir in P. vivax. Several P. falciparum gene families (stevor, rif, and PfMC-2TM) are classified with pir by their similar gene structures, which characteristically include a short first exon, a long second exon, and a third exon encoding a transmembrane domain. In a recent study, the pir genes from P. chabaudi (cir) were shown to be expressed in different cellular locations, within and on the surface of iRBCs, and in merozoites. Malaria parasites devote large portions of their genomes to gene families that ensure evasion of host immune defenses and protection of molecular processes essential to infection. These families emphasize the importance of research on their roles in parasite-host interactions and virulence, despite the difficulties inherent to their investigation. [0351] An additional, exemplary polymorphic gene family comprises a group of 14 genes encoding proteins with six cysteines (6-Cys). These proteins often localize on the parasite surface interacting with host proteins and are expressed at different parasite developmental stages.6-Cys proteins also demonstrate diverse functions and have been shown to play roles in, for example, parasite fertilization, mating interactions, evasion of immune responses, and invasion of hepatocytes. The proteins expressed in asexual stages are generally polymorphic and/or under selection, suggesting that they could be targets of the host immune response; however, their functions in parasite development remain largely unknown. [0352] Plasmodium genomes can be highly polymorphic. Early studies demonstrated polymorphisms involving tens to hundreds of kilobases and that the chromosome structure in P. falciparum is largely conserved in central regions but extensively polymorphic is both length and sequence near the telomeres. Much of the subtelomeric variation was explained by recombination within blocks of repetitive sequences and families of genes. [0353] The frequency of simple sequence repeats (microsatellites) in P. falciparum is estimated to be approximately one polymorphic microsatellite per kb DNA. Without wishing to be bound by any one theory, this high rate may reflect the AT-rich nature of the genome. Microsatellites seem to be less frequent in other Plasmodium species that have genomes with lower AT contents. In addition to the highly polymorphic and repetitive structure of Plasmodium genomes, there are also large numbers of Single Nucleotide Polymorphisms (SNPs) and Copy Number Variations (CNVs) (Su et al., Plasmodium Genomics and Genetics: New Insights into Malaria Pathogenesis, Drug Resistance, Epidemiology, and Evolution. Clin Microbiol Rev.2019 Jul 31;32(4), which is incorporated herein by reference in its entirety). C. Plasmodium Proteins [0354] Plasmodium parasites are known to express various proteins at different stages of their lifecycles. Exemplary Plasmodium proteins are described below, and exemplary amino acid sequences are provided in Table 2. [0355] Circumsporozoite protein (CSP) is a multifunctional protein that is involved in Plasmodium life cycle, as it is required for the formation of sporozoites in the mosquito midgut, the release of sporozoites from the oocyst, invasion of salivary glands, attachment of sporozoites to hepatocytes in the liver, and sporozoite invasion of hepatocytes (see, e.g., Zhao et al. (2016) PLoS ONE 11(8): e0161607, which is incorporated herein by reference in its entirety). CSP is present in all Plasmodium species, and although variation exists in the amino acid sequence across species, the overall domain structure of a central repeat region and nonrepeat flanking regions is well conserved (see, e.g., Zhao et al. (2016) PLoS ONE 11(8): e0161607; Wahl et al. (2022) J. Exp. Med.219: e20201313, each of which is incorporated herein by reference in its entirety). CSP sequences are known (see, e.g., UniProt accession numbers A0A2L1CF52, A0A2L,1CF88, C6FGZ3, C6FH2,7 C6FHG7, M1V060, M1V0A3, M1V0B0, M1V0C4, M1V0E0, M1V9I4, M1VFN9, M1VKZ2, P02893, Q5EIJ9, Q5EIK2, Q5EIK8, Q5EIL3, Q5EIL5, Q5EIL8, Q5R2L2, Q7K740, Q8I9G5, Q8I9J3, Q8I9J4), and Table 1 includes exemplary sequences for CSP P. falciparum isolates from Asia, South America and Africa. Table 1: Exemplary Sequences Encoding CSP P. falciparum isolates from Asia, South America and Africa

[0356] An exemplary wild-type CSP polypeptide amino sequence from Plasmodium falciparum isolate 3D7 is presented in Table 2 as SEQ ID NO: 1, and includes the following: a secretory signal (amino acids 1-18); an N- terminal domain (amino acids 19-104); a junction region (amino acids 93-104), a central domain (amino acids 105- 272); and a C-terminal domain (amino acids 273-397). In exemplary SEQ ID NO: 1, the N-terminal domain includes an N-terminal region (amino acids 19-80); an N-terminal end region (amino acids 81-92); and a junction region (amino acids 93-104). In exemplary SEQ ID NO: 1, the junction region includes an R1 region (amino acids 93-97) and a junction (SEQ ID NO: 277) at positions 98-104. In exemplary SEQ ID NO: 1, the central domain includes a minor repeat region (amino acids 105-128) and a major repeat region (amino acids 129-272). In exemplary SEQ ID NO: 1, the minor repeat region includes three repeats of the amino acid sequence NANPNVDP (SEQ ID NO: 223). In exemplary SEQ ID NO: 1, the major repeat region includes 35 repeats of the amino acid sequence NANP (SEQ ID NO: 230), wherein 35 repeats of the amino acid sequence NANP (SEQ ID NO: 230) are separated into two contiguous stretches, and wherein one stretch includes 17 repeats of the amino acid sequence NANP (SEQ ID NO: 230) and one includes 18 repeats of the amino acid sequence NANP (SEQ ID NO: 230) which flank an amino acid sequence of NVDP (SEQ ID NO: 229). The major repeat region includes the amino acid sequences NPNANP (SEQ ID NO: 231) and NANPNA (SEQ ID NO: 232). In exemplary SEQ ID NO: 1, the C-terminal domain includes a C-terminal region (amino acids 273-375), a serine-valine (amino acids 376-377), and a transmembrane domain (amino acids 378-397). In exemplary SEQ ID NO: 1, the C-terminal region includes a Th2R region (amino acids 314-327) and a Th3R region (amino acids 352-363). Exemplary CSP amino acid sequence is provided in Table 2. [0357] Upregulated in infective sporozoites gene 3 (UIS3) is a membrane-bound protein localized to sporozoite parasitophorous vacuolar membrane (PVM) in infected hepatocytes. UIS3 was shown to interact with liver fatty acid- binding protein (L-FABP) and be involved in fatty acid and/or lipid import during phases of Plasmodium growth (see, e.g., Sharma et al., J Biol Chem. 2008 Aug 29; 283(35): 24077–24088; Mikolajczak et al., Int J Parasitol.2007 Apr;37(5):483-9, each of which is incorporated herein by reference in its entirety). [0358] After sporozoite invasion of host liver cells, there is synthesis of vital Plasmodium structural features (e.g., parasitophorous vacuolar membrane). During hepatocytic stages, the Plasmodium relies on host fatty acids for rapid synthesis of its membranes (see, e.g., Sharma et al., J Biol Chem.2008 Aug 29; 283(35): 24077–24088, which is incorporated herein by reference in its entirety). UIS3 insertion in the PVM provides Plasmodium a method to import essential fatty acids and/or lipids during rapid sporozoites growth phases (see, e.g., Sharma et al., J Biol Chem. 2008 Aug 29; 283(35): 24077–24088, which is incorporated herein by reference in its entirety). [0359] Immunization with UIS3-deficient Plasmodium berghei sporozoites protected against malaria in rodent malaria model (see, e.g., Mueller et al., Nature. 2005 Jan 13;433(7022):164-7, which is incorporated herein by reference in its entirety). UIS3-deficient Plasmodium berghei can start the transformation process in the liver; however, they show severe defects during transformation into trophozoites (see, e.g., Mueller et al., Nature. 2005 Jan 13;433(7022):164-7, which is incorporated herein by reference in its entirety). UIS3-deficient Plasmodium berghei are also unable to develop into mature liver schizonts and therefore abort malaria infection within the liver itself (see, e.g., Mueller et al., Nature. 2005 Jan 13;433(7022):164-7, which is incorporated herein by reference in its entirety). Further, it was previously demonstrated that UIS3 derived from Plasmodium berghei and UIS3 derived from Plasmodium falciparum exhibited a low (i.e. 34%) amino acid sequence identity (see, e.g., Mueller et al., Nature. 2005 Jan 13;433(7022):164-7, which is incorporated herein by reference in its entirety). [0360] Plasmodium UIS3 sequences are known (see, e.g., UniProt accession number A0A509ARS3, A0A1C6YLP3, Q8IEU1, A0A384KLI1, A0A1G4H423, A0A077YB01, Q9NFU4, each of which is incorporated herein by reference in its entirety). Exemplary UIS3 amino acid sequence is provided in Table 2. [0361] Plasmodium falciparum early transcribed membrane protein 10.3 (ETRAMP10.3) is an approximately 10 kDa protein and member of the early transcribed membrane proteins multigene family, a family which is conserved across Plasmodium species and includes proteins located in the parasitophorous vacuole. Several ETRAMP proteins are specific to P. falciparum and not found in Plasmodium species that infect other organisms. ETRAMP10.3 is one example, which is expressed in both liver and blood stage P. falciparum parasites. ETRAMP10.3 transcription has been found to peak during the transition from ring to trophozoite stages of P. falciparum blood stage infection in a human host. ETRAMP10.3 localizes to the parasitophorous vacuole and is exported to a host erythrocyte during blood stage infection. Although ETRAMP10.3 is sometimes referred to as Upregulated in Infectious Sporozoites gene 4 (UIS4), ETRAMP10.3 is understood to be an ortholog of UIS4 on the basis of synteny and structural similarity. However, ETRAMP10.3 is not a functional ortholog of UIS4 and may play a different biological role. Although the biological function of ETRAMP10.3 has not yet been completely resolved, localization to vesicular structures in the host erythrocyte suggests a role in host-parasite interaction or in remodeling of infected erythrocyte. ETRAMP10.3 appears to play a key role in the Plasmodium life cycle. When ETRAMP10.3 is deleted, the deletion can lead to the disruption of liver-stage development in mice and asexual blood stage progression. [0362] Although the terms “UIS4” and “ETRAMP10.3” in the literature are sometimes used to refer to different proteins, in context of the present disclosure, the terms “UIS4” and “ETRAMP10.3” interchangeably to refer to ETRAMP10.3. [0363] Plasmodium ETRAMP10.3 sequences are known (see, e.g., UniProt accession number Q8IJM9, which is incorporated herein by reference in its entirety). An exemplary ETRAMP10.3 amino acid sequence is provided in Table 2. [0364] Liver specific protein 1 (LISP-1) is expressed during Plasmodium development in hepatocytes and localized to the parasitophorous vacuolar membrane (PVM) (see, e.g., Ishino et al., Cell Microbiol.2009 Sep; 11(9): 1329–1339, which is incorporated herein by reference in its entirety). LISP-1 was shown to be expressed at high levels during late liver stages development and to be involved in PVM breakdown and subsequent merozoite release (see, e.g., Ishino et al., Cell Microbiol. 2009 Sep; 11(9): 1329–1339, which is incorporated herein by reference in its entirety). [0365] Intracellular Plasmodium deficient in LISP-1 develop into hepatic merozoites and display normal infectivity to erythrocytes (see, e.g., Ishino et al., Cell Microbiol. 2009 Sep; 11(9): 1329–1339, which is incorporated herein by reference in its entirety). However, LISP1-deficient liver-stage Plasmodium do not rupture PVM and remain trapped inside hepatocytes (see, e.g., Ishino et al., Cell Microbiol.2009 Sep; 11(9): 1329–1339, which is incorporated herein by reference in its entirety). [0366] Plasmodium LISP-1 sequences are known (see, e.g., UniProt accession number A0A2I0C2X6, Q8ILR5, each of which is incorporated herein by reference in its entirety). Exemplary LISP-1 amino acid sequence is provided in Table 2. [0367] Liver specific protein 2 (LISP-2) contains a modified 6-cys domain and is expressed during Plasmodium development in hepatocytes (see, e.g., Orito et al., Mol Microbiol.2013 Jan;87(1):66-79, which is incorporated herein by reference in its entirety). LISP-2 was shown to be expressed by liver stages Plasmodium, exported to hepatocytes, and be distributed throughout the host cell, including the nucleus (see, e.g., Orito et al., Mol Microbiol. 2013 Jan;87(1):66-79, which is incorporated herein by reference in its entirety). [0368] Intracellular Plasmodium deficient in LISP2 do not mature effectively during merozoites development (see, e.g., Orito et al., Mol Microbiol.2013 Jan;87(1):66-79, which is incorporated herein by reference in its entirety). [0369] Plasmodium LISP-2 sequences are known (see, e.g., UniProt accession number A0A2I0BZR4, Q8I1X6, Q9U0D4, each of which is incorporated herein by reference in its entirety). Exemplary LISP-2 amino acid sequence is provided in Table 2. [0370] Thrombospondin-related adhesion protein (TRAP) contains an N-terminal domain that is commonly referred to as von Willebrand factor A domain, although it is most similar to an integrin I domain because it contains a metal ion-dependent adhesion site (MIDAS) with a bound Mg²⁺ ion that is required for sporozoite motility in vitro and infection in vivo (see, e.g., Lu et al., PLoS One.2020; 15(1): e0216260, which is incorporated herein by reference in its entirety). The I domain is inserted in an extensible β-ribbon and followed by a thrombospondin repeat (TSR) domain, a proline-rich segment at the C-terminus, a single-pass transmembrane domain, and a cytoplasmic domain (see, e.g., Lu et al., PLoS One.2020; 15(1): e0216260, which is incorporated herein by reference in its entirety). Sequence analysis of the proline-rich segment revealed the presence of SH3-domain binding PxxP motifs in Plasmodium TRAPs (Akhouri et al., Malar J.2008 Apr 22;7:63. doi: 10.1186/1475-2875-7-63, which is incorporated herein by reference in its entirety). [0371] TRAP is stored in the micronemes and becomes surface exposed at the sporozoite anterior tip when parasite comes in contact with host cells (Akhouri et al., Malar J. 2008 Apr 22;7:63. doi: 10.1186/1475-2875-7-63, which is incorporated herein by reference in its entirety). TRAP also plays an important role in liver cell invasion of sporozoites by helping sporozoites in gliding motility and in recognition of host receptors on the mosquito salivary gland and hepatocytes (Akhouri et al., Malar J. 2008 Apr 22;7:63. doi: 10.1186/1475-2875-7-63, which is incorporated herein by reference in its entirety). [0372] Plasmodium TRAP sequences are known (see, e.g., UniProt accession numbers A0A5Q2EXK8, A0A5Q2EZD7, A0A5Q2F1F6, A0A5Q2F2B8, A0A5Q2F2H6, A0A5Q2F4G9, O76110, P16893, Q01507, Q26020, Q76NM2, W8VNB6, each of which is incorporated herein by reference in its entirety), and exemplary TRAP amino acid sequence is provided in Table 2. [0373] Liver-stage-associated protein (LSAP-1) has been shown to be found mainly at the periphery of the intracellular hepatic parasite throughout its development, but not in blood stage parasites and possibly in minor quantities in salivary gland sporozoites (see, e.g., Siau et al., PLoS Pathog.2008 Aug 8;4(8):e1000121, which is incorporated herein by reference in its entirety). LSAP-1 is among the most abundant transcripts in the salivary gland transcriptome but has not been detected in proteomic surveys of sporozoites. Rather, expression has only been detected only in liver stages (see, e.g., Siau et al., PLoS Pathog. 2008 Aug 8;4(8):e1000121, which is incorporated herein by reference in its entirety). [0374] Plasmodium LSAP-1 sequences are known (see, e.g., UniProt accession number Q8I632, W7JR53, each of which is incorporated herein by reference in its entirety). Exemplary LSAP-1 amino acid sequence is provided in Table 2. [0375] Like LSAP-1, LSAP-2 is also among the most abundant transcripts in the salivary gland transcriptome but has not been detected in proteomic surveys of sporozoites. LSAP-2 has shown some efficacy as a vaccine when combined with other antigens. See, e.g., Halbroth et al., Infect Immun.2020 Jan 22;88(2):e00573-19. doi: 10.1128/IAI.00573-19. Print 2020 Jan 22, which is incorporated herein by reference in its entirety. [0376] Plasmodium LSAP-2 sequences are known (see, e.g., UniProt accession number Q8I632, W7JR53, each of which is incorporated herein by reference in its entirety). Exemplary LSAP-2 amino acid sequence is provided in Table 2. [0377] Liver-Stage Antigen 1 (LSA-1) is expressed after Plasmodium have invaded hepatocytes and antigen accumulates in the parasitophorous vacuole (see, e.g., Tucker, K. et al., 2016, 'Pre-Erythrocytic Vaccine Candidates in Malaria', in A. J. Rodriguez-Morales (ed.), Current Topics in Malaria, IntechOpen, London.10.5772/65592, each of which is incorporated herein by reference in its entirety). The function of LSA-1 remains currently not known (see, e.g., Tucker, K. et al., 2016, 'Pre-Erythrocytic Vaccine Candidates in Malaria', in A. J. Rodriguez-Morales (ed.), Current Topics in Malaria, IntechOpen, London. 10.5772/65592, which is incorporated herein by reference in its entirety). [0378] LSA-1 is a 230 kDa preerythrocytic stage protein containing a large central region consisting of over eighty 17 amino acid residue repeat units flanked by highly conserved C- and N-terminal regions (Richie, T.L. and Parekh, F.K. (2009) Malaria, which is incorporated herein by reference in its entirety). In Vaccines for Biodefense and Emerging and Neglected Diseases (Barrett, A.D.T. and Stanberry L.R., eds), pp. 1309–1364, Elsevier, which is incorporated herein by reference in its entirety). LSA1 is expressed only by liver stage Plasmodium and not by sporozoites (Richie, T.L. and Parekh, F.K. (2009) Malaria, which is incorporated herein by reference in its entirety). In Vaccines for Biodefense and Emerging and Neglected Diseases (Barrett, A.D.T. and Stanberry L.R., eds), pp. 1309– 1364, Elsevier, which is incorporated herein by reference in its entirety). The repeat region results in significant variation of the protein between strains of Plasmodium falciparum (see, e.g., Tucker, K. et al., 2016, 'Pre-Erythrocytic Vaccine Candidates in Malaria', in A. J. Rodriguez-Morales (ed.), Current Topics in Malaria, IntechOpen, London. 10.5772/65592, which is incorporated herein by reference in its entirety). [0379] Plasmodium LSA-1 sequences are known (see, e.g., UniProt accession number Q25886, Q25887, Q25893, Q26028, Q9GTX5, O96125, each of which is incorporated herein by reference in its entirety). Exemplary LSA-1 amino acid sequence is provided in Table 2. [0380] Liver stage antigen 3 (LSA-3) is a 200-kDa protein that is composed of three nonrepeating regions (NR- A, NR-B, and NR-C) flanking two short repeat regions and one long repeat region (see, e.g., Tucker, K. et al., 2016, 'Pre-Erythrocytic Vaccine Candidates in Malaria', in A. J. Rodriguez-Morales (ed.), which is incorporated herein by reference in its entirety), Current Topics in Malaria, IntechOpen, London. 10.5772/65592, which is incorporated herein by reference in its entirety). The nonrepeat regions are well conserved across geographically diverse strains of Plasmodium falciparum (see, e.g., Tucker, K. et al., 2016, 'Pre-Erythrocytic Vaccine Candidates in Malaria', in A. J. Rodriguez-Morales (ed.), Current Topics in Malaria, IntechOpen, London. 10.5772/65592, which is incorporated herein by reference in its entirety). The most significant variation is in the repeating regions due to organization and number of repeating subunits rather than composition of the repeating regions (see, e.g., Tucker, K. et al., 2016, 'Pre-Erythrocytic Vaccine Candidates in Malaria', in A. J. Rodriguez-Morales (ed.), Current Topics in Malaria, IntechOpen, London. 10.5772/65592, which is incorporated herein by reference in its entirety). [0381] Recently, in vitro data has shown that antibodies against LSA-3 (in particular, the C-terminal portion of LSA-3) may provide some protection (see, e.g., Morita et al, Sci Rep.2017 Apr 5;7:46086. doi: 10.1038/srep46086, which is incorporated herein by reference in its entirety). [0382] Plasmodium LSA-3 sequences are known (see, e.g., UniProt accession number C7DU21, C7DU22, C7DU23, C7DU24, C7DU25, C7DU26, C7DU27, C7DU28, C7DU29, C7DU32, C7DU33, C7DU34, C7DU36, C7DU37, C7DU38, C7DU39, C7DU40, Q8I042, Q8I0A5, Q8I0D0, Q8IFR1, Q8IFR2, Q8IFR3, Q8IFR4, Q8IFR5, Q8IFR6, Q8IFR7, Q8IFR8, Q8IFR9, Q8IFS0, Q8IFS1, Q8IFS2, Q8IFS3, Q8IFS4, Q8IFS5, Q8IFS6, Q8IFS7, Q8IFS8, Q8IFS9, Q8IFT0, Q8IFT1, Q8IFT2, Q8IFT3, Q8IFT4, Q9U0N9, Q9U0P0, A0A2I0BVD6, A0PFM9, O96275, each of which is incorporated herein by reference in its entirety). Exemplary LSA-3 amino acid sequence is provided in Table 2. Table 2: Exemplary amino acid sequences

II. Combinations [0383] The present disclosure provides combinations of polyribonucleotides that can be used to express one or more Plasmodium polypeptide constructs encoding at least two Plasmodium polypeptides or antigenic portions thereof, wherein the at least two Plasmodium polypeptides or antigenic portions thereof are expressed during different stages of the Plasmodium life cycle. In some embodiments, a combination as described herein comprises one or more polyribonucleotides that encode one or more polypeptides or antigenic portions thereof that are expressed during the Plasmodium sporozoite stage (e.g., shortly after a Plasmodium parasite has entered a subject and before the Plasmodium parasite has infected a hepatocyte), and one or more polypeptides or antigenic portions thereof that are expressed during the Plasmodium liver stage (e.g., after a Plasmodium parasite has entered a hepatocyte). [0384] In a preferred embodiment, a combination as described herein comprises one or more polyribonucleotides that encode one or more Plasmodium liver stage polypeptides or antigenic portions thereof (e.g., that elicit a T cell response) and one or more polyribonucleotides that encode one or more Plasmodium sporozoite stage (e.g., initial sporozoite stage) polypeptides or antigenic portions thereof (e.g., CSP). In some preferred embodiments, one or more Plasmodium liver stage polypeptides or antigenic portions thereof comprises between 2 to 20 liver stage polypeptides or antigenic portions thereof (e.g., antigenic portions that induce a T cell response). [0385] In some embodiments, a combination as described herein comprises one or more polyribonucleotides that encode one or more Plasmodium T-cell string polypeptide constructs as described herein and one or more polyribonucleotides that encode one or more Plasmodium CSP polypeptide constructs as described herein. [0386] In some embodiments, a combination as described herein comprises a first polyribonucleotide that encodes a Plasmodium T-cell string polypeptide construct as described herein and a second polyribonucleotide that encodes a Plasmodium CSP polypeptide construct as described herein. In some embodiments, a combination as described herein comprises a first polyribonucleotide that encodes a first Plasmodium T-cell string polypeptide construct as described herein, a second polyribonucleotide that encodes a second Plasmodium T-cell string polypeptide construct as described herein, and a third polyribonucleotide that encodes a Plasmodium CSP polypeptide construct as described herein. [0387] In some embodiments, a combination comprises a first pharmaceutical composition and a second pharmaceutical composition. In some embodiments, a first pharmaceutical composition comprises a first polyribonucleotide, wherein the first polyribonucleotide encodes a Plasmodium T-cell string polypeptide. In some embodiments, a second pharmaceutical composition comprises a second polyribonucleotide, wherein the first polyribonucleotide encodes a Plasmodium CSP polypeptide. In some embodiments, a first pharmaceutical composition and a second pharmaceutical composition are the same pharmaceutical composition. In some embodiments, a first pharmaceutical composition and a second pharmaceutical composition are different pharmaceutical compositions. [0388] In some embodiments, a combination comprises a first pharmaceutical composition, a second pharmaceutical composition, and a third pharmaceutical composition. In some embodiments, a first pharmaceutical composition comprises a first polyribonucleotide, wherein the first polyribonucleotide encodes a first Plasmodium T- cell string polypeptide. In some embodiments, a second pharmaceutical composition comprises a second polyribonucleotide, wherein the second polyribonucleotide encodes a second Plasmodium T-cell string polypeptide. In some embodiments, a third pharmaceutical composition comprises a third polyribonucleotide, wherein the third polyribonucleotide encodes a Plasmodium CSP polypeptide. In some embodiments, a first pharmaceutical composition, a second pharmaceutical composition, and a third pharmaceutical composition are the same pharmaceutical composition. In some embodiments, a first pharmaceutical composition, a second pharmaceutical composition, and a third pharmaceutical composition are different pharmaceutical compositions. In some embodiments, a first pharmaceutical composition and a second pharmaceutical composition are the same pharmaceutical composition. In some embodiments, (i) a first pharmaceutical composition or a second pharmaceutical composition and (ii) a third pharmaceutical composition are the same pharmaceutical composition. [0389] Descriptions of exemplary Plasmodium T-cell string polypeptide constructs and exemplary Plasmodium CSP polypeptide constructs are provided below. A. Plasmodium T-Cell String Polypeptide Constructs [0390] The present disclosure, among other things, utilizes RNA technologies as a modality to express one or more Plasmodium T-cell string polypeptide constructs (also referred to as “Plasmodium T-cell string polypeptides,” “malaria T-cell string polypeptide constructs” or “malarial T-cell peptide string constructs”). Plasmodium T-cell string polypeptide constructs as described herein can include one or more T-cell antigens from one or more Plasmodium polypeptide, or one or more portions thereof, (e.g., one or more antigenic fragments thereof) as described herein. In some embodiments, a Plasmodium T-cell string polypeptide construct as described herein comprises one or more Plasmodium liver stage antigens that elicit a T cell response. As is understood in the art, a “T-cell antigen” as described herein can induce a T cell response in a subject or model system. In some embodiments, a Plasmodium T- cell string polypeptide construct that targets the liver stage of a Plasmodium infection includes polypeptides or antigenic portions thereof that are expected to be both of relatively high abundance in infected hepatocytes and elicit T cell response(s). Polyribonucleotides as described herein encoding Plasmodium T-cell string polypeptide constructs, as well as Plasmodium T-cell string polypeptide constructs described herein, are designed to deliver a polypeptide to a subject, and in turn, for protein degradation and processing for presentation within the subject so that the subject raises an immune response (e.g., T cell response(s)). Methods to determine the presence of a T-cell response are well known in the art and described in the examples. In a preferred embodiment, Plasmodium T-cell string polypeptide constructs as described herein include more than one T-cell antigen and/or epitope from Plasmodium liver stage polypeptides or one or more portions thereof. In some preferred embodiments, one or more Plasmodium liver stage polypeptides or antigenic portions thereof comprises between 2 to 20 liver stage polypeptides or antigenic portions thereof (e.g., antigenic portions that induce a T cell response). In some embodiments, a Plasmodium T-cell string polypeptide construct comprises 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19 or 20, preferably 4, 5, 6, 7, 8, 9, 10, 11 or 12 different liver stage polypeptides or antigenic portions thereof (e.g., which each are capable of eliciting a T-cell response). [0391] For example, in some embodiments, a Plasmodium T-cell string polypeptide construct includes one or more Plasmodium T-cell antigens from CSP, LSA-1 (e.g., LSA-1(a), LSA-1(b)), TRAP, LSAP2, UIS3, ETRAMP10.3, LISP-1, LISP-2, LSA-3, EXP1, LSAP1 and/or polypeptide regions or portions thereof (e.g., one or more antigenic fragments thereof). In some embodiments, a Plasmodium T-cell string polypeptide construct comprises between about 10 amino acids and about 1200 amino acids, e.g., between about 10 amino acids and about 1100 amino acids, e.g., between about 10 amino acids and about 1000 amino acids, e.g., between about 10 amino acids and about 750 amino acids, e.g., between about 25 amino acids and about 500 amino acids. In some embodiments, a Plasmodium T-cell string polypeptide construct comprises about 10, about 15, about 20, about 25, about 50, about 75, about 100, about 150, about 200, about 250, about 300, about 350, about 400, about 450, about 500, about 550, about 600, about 650, about 700, about 750, about 800, about 850, about 900, about 950, about 1000, about 1050, about 1100, about 1150, or about 1200 amino acids. In some embodiments, a Plasmodium T-cell string polypeptide construct additionally includes one or more additional amino acid sequences, such as a secretory signal (e.g., a heterologous secretory signal), a transmembrane region (e.g., a heterologous transmembrane region), a trafficking signal, and/or a linker, as described herein. 1. Selection of T-cell Antigens [0392] In some embodiments, a T-cell antigen utilized in a Plasmodium T-cell string polypeptide construct described herein includes Plasmodium protein sequences identified and/or characterized by one or more of: - HLA-I or HLA-II binding (e.g., to HLA allele(s) present in a relevant population) - HLA ligandomics data confirmed by mass spectrometry - Relatively high expression - Sequence conservation - Expression during the early liver stage of parasite lifecycle - Localization to the parasitophorous vaculous membrane - Serum reactivity - Immunogenicity (e.g., presence of one or more B-cell and/or T-cell epitopes; evidence of ability to induce sterile protection in model systems including, e.g., humans, non-human primates, and/or mice). - Absence of sequences 8 amino acids and greater that overlap with human proteome unless 6 or more amino acids are from a linker sequence. [0393] In some embodiments, such characteristics are experimentally or computationally assessed. In some embodiments, such characteristics are assessed by consultation with published reports. [0394] For example, in some embodiments, HLA-I and/or HLA-II binding is experimentally assessed; in some embodiments it is predicted. In some embodiments, predicted HLA-I or HLA-II binding is assessed using an algorithm such as neonmhc 1 and/or neonmhc2, which predict and/or characterize likelihood of MHC class I and MHC class II binding, respectively. Alternatively or additionally, in some embodiments, an MHC-polypeptide presentation prediction algorithm or MHC-polypeptide presentation predictor is or comprises NetMHCpan or NetMHCIIpan. In some embodiments, a hidden Markov model approach may be utilized for MHC-polypeptide presentation prediction and/or characterization. In some embodiments, the polypeptide prediction model MARIA may be utilized. In some embodiments, NetMHCpan is not utilized to predict or characterize likelihood of MHC binding for polypeptides as described herein. In some embodiments, the polypeptide prediction model MARIA may be utilized. In some embodiments, NetMHCIIpan is not utilized to predict or characterize likelihood of MHC binding for polypeptides as described herein. In some embodiments, neither NetMHCpan nor NetMHCIIpan is utilized to predict or characterize likelihood of MHC binding for polypeptides as described herein. In some embodiments, an MHC-polypeptide presentation prediction algorithm or MHC-polypeptide presentation predictor is or comprises RECON® (Real-time Epitope Computation for ONcology), which offers high quality MHC-polypeptide presentation prediction based on expression, processing and binding capabilities. See, for example, Abelin et al., Immunity 21:315, 2017; Abelin et al., Immunity 15:766, 2019, each of which is incorporated herein by reference in its entirety. [0395] In some embodiments, HLA binding and/or ligandomics assessments can consider the geographic region of subjects to be immunized. For example, in some embodiments, HLA allelic diversity can be considered. In some embodiments, T cell antigens comprise polypeptides (e.g., epitopes) expected or determined, when considered together, to bind to a significant percentage (e.g., at least 60%, 65%, 70%, 75%, 80%, 85%, 90%, 95%, or more) of HLA alleles expected or known to be present in a relevant region or population. In some embodiments, T cell antigens comprise polypeptides expected or determined, when considered together, to bind to the most prevalent (e.g., the 1, 2, 3, 4, 5, 6, 7, 8, 9, or 10 most prevalent, or at least 1, 2, 3, 4, or 5 of the 10 most prevalent, etc.) HLA alleles expected or known to be present in a relevant region or population). [0396] In some embodiments, expression level is experimentally determined (e.g., in a model system or in infected humans). In some embodiments, expression level is a reported level (e.g., in a published or presented report). In some embodiments, expression level is assessed as RNA (e.g., via RNASeq). In some embodiments (and typically preferably), expression levels is assessed as protein. [0397] In some embodiments, sequence conservation is assessed, for example, using publicly available sequence evaluation software (such as, for example, multiple sequence alignment programs MAFFT, Clustal Omega, etc.). In some embodiments, sequence conservation is determined by consultation with published resources (e.g., sequences). In some embodiments, sequence conservation includes consideration of currently or recently detected strains (e.g., in an active outbreak). [0398] In some embodiments, surface exposure is assessed by reference to publicly available database and/or software. In some embodiments, surface exposure is assessed by reference to publicly available data, e.g., as described in Swearingen et al., “Interrogating the Plasmodium Sporozoite Surface: Identification of Surface-Exposed Proteins and Demonstration of Glycosylation on CSP and TRAP by Mass Spectrometry-Based Proteomics” PLoS Pathog (2016), the content of which is incorporated herein by reference for the purposes described herein. [0399] In some embodiments, serum reactivity is assessed by contacting serum samples from infected individuals with polypeptide including sequences of interest (e.g., as may be displayed via, for example, phage display or polypeptide array, etc.; see, for example, Whittemore et al PlosOne, 2016, which is incorporated herein by reference in its entirety). In some embodiments, serum reactivity is assessed by consultation with literature reports and or database data indicating serum-recognized sequences. [0400] In some embodiments, assessment of immunoreactivity and/or of presence of an epitope may be or comprise consultation with the Immune Epitope Database (IEDB) which those skilled in the art will be aware is a freely available resource funded by NIAID that catalogs experimental data on antibody and T cell epitopes (see iedb.org). [0401] In some embodiments, ability to induce sterile protection is assessed, for example, as described in one or more of Schofield et al. “γ Interferon, CD8+ T cells and antibodies required for immunity to malaria sporozoites” Nature 330, 664–666 (1987); Weiss et al. (1988). “CD8+ T cells (cytotoxic/suppressors) are required for protection in mice immunized with malaria sporozoites” Proc. Natl. Acad. Sci. U.S.A. 85, 573–576; Romero et al. “Cloned cytotoxic T cells recognize an epitope in the circumsporozoite protein and protect against malaria.” Nature 341, 323–326 (1989); Rodrigues et al. (1991) “CD8+ cytolytic T cell clones derived against the Plasmodium yoelii circumsporozoite protein protect against malaria.” Int. Immunol. 3, 579–585; Chakravarty et al. “CD8+ T lymphocytes protective against malaria liver stages are primed in skin-draining lymph nodes.” Nat Med. 2007 Sep;13(9):1035-41. Epub 2007 Aug 19., each of which is incorporated herein by reference in its entirety). [0402] In some embodiments, T cell antigens are characterized by dendritic cell presentation which, in turn may be indicative of HLA binding and/or of immunogenicity. Without wishing to be bound by any particular theory, it is proposed that dendritic cell presentation, e.g., in peripheral lymph nodes, may induce CD8+ T cells that migrate to the liver and, for example, may eliminate parasite-infected hepatocytes. See, for example, Chakravarty et al. “CD8+ T lymphocytes protective against malaria liver stages are primed in skin-draining lymph nodes.” Nat Med. 2007 Sep; 13(9):1035-41. Epub 2007 Aug 19, the entire content of which is incorporated herein by reference for the purposes described herein. 2. Exemplary T-cell Antigens [0403] In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes one or more one or more Plasmodium T-cell antigens. In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes one or more Plasmodium T-cell antigens from Plasmodium CSP, LSA-1 (e.g., LSA- 1(a), LSA-1(b)), TRAP, LSAP2, UIS3, ETRAMP10.3, LISP-1, LISP-2, LSA-3, EXP1, LSAP1, or a combination thereof. [0404] In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes 2 to about 20 Plasmodium T-cell antigens (e.g., about 2 to about 15, about 2 to about 10, about 2 to about 9, about 2 to about 8, about 2 to about 7, about 2 to about 6, or about 2 to about 5 Plasmodium T-cell antigens). In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes about 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, or 15 Plasmodium T-cell antigens. In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes four Plasmodium T-cell antigens. In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes five Plasmodium T-cell antigens. In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes six Plasmodium T-cell antigens. In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes seven Plasmodium T-cell antigens. In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes eight Plasmodium T-cell antigens. In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes nine Plasmodium T-cell antigens. In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes ten Plasmodium T-cell antigens. In some embodiments, a Plasmodium T-cell string polypeptide construct described herein comprises one or more immunogenic portions of the Plasmodium T-cell antigens. [0405] In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes a CSP polypeptide, e.g., Plasmodium CSP, e.g., P. falciparum CSP, preferably from Plasmodium falciparum isolate 3D7. In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes a CSP polypeptide comprising or consisting of the amino acid sequence of SEQ ID NO: 1. In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes a CSP polypeptide comprising or consisting of an amino acid sequence having at least 85% (e.g., at least 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99%) sequence identity to an amino acid sequence according to SEQ ID NO: 1. In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes an antigenic Plasmodium CSP polypeptide fragment. In some embodiments, an antigenic Plasmodium CSP polypeptide fragment comprises a Plasmodium CSP N-terminal region. In some embodiments, an antigenic Plasmodium CSP polypeptide fragment comprises a Plasmodium CSP N-terminal domain. In some embodiments, an antigenic Plasmodium CSP polypeptide fragment comprises a Plasmodium CSP N-terminal region and junction region. In some embodiments, an antigenic Plasmodium CSP polypeptide fragment comprises a Plasmodium CSP N-terminal end region and junction region. In some embodiments, an antigenic Plasmodium CSP polypeptide fragment comprises a Plasmodium CSP N-terminal domain and junction region. In some embodiments, an antigenic Plasmodium CSP polypeptide fragment containing at least some part of the N-terminal domain does not contain a C-terminal region. In some embodiments, an antigenic Plasmodium CSP polypeptide fragment comprises or consists of an amino acid sequence with at least 85% (e.g., at least 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99%) sequence identity to an amino acid sequence according to SEQ ID NO: 437. In some embodiments, an antigenic Plasmodium CSP polypeptide fragment comprises or consists of the amino acid according to SEQ ID NO: 437. In some embodiments, an antigenic Plasmodium CSP polypeptide fragment comprises or consists of an amino acid sequence with at least 85% (e.g., at least 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99%) sequence identity to AILSVSSFL (SEQ ID NO: 441), LSVSSFLF (SEQ ID NO: 442), FVEALFQEY (SEQ ID NO: 443), GSSSNTRVL (SEQ ID NO: 444), or ELNYDNAGTNLY (SEQ ID NO: 445). In some embodiments, an antigenic Plasmodium CSP polypeptide fragment comprises or consists of the amino acid sequence AILSVSSFL (SEQ ID NO: 441), LSVSSFLF (SEQ ID NO: 442), FVEALFQEY (SEQ ID NO: 443), GSSSNTRVL (SEQ ID NO: 444), and/or ELNYDNAGTNLY (SEQ ID NO: 445). [0406] In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes a LSA-1(a) polypeptide, e.g., Plasmodium LSA-1(a) polypeptide. In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes a LSA-1(a) polypeptide comprising or consisting of the amino acid sequence of SEQ ID NO: 424. In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes a LSA-1(a) polypeptide comprising or consisting of an amino acid sequence having at least 85% (e.g., at least 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99%) sequence identity to an amino acid sequence according to SEQ ID NO: 424. In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes an antigenic Plasmodium LSA-1(a) polypeptide fragment. In some embodiments, an antigenic Plasmodium LSA-1(a) polypeptide fragment comprises or consists of an amino acid sequence with at least 85% (e.g., at least 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99%) sequence identity to an amino acid sequence according to SEQ ID NO: 447. In some embodiments, an antigenic Plasmodium LSA-1(a) polypeptide fragment comprises or consists of the amino acid according to SEQ ID NO: 447. In some embodiments, an antigenic Plasmodium LSA-1(a) polypeptide fragment comprises or consists of an amino acid sequence with at least 85% (e.g., at least 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99%) sequence identity to HGDVLAEDLY (SEQ ID NO: 451), VLAEDLYGRL (SEQ ID NO: 452), KSADIQNHTL (SEQ ID NO: 453), IQNHTLETV (SEQ ID NO: 454), and/or ISDVNDFQISKY (SEQ ID NO: 455). In some embodiments, an antigenic Plasmodium LSA-1(a) polypeptide fragment comprises or consists of the amino acid sequence HGDVLAEDLY (SEQ ID NO: 451), VLAEDLYGRL (SEQ ID NO: 452), KSADIQNHTL (SEQ ID NO: 453), IQNHTLETV (SEQ ID NO: 454), and/or ISDVNDFQISKY (SEQ ID NO: 455). [0407] In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes a LSA-1(b) polypeptide, e.g., Plasmodium LSA-1(b) polypeptide. In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes a LSA-1(b) polypeptide comprising or consisting of the amino acid sequence of SEQ ID NO: 425. In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes a LSA-1(b) polypeptide comprising or consisting of an amino acid sequence having at least 85% (e.g., at least 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99%) sequence identity to an amino acid sequence according to SEQ ID NO: 425. In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes an antigenic Plasmodium LSA-1(b) polypeptide fragment. In some embodiments, an antigenic Plasmodium LSA-1(b) polypeptide fragment comprises or consists of an amino acid sequence with at least 85% (e.g., at least 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99%) sequence identity to an amino acid sequence according to SEQ ID NO: 457. In some embodiments, an antigenic Plasmodium LSA-1(b) polypeptide fragment comprises or consists of the amino acid according to SEQ ID NO: 457. In some embodiments, an antigenic Plasmodium LSA-1(b) polypeptide fragment comprises or consists of an amino acid sequence with at least 85% (e.g., at least 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99%) sequence identity to DEFKPIVQY (SEQ ID NO: 461), FQDEENIGI (SEQ ID NO: 462), FQDEENIGIY (SEQ ID NO: 463), KSLYDEHIKKY (SEQ ID NO: 464), SLYDEHIKK (SEQ ID NO: 465), SLYDEHIKKYK (SEQ ID NO: 466), YDEHIKKY (SEQ ID NO: 467), HIFDGDNEILQI (SEQ ID NO: 468), IVDELSEDITKY (SEQ ID NO: 469), and/or SEDITKYFM (SEQ ID NO: 470). In some embodiments, an antigenic Plasmodium LSA-1(b) polypeptide fragment comprises or consists of the amino acid sequence DEFKPIVQY (SEQ ID NO: 461), FQDEENIGI (SEQ ID NO: 462), FQDEENIGIY (SEQ ID NO: 463), KSLYDEHIKKY (SEQ ID NO: 464), SLYDEHIKK (SEQ ID NO: 465), SLYDEHIKKYK (SEQ ID NO: 466), YDEHIKKY (SEQ ID NO: 467), HIFDGDNEILQI (SEQ ID NO: 468), IVDELSEDITKY (SEQ ID NO: 469), and/or SEDITKYFM (SEQ ID NO: 470). [0408] In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes a TRAP polypeptide, e.g., Plasmodium TRAP polypeptide. In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes a TRAP polypeptide comprising or consisting of the amino acid sequence of SEQ ID NO: 422. In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes a TRAP polypeptide comprising or consisting of an amino acid sequence having at least 85% (e.g., at least 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99%) sequence identity to an amino acid sequence according to SEQ ID NO: 422. In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes an antigenic Plasmodium TRAP polypeptide fragment. In some embodiments, an antigenic Plasmodium TRAP polypeptide fragment comprises or consists of an amino acid sequence with at least 85% (e.g., at least 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99%) sequence identity to an amino acid sequence according to SEQ ID NO: 472. In some embodiments, an antigenic Plasmodium TRAP polypeptide fragment comprises or consists of the amino acid according to SEQ ID NO: 472. In some embodiments, an antigenic Plasmodium TRAP polypeptide fragment comprises or consists of an amino acid sequence with at least 85% (e.g., at least 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99%) sequence identity to LLMDCSGSI (SEQ ID NO: 476), GSIRRHNW (SEQ ID NO: 477), NLNDNAIHL (SEQ ID NO: 478), NLNDNAIHLY (SEQ ID NO: 479), LNDNAIHLY (SEQ ID NO: 480), ALIIIKSLL (SEQ ID NO: 481), SLLSTNLPY (SEQ ID NO: 482), SLLSTNLPYGK (SEQ ID NO: 483), NLTDALLQV (SEQ ID NO: 484), HLNDRINRENANQ (SEQ ID NO: 485), KLSDRGVKI (SEQ ID NO: 486), KLSDRGVKIAV (SEQ ID NO: 487), AVFGIGQGINV (SEQ ID NO: 488), AVFGIGQGINVA (SEQ ID NO: 489), and/or FGIGQGINV (SEQ ID NO: 490). In some embodiments, an antigenic Plasmodium TRAP polypeptide fragment comprises or consists of the amino acid sequence to LLMDCSGSI (SEQ ID NO: 476), GSIRRHNW (SEQ ID NO: 477), NLNDNAIHL (SEQ ID NO: 478), NLNDNAIHLY (SEQ ID NO: 479), LNDNAIHLY (SEQ ID NO: 480), ALIIIKSLL (SEQ ID NO: 481), SLLSTNLPY (SEQ ID NO: 482), SLLSTNLPYGK (SEQ ID NO: 483), NLTDALLQV (SEQ ID NO: 484), HLNDRINRENANQ (SEQ ID NO: 485), KLSDRGVKI (SEQ ID NO: 486), KLSDRGVKIAV (SEQ ID NO: 487), AVFGIGQGINV (SEQ ID NO: 488), AVFGIGQGINVA (SEQ ID NO: 489), and/or FGIGQGINV (SEQ ID NO: 490). [0409] In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes a LSAP1 polypeptide, e.g., Plasmodium LSAP1 polypeptide. In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes a LSAP1 polypeptide comprising or consisting of the amino acid sequence of SEQ ID NO: 427. In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes a LSAP1 polypeptide comprising or consisting of an amino acid sequence having at least 85% (e.g., at least 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99%) sequence identity to an amino acid sequence according to SEQ ID NO: 427. In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes an antigenic Plasmodium LSAP1 polypeptide fragment. In some embodiments, an antigenic Plasmodium LSAP1 polypeptide fragment comprises or consists of an amino acid sequence with at least 85% (e.g., at least 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99%) sequence identity to an amino acid sequence according to SEQ ID NO: 492. In some embodiments, an antigenic Plasmodium LSAP1 polypeptide fragment comprises or consists of the amino acid according to SEQ ID NO: 492. [0410] In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes a LSAP2 polypeptide, e.g., Plasmodium LSAP2 polypeptide. In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes a LSAP2 polypeptide comprising or consisting of the amino acid sequence of SEQ ID NO: 428. In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes a LSAP2 polypeptide comprising or consisting of an amino acid sequence having at least 85% (e.g., at least 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99%) sequence identity to an amino acid sequence according to SEQ ID NO: 428. In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes an antigenic Plasmodium LSAP2 polypeptide fragment. In some embodiments, an antigenic Plasmodium LSAP2 polypeptide fragment comprises or consists of an amino acid sequence with at least 85% (e.g., at least 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99%) sequence identity to an amino acid sequence according to SEQ ID NO: 497. In some embodiments, an antigenic Plasmodium LSAP2 polypeptide fragment comprises or consists of the amino acid according to SEQ ID NO: 497. In some embodiments, an antigenic Plasmodium LSAP2 polypeptide fragment comprises or consists of an amino acid sequence with at least 85% (e.g., at least 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99%) sequence identity to GLKPSDLNRK (SEQ ID NO: 501), VTEEDLERM (SEQ ID NO: 502), LIWHYSHSL (SEQ ID NO: 503), SLWSICGKL (SEQ ID NO: 504), LAHEHKLPF (SEQ ID NO: 505), HVTDELLIK (SEQ ID NO: 506), HDDYNSIY (SEQ ID NO: 507), and/or HDDYNSIYNY (SEQ ID NO: 508). In some embodiments, an antigenic Plasmodium LSAP2 polypeptide fragment comprises or consists of the amino acid sequence GLKPSDLNRK (SEQ ID NO: 501), VTEEDLERM (SEQ ID NO: 502), LIWHYSHSL (SEQ ID NO: 503), SLWSICGKL (SEQ ID NO: 504), LAHEHKLPF (SEQ ID NO: 505), HVTDELLIK (SEQ ID NO: 506), HDDYNSIY (SEQ ID NO: 507), and/or HDDYNSIYNY (SEQ ID NO: 508). [0411] In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes a UIS3 polypeptide, e.g., Plasmodium UIS3 polypeptide. In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes a UIS3 polypeptide comprising or consisting of the amino acid sequence of SEQ ID NO: 434. In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes a UIS3 polypeptide comprising or consisting of an amino acid sequence having at least 85% (e.g., at least 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99%) sequence identity to an amino acid sequence according to SEQ ID NO: 434. In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes an antigenic Plasmodium UIS3 polypeptide fragment. In some embodiments, an antigenic Plasmodium UIS3 polypeptide fragment comprises or consists of an amino acid sequence with at least 85% (e.g., at least 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99%) sequence identity to an amino acid sequence according to SEQ ID NO: 510. In some embodiments, an antigenic Plasmodium UIS3 polypeptide fragment comprises or consists of the amino acid according to SEQ ID NO: 410. In some embodiments, an antigenic Plasmodium UIS3 polypeptide fragment comprises or consists of an amino acid sequence with at least 85% (e.g., at least 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99%) sequence identity to SLIASGAIASV (SEQ ID NO: 514). In some embodiments, an antigenic Plasmodium UIS3 polypeptide fragment comprises or consists of the amino acid sequence SLIASGAIASV (SEQ ID NO: 514). [0412] In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes an ETRAMP10.3 polypeptide, e.g., Plasmodium ETRAMP10.3 polypeptide. In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes an ETRAMP10.3 polypeptide comprising or consisting of the amino acid sequence of SEQ ID NO: 435. In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes an ETRAMP10.3 polypeptide comprising or consisting of an amino acid sequence having at least 85% (e.g., at least 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99%) sequence identity to an amino acid sequence according to SEQ ID NO: 435. In some embodiments, a Plasmodium T- cell string polypeptide construct described herein includes an antigenic Plasmodium ETRAMP10.3 polypeptide fragment. In some embodiments, an antigenic Plasmodium ETRAMP10.3 polypeptide fragment comprises or consists of an amino acid sequence with at least 85% (e.g., at least 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99%) sequence identity to an amino acid sequence according to SEQ ID NO: 516. In some embodiments, an antigenic Plasmodium ETRAMP10.3 polypeptide fragment comprises or consists of the amino acid according to SEQ ID NO: 516. In some embodiments, an antigenic Plasmodium ETRAMP10.3 polypeptide fragment comprises or consists of an amino acid sequence with at least 85% (e.g., at least 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99%) sequence identity to SLLGCVLTL (SEQ ID NO: 520), RTLEKLLRK (SEQ ID NO: 521), RTLEKLLRKK (SEQ ID NO: 522), and/or GLFGSLGYK (SEQ ID NO: 523). In some embodiments, an antigenic Plasmodium ETRAMP10.3 polypeptide fragment comprises or consists of the amino acid sequence SLLGCVLTL (SEQ ID NO: 520), RTLEKLLRK (SEQ ID NO: 521), RTLEKLLRKK (SEQ ID NO: 522), and/or GLFGSLGYK (SEQ ID NO: 523). [0413] In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes a LISP-1 polypeptide, e.g., Plasmodium LISP-1 polypeptide. In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes a LISP-1 polypeptide comprising or consisting of the amino acid sequence of SEQ ID NO: 429. In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes a LISP-1 polypeptide comprising or consisting of an amino acid sequence having at least 85% (e.g., at least 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99%) sequence identity to an amino acid sequence according to SEQ ID NO: 429. In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes an antigenic Plasmodium LISP-1 polypeptide fragment. In some embodiments, an antigenic Plasmodium LISP-1 polypeptide fragment comprises or consists of an amino acid sequence with at least 85% (e.g., at least 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99%) sequence identity to an amino acid sequence according to SEQ ID NO: 525. In some embodiments, an antigenic Plasmodium LISP-1 polypeptide fragment comprises or consists of the amino acid according to SEQ ID NO: 525. In some embodiments, an antigenic Plasmodium LISP-1 polypeptide fragment comprises or consists of an amino acid sequence with at least 85% (e.g., at least 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99%) sequence identity to YTVGDVLRY (SEQ ID NO: 529), SIYIFHEKK (SEQ ID NO: 530), and/or KIFGCITNK (SEQ ID NO: 531). In some embodiments, an antigenic Plasmodium LISP-1 polypeptide fragment comprises or consists of the amino acid YTVGDVLRY (SEQ ID NO: 529), SIYIFHEKK (SEQ ID NO: 530), and/or KIFGCITNK (SEQ ID NO: 531). [0414] In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes a LISP-2 polypeptide, e.g., Plasmodium LISP-2 polypeptide. In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes a LISP-2 polypeptide comprising or consisting of the amino acid sequence of SEQ ID NO: 430. In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes a LISP-2 polypeptide comprising or consisting of an amino acid sequence having at least 85% (e.g., at least 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99%) sequence identity to an amino acid sequence according to SEQ ID NO: 430. In some embodiments, a Plasmodium T ll string polypeptide construct described herein includes an antigenic Plasmodium LISP-2 polypeptide fragment. In some embodiments, an antigenic Plasmodium LISP-2 polypeptide fragment comprises or consists of an amino acid sequence with at least 85% (e.g., at least 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99%) sequence identity to an amino acid sequence according to SEQ ID NO: 533. In some embodiments, an antigenic Plasmodium LISP-2 polypeptide fragment comprises or consists of the amino acid according to SEQ ID NO: 533. In some embodiments, an antigenic Plasmodium LISP-2 polypeptide fragment comprises or consists of an amino acid sequence with at least 85% (e.g., at least 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99%) sequence identity to ALNIHVMSK (SEQ ID NO: 537), ALNIHVMSKY (SEQ ID NO: 538), NVENRINNISNHY (SEQ ID NO: 539), RLFFLLFYK (SEQ ID NO: 540), and/or KIYYKTKHFEK (SEQ ID NO: 541). In some embodiments, an antigenic Plasmodium LISP-2 polypeptide fragment comprises or consists of the amino acid sequence ALNIHVMSK (SEQ ID NO: 537), ALNIHVMSKY (SEQ ID NO: 538), NVENRINNISNHY (SEQ ID NO: 539), RLFFLLFYK (SEQ ID NO: 540), and/or KIYYKTKHFEK (SEQ ID NO: 541). [0415] In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes a LSA-3 polypeptide, e.g., Plasmodium LSA-3 polypeptide. In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes a LSA-3 polypeptide comprising or consisting of the amino acid sequence of SEQ ID NO: 426. In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes a LSA-3 polypeptide comprising or consisting of an amino acid sequence having at least 85% (e.g., at least 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99%) sequence identity to an amino acid sequence according to SEQ ID NO: 426. In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes an antigenic Plasmodium LSA-3 polypeptide fragment. In some embodiments, an antigenic Plasmodium LSA-3 polypeptide fragment comprises or consists of an amino acid sequence with at least 85% (e.g., at least 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99%) sequence identity to an amino acid sequence according to SEQ ID NO: 543. In some embodiments, an antigenic Plasmodium LSA-3 polypeptide fragment comprises or consists of the amino acid according to SEQ ID NO: 543. In some embodiments, an antigenic Plasmodium LSA-3 polypeptide fragment comprises or consists of an amino acid sequence with at least 85% (e.g., at least 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99%) sequence identity to KLIEETQEL (SEQ ID NO: 547), VEADLIKDM (SEQ ID NO: 548), EEHDITTTL (SEQ ID NO: 549), TTLDEVVEL (SEQ ID NO: 550), TLDEVVEL (SEQ ID NO: 551), ELESEILEDY (SEQ ID NO: 552), LESEILEDY (SEQ ID NO: 553), KTIETDILEEK (SEQ ID NO: 554), and/or ETDILEEKK (SEQ ID NO: 555). In some embodiments, an antigenic Plasmodium LSA-3 polypeptide fragment comprises or consists of the amino acid sequence KLIEETQEL (SEQ ID NO: 547), VEADLIKDM (SEQ ID NO: 548), EEHDITTTL (SEQ ID NO: 549), TTLDEVVEL (SEQ ID NO: 550), TLDEVVEL (SEQ ID NO: 551), ELESEILEDY (SEQ ID NO: 552), LESEILEDY (SEQ ID NO: 553), KTIETDILEEK (SEQ ID NO: 554), and/or ETDILEEKK (SEQ ID NO: 555). [0416] In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes an EXP1 polypeptide, e.g., Plasmodium EXP1 polypeptide. In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes an EXP1 polypeptide comprising or consisting of the amino acid sequence of SEQ ID NO: 431. In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes a EXP1 polypeptide comprising or consisting of an amino acid sequence having at least 85% (e.g., at least 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99%) sequence identity to an amino acid sequence according to SEQ ID NO: 431. In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes an antigenic Plasmodium EXP1 polypeptide fragment. In some embodiments, an antigenic Plasmodium EXP1 polypeptide fragment comprises or consists of an amino acid sequence with at least 85% (e.g., at least 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99%) sequence identity to an amino acid sequence according to SEQ ID NO: 557. In some embodiments, an antigenic Plasmodium EXP1 polypeptide fragment comprises or consists of the amino acid according to SEQ ID NO: 557. 3. Trafficking Signals [0417] In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes a trafficking signal. For example, in some embodiments, a trafficking signal is an MHC class I trafficking signal (MITD). In some embodiments, the MITD comprises or consists of an amino acid sequence according to SEQ ID NO: 561. 4. Select Embodiments of Plasmodium T-cell String Peptide Constructs [0418] The present disclosure provides, among other things, polyribonucleotides that encode a Plasmodium T- cell string polypeptide construct. In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes two or more of: (i) an antigenic Plasmodium CSP polypeptide fragment; (ii) an antigenic Plasmodium LSA-1 (e.g., LSA-1(a) and/or LSA-1(b)) polypeptide fragment; (iii) an antigenic Plasmodium TRAP polypeptide fragment; (iv) an antigenic Plasmodium LSAP2 polypeptide fragment; (v) an antigenic Plasmodium UIS3 polypeptide fragment; (vi) an antigenic Plasmodium ETRAMP10.3 polypeptide fragment; (vii) an antigenic Plasmodium LISP-1 polypeptide fragment; (viii) an antigenic Plasmodium LISP-2 polypeptide fragment; and (ix) an antigenic Plasmodium LSA-3 polypeptide fragment. [0419] In some embodiments, a Plasmodium T ll string polypeptide construct described herein includes one or more polypeptide or portions (e.g., antigenic portions) thereof from Plasmodium falciparum. In some embodiments, one or more polypeptide or portions (e.g., antigenic portions) thereof are one or more P. falciparum T cell antigens. In some embodiments, one or more P. falciparum T cell antigens are from P. falciparum isolate 3D7. [0420] In some embodiments, a Plasmodium T-cell string polypeptide construct described herein does not include one or more polypeptide or portions (e.g., antigenic portions) thereof from Plasmodium berghei (e.g., antigenic Plasmodium berghei CSP polypeptide fragments). [0421] In some embodiments, a Plasmodium T-cell string polypeptide construct describes herein does not include an antigenic fragment of a bacterial polypeptide. In some embodiments, a Plasmodium T-cell string polypeptide construct describes herein does not include an antigenic bacillus Calmette-Guérin (BCG) polypeptide fragment. In some embodiments, an antigenic BCG polypeptide fragment comprises an amino acid sequence according to SEQ ID NO: 416. In some embodiments, a Plasmodium T-cell string polypeptide construct describes herein does not include an antigenic tetanus toxin (TT) polypeptide fragment. In some embodiments, an antigenic TT polypeptide fragment comprises an amino acid sequence according to SEQ ID NO: 417. [0422] In some embodiments, a Plasmodium T-cell string polypeptide construct describes herein does not include an antigenic Plasmodium sporozoite threonine–asparagine-rich protein (STARP) polypeptide fragment. In some embodiments, an antigenic Plasmodium STARP polypeptide fragment comprises an amino acid sequence according to SEQ ID NO: 418. [0423] In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes one or more Plasmodium polypeptide regions or portions (e.g., antigenic portions) thereof, as described above. Exemplary constructs are described below. Exemplary descriptions and sequences for the one or more Plasmodium polypeptide regions or portions (e.g., antigenic portions) thereof discussed below are further discussed in Section IIA(ii) above. Constructs including CSP, TRAP, LSA-1(a), LSA-1(b), LSA-3, LSAP2 [0424] In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes a CSP polypeptide (or one or more antigenic Plasmodium CSP polypeptide fragments) as described above, a Plasmodium TRAP polypeptide (or one or more antigenic Plasmodium TRAP polypeptide fragments) as described above, a Plasmodium LSA-1(a) polypeptide (or one or more antigenic Plasmodium LSA-1(a) polypeptide fragments) as described above, a Plasmodium LSA-1(b) polypeptide (or one or more antigenic Plasmodium LSA-1(b) polypeptide fragments) as described above, a Plasmodium LSA-3 polypeptide (or one or more antigenic Plasmodium LSA-3 polypeptide fragments) as described above, and a Plasmodium LSAP2 polypeptide (or one or more antigenic Plasmodium LSAP2 polypeptide fragments) as described above, wherein the Plasmodium is preferably Plasmodium falciparum and more preferably Plasmodium falciparum isolate 3D7. [0425] In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes: (i) an antigenic Plasmodium CSP polypeptide fragment; (ii) an antigenic Plasmodium TRAP polypeptide fragment; (iii) an antigenic Plasmodium LSA-1(a) polypeptide fragment; (iv) an antigenic Plasmodium LSA-1(b) polypeptide fragment; (v) an antigenic Plasmodium LSA-3 polypeptide fragment; and (vi) an antigenic Plasmodium LSAP2 polypeptide fragment, wherein the Plasmodium is preferably Plasmodium falciparum and more preferably Plasmodium falciparum isolate 3D7. In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes in order: (i) an antigenic Plasmodium CSP polypeptide fragment; (ii) an antigenic Plasmodium TRAP polypeptide fragment; (iii) an antigenic Plasmodium LSA-1(a) polypeptide fragment; (iv) an antigenic Plasmodium LSA-1(b) polypeptide fragment; (v) an antigenic Plasmodium LSA-3 polypeptide fragment; and (vi) an antigenic Plasmodium LSAP2 polypeptide fragment, wherein the Plasmodium is preferably Plasmodium falciparum and more preferably Plasmodium falciparum isolate 3D7. In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes an amino acid sequence with at least 85% (e.g., at least 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99%) sequence identity to an amino acid sequence according to SEQ ID NO:167. In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes the amino acid sequence of SEQ ID NO: 167. In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes in order: (i) an antigenic Plasmodium LSA-1(a) polypeptide fragment; (ii) an antigenic Plasmodium LSA-1(b) polypeptide fragment; (iii) an antigenic Plasmodium LSAP2 polypeptide fragment; (iv) an antigenic Plasmodium CSP polypeptide fragment; (v) an antigenic Plasmodium LSA-3 polypeptide fragment; and (vi) an antigenic Plasmodium TRAP polypeptide fragment, wherein the Plasmodium is preferably Plasmodium falciparum and more preferably Plasmodium falciparum isolate 3D7. In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes an amino acid sequence with at least 85% (e.g., at least 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99%) sequence identity to an amino acid sequence according to SEQ ID NO: 170. In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes the amino acid sequence of SEQ ID NO: 170. Constructs including LSAP1, EXP1, UIS3, ETRAMP10.3, LISP-1, LISP-2 [0426] In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes a Plasmodium LSAP1 polypeptide (or one or more antigenic Plasmodium LSAP1 polypeptide fragments) as described above, a Plasmodium EXP1 polypeptide (or one or more antigenic Plasmodium EXP1 polypeptide fragments) as described above, a Plasmodium UIS3 polypeptide (or one or more antigenic Plasmodium UIS3 polypeptide fragments) as described above, a Plasmodium ETRAMP10.3 polypeptide (or one or more antigenic Plasmodium ETRAMP10.3 polypeptide fragments) as described above, a Plasmodium LISP-1 polypeptide (or one or more antigenic Plasmodium LISP-1 polypeptide fragments) as described above, and a Plasmodium LISP-2 polypeptide (or one or more antigenic Plasmodium LISP-2 polypeptide fragments) as described above, wherein the Plasmodium is preferably Plasmodium falciparum and more preferably Plasmodium falciparum isolate 3D7. [0427] In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes: (i) an antigenic Plasmodium LSAP1 polypeptide fragment; (ii) an antigenic Plasmodium EXP1 polypeptide fragment; (iii) an antigenic Plasmodium UIS3 polypeptide fragment; (iv) an antigenic Plasmodium ETRAMP10.3 polypeptide fragment; (v) an antigenic Plasmodium LISP-1 polypeptide fragment; and (vi) an antigenic Plasmodium LISP-2 polypeptide fragment, wherein the Plasmodium is preferably Plasmodium falciparum and more preferably Plasmodium falciparum isolate 3D7. In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes in order: (i) an antigenic Plasmodium EXP1 polypeptide fragment; (ii) an antigenic Plasmodium UIS3 polypeptide fragment; (iii) an antigenic Plasmodium ETRAMP10.3 polypeptide fragment; (iv) an antigenic Plasmodium LSAP1 polypeptide fragment; (v) an antigenic Plasmodium LISP-2 polypeptide fragment; and (vi) an antigenic Plasmodium LISP-1 polypeptide fragment, wherein the Plasmodium is preferably Plasmodium falciparum and more preferably Plasmodium falciparum isolate 3D7. In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes an amino acid sequence with at least 85% (e.g., at least 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99%) sequence identity to an amino acid sequence according to SEQ ID NO: 173. In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes the amino acid sequence of SEQ ID NO: 173. In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes in order: (i) an antigenic Plasmodium UIS3 polypeptide fragment; (ii) an antigenic Plasmodium LSAP1 polypeptide fragment; (iii) an antigenic Plasmodium LISP-1 polypeptide fragment; (iv) an antigenic Plasmodium EXP1 polypeptide fragment; (v) an antigenic Plasmodium ETRAMP10.3 polypeptide fragment; and (vi) an antigenic Plasmodium LISP-2 polypeptide fragment. In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes an amino acid sequence with at least 85% (e.g., at least 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99%) sequence identity to an amino acid sequence according to SEQ ID NO: 176. In some embodiments, a Pl i T ll string polypeptide construct described herein includes the amino acid sequence of SEQ ID NO: 176. Constructs including CSP, TRAP, LSAP2, UIS3, ETRAMP10.3 [0428] In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes a CSP polypeptide (or one or more antigenic Plasmodium CSP polypeptide fragments) as described above, a Plasmodium TRAP polypeptide (or one or more antigenic Plasmodium TRAP polypeptide fragments) as described above, a Plasmodium LSAP2 polypeptide (or one or more antigenic Plasmodium LSAP2 polypeptide fragments) as described above, a Plasmodium UIS3 polypeptide (or one or more antigenic Plasmodium UIS3 polypeptide fragments) as described above, and a Plasmodium ETRAMP10.3 polypeptide (or one or more antigenic Plasmodium ETRAMP10.3 polypeptide fragments) as described above, wherein the Plasmodium is preferably Plasmodium falciparum and more preferably Plasmodium falciparum isolate 3D7. [0429] In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes: (i) an antigenic Plasmodium CSP polypeptide fragment; (ii) an antigenic Plasmodium TRAP polypeptide fragment; (iii) an antigenic Plasmodium UIS3 polypeptide fragment; (iv) an antigenic Plasmodium ETRAMP10.3 polypeptide fragment; and (v) an antigenic Plasmodium LSAP2 polypeptide fragment, wherein the Plasmodium is preferably Plasmodium falciparum and more preferably Plasmodium falciparum isolate 3D7. In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes in order: (i) an antigenic Plasmodium CSP polypeptide fragment; (ii) an antigenic Plasmodium TRAP polypeptide fragment; (iii) an antigenic Plasmodium UIS3 polypeptide fragment; (iv) an antigenic Plasmodium ETRAMP10.3 polypeptide fragment; and (v) an antigenic Plasmodium LSAP2 polypeptide fragment, wherein the Plasmodium is preferably Plasmodium falciparum and more preferably Plasmodium falciparum isolate 3D7. In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes an amino acid sequence with at least 85% (e.g., at least 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99%) sequence identity to an amino acid sequence according to SEQ ID NO: 179. In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes the amino acid sequence of SEQ ID NO: 179. [0430] In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes in order: (i) an antigenic Plasmodium CSP polypeptide fragment; (ii) an antigenic Plasmodium TRAP polypeptide fragment; (iii) an antigenic Plasmodium UIS3 polypeptide fragment; (iv) an antigenic Plasmodium ETRAMP10.3 polypeptide fragment; and (v) an antigenic Plasmodium LSAP2 polypeptide fragment, wherein the Plasmodium is preferably Plasmodium falciparum and more preferably Plasmodium falciparum isolate 3D7. In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes an amino acid sequence with at least 85% (e.g., at least 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99%) sequence identity to an amino acid sequence according to SEQ ID NO: 221. In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes the amino acid sequence of SEQ ID NO: 221. Constructs including CSP, TRAP, LSA-1(a), LSA-1(b), LSA-3, LSAP2, UIS3, ETRAMP10.3 [0431] In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes a CSP polypeptide (or one or more antigenic Plasmodium CSP polypeptide fragments) as described above, a Plasmodium TRAP polypeptide (or one or more antigenic Plasmodium TRAP polypeptide fragments) as described above, a Plasmodium LSA-1(a) polypeptide (or one or more antigenic Plasmodium LSA-1(a) polypeptide fragments) as described above, a Plasmodium LSA-1(b) polypeptide (or one or more antigenic Plasmodium LSA-1(b) polypeptide fragments) as described above, a Plasmodium LSA-3 polypeptide (or one or more antigenic Plasmodium LSA-3 polypeptide fragments) as described above, a Plasmodium LSAP2 polypeptide (or one or more antigenic Plasmodium LSAP2 polypeptide fragments) as described above, a Plasmodium UIS3 polypeptide (or one or more antigenic Plasmodium UIS3 polypeptide fragments) as described above, and a Plasmodium ETRAMP10.3 polypeptide (or one or more antigenic Plasmodium ETRAMP10.3 polypeptide fragments) as described above, wherein the Plasmodium is preferably Plasmodium falciparum and more preferably Plasmodium falciparum isolate 3D7. [0432] In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes: (i) an antigenic Plasmodium CSP polypeptide fragment; (ii) an antigenic Plasmodium TRAP polypeptide fragment; (iii) an antigenic Plasmodium UIS3 polypeptide fragment; (iv) an antigenic Plasmodium ETRAMP10.3 polypeptide fragment; (v) an antigenic Plasmodium LSAP2 polypeptide fragment; (vi) an antigenic Plasmodium LSA-3 polypeptide fragment; (vii) an antigenic Plasmodium LSA-1(a) polypeptide fragment; and (viii) an antigenic Plasmodium LSA-1(b) polypeptide fragment, wherein the Plasmodium is preferably Plasmodium falciparum and more preferably Plasmodium falciparum isolate 3D7. In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes in order: (i) an antigenic Plasmodium CSP polypeptide fragment; (ii) an antigenic Plasmodium TRAP polypeptide fragment; (iii) an antigenic Plasmodium UIS3 polypeptide fragment; (iv) an antigenic Plasmodium ETRAMP10.3 polypeptide fragment; (v) an antigenic Plasmodium LSAP2 polypeptide fragment; (vi) an antigenic Plasmodium LSA-3 polypeptide fragment; (vii) an antigenic Plasmodium LSA-1(a) polypeptide fragment; and (viii) an antigenic Plasmodium LSA-1(b) polypeptide fragment, wherein the Plasmodium is preferably Plasmodium falciparum and more preferably Plasmodium falciparum isolate 3D7. In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes an amino acid sequence with at least 85% (e.g., at least 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99%) sequence identity to an amino acid sequence according to SEQ ID NO: 182. In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes the amino acid sequence of SEQ ID NO: 182. Constructs including CSP, TRAP, LSA-1(a), LSA-1(b), LSAP2, UIS3, ETRAMP10.3, LISP-1, LISP-2 [0433] In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes a CSP polypeptide (or one or more antigenic Plasmodium CSP polypeptide fragments) as described above, a Plasmodium TRAP polypeptide (or one or more antigenic Plasmodium TRAP polypeptide fragments) as described above, a Plasmodium LSA-1(a) polypeptide (or one or more antigenic Plasmodium LSA-1(a) polypeptide fragments) as described above, a Plasmodium LSA-1(b) polypeptide (or one or more antigenic Plasmodium LSA-1(b) polypeptide fragments) as described above, a Plasmodium LSAP2 polypeptide (or one or more antigenic Plasmodium LSAP2 polypeptide fragments) as described above, a Plasmodium UIS3 polypeptide (or one or more antigenic Plasmodium UIS3 polypeptide fragments) as described above, a Plasmodium ETRAMP10.3 polypeptide (or one or more antigenic Plasmodium ETRAMP10.3 polypeptide fragments) as described above, a Plasmodium LISP-1 polypeptide (or one or more antigenic Plasmodium LISP-1 polypeptide fragments) as described above, and a Plasmodium LISP-2 polypeptide (or one or more antigenic Plasmodium LISP-2 polypeptide fragments) as described above, wherein the Plasmodium is preferably Plasmodium falciparum and more preferably Plasmodium falciparum isolate 3D7. [0434] In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes: (i) an antigenic Plasmodium CSP polypeptide fragment; (ii) an antigenic Plasmodium TRAP polypeptide fragment; (iii) an antigenic Plasmodium UIS3 polypeptide fragment; (iv) an antigenic Plasmodium ETRAMP10.3 polypeptide fragment; (v) an antigenic Plasmodium LSAP2 polypeptide fragment; (vi) an antigenic Plasmodium LSA-1(a) polypeptide fragment; (vii) an antigenic Plasmodium LSA-1(b) polypeptide fragment; (viii) an antigenic Plasmodium LISP-2 polypeptide fragment; and (ix) an antigenic Plasmodium LISP-1 polypeptide fragment, wherein the Plasmodium is preferably Plasmodium falciparum and more preferably Plasmodium falciparum isolate 3D7. In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes in order: (i) an antigenic Plasmodium CSP polypeptide fragment; (ii) an antigenic Plasmodium TRAP polypeptide fragment; (iii) an antigenic Plasmodium UIS3 polypeptide fragment; (iv) an antigenic Plasmodium ETRAMP10.3 polypeptide fragment; (v) an antigenic Plasmodium LSAP2 polypeptide fragment; (vi) an antigenic Plasmodium LSA-1(a) polypeptide fragment; (vii) an antigenic Plasmodium LSA-1(b) polypeptide fragment; (viii) an antigenic Plasmodium LISP-2 polypeptide fragment; and (ix) an antigenic Plasmodium LISP-1 polypeptide fragment, wherein the Plasmodium is preferably Plasmodium falciparum and more preferably Plasmodium falciparum isolate 3D7. In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes an amino acid sequence with at least 85% (e.g., at least 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99%) sequence identity to an amino acid sequence according to SEQ ID NO: 188 In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes the amino acid sequence of SEQ ID NO: 188. Constructs including CSP, TRAP, LSA-1(a), LSA-1(b), LSAP2, UIS3, ETRAMP10.3, LISP-1 [0435] In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes a CSP polypeptide (or one or more antigenic Plasmodium CSP polypeptide fragments) as described above, a Plasmodium TRAP polypeptide (or one or more antigenic Plasmodium TRAP polypeptide fragments) as described above, a Plasmodium LSA-1(a) polypeptide (or one or more antigenic Plasmodium LSA-1(a) polypeptide fragments) as described above, a Plasmodium LSA-1(b) polypeptide (or one or more antigenic Plasmodium LSA-1(b) polypeptide fragments) as described above, a Plasmodium LSAP2 polypeptide (or one or more antigenic Plasmodium LSAP2 polypeptide fragments) as described above, a Plasmodium UIS3 polypeptide (or one or more antigenic Plasmodium UIS3 polypeptide fragments) as described above, a Plasmodium ETRAMP10.3 polypeptide (or one or more antigenic Plasmodium ETRAMP10.3 polypeptide fragments) as described above, and a Plasmodium LISP-1 polypeptide (or one or more antigenic Plasmodium LISP-1 polypeptide fragments) as described above, wherein the Plasmodium is preferably Plasmodium falciparum and more preferably Plasmodium falciparum isolate 3D7. [0436] In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes: (i) an antigenic Plasmodium CSP polypeptide fragment; (ii) an antigenic Plasmodium TRAP polypeptide fragment; (iii) an antigenic Plasmodium UIS3 polypeptide fragment; (iv) an antigenic Plasmodium ETRAMP10.3 polypeptide fragment; (v) an antigenic Plasmodium LSAP2 polypeptide fragment; (vi) an antigenic Plasmodium LSA-1(a) polypeptide fragment; (vii) an antigenic Plasmodium LSA-1(b) polypeptide fragment; and (viii) an antigenic Plasmodium LISP-1 polypeptide fragment, wherein the Plasmodium is preferably Plasmodium falciparum and more preferably Plasmodium falciparum isolate 3D7. In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes in order: (i) an antigenic Plasmodium CSP polypeptide fragment; (ii) an antigenic Plasmodium TRAP polypeptide fragment; (iii) an antigenic Plasmodium UIS3 polypeptide fragment; (iv) an antigenic Plasmodium ETRAMP10.3 polypeptide fragment; (v) an antigenic Plasmodium LSAP2 polypeptide fragment; (vi) an antigenic Plasmodium LSA-1(a) polypeptide fragment; (vii) an antigenic Plasmodium LSA-1(b) polypeptide fragment; and (viii) an antigenic Plasmodium LISP-1 polypeptide fragment, wherein the Plasmodium is preferably Plasmodium falciparum and more preferably Plasmodium falciparum isolate 3D7. In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes an amino acid sequence with at least 85% (e.g., at least 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99%) sequence identity to an amino acid sequence according to SEQ ID NO: 191. In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes the amino acid sequence of SEQ ID NO: 191. Constructs including CSP, TRAP, LSAP2, UIS3, ETRAMP10.3, LISP-1, LISP-2 [0437] In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes a CSP polypeptide (or one or more antigenic Plasmodium CSP polypeptide fragments) as described above, a Plasmodium TRAP polypeptide (or one or more antigenic Plasmodium TRAP polypeptide fragments) as described above, a Plasmodium LSAP2 polypeptide (or one or more antigenic Plasmodium LSAP2 polypeptide fragments) as described above, a Plasmodium UIS3 polypeptide (or one or more antigenic Plasmodium UIS3 polypeptide fragments) as described above, a Plasmodium ETRAMP10.3 polypeptide (or one or more antigenic Plasmodium ETRAMP10.3 polypeptide fragments) as described above, a Plasmodium LISP-1 polypeptide (or one or more antigenic Plasmodium LISP-1 polypeptide fragments) as described above, and a Plasmodium LISP-2 polypeptide (or one or more antigenic Plasmodium LISP-2 polypeptide fragments) as described above, wherein the Plasmodium is preferably Plasmodium falciparum and more preferably Plasmodium falciparum isolate 3D7. [0438] In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes: (i) an antigenic Plasmodium CSP polypeptide fragment; (ii) an antigenic Plasmodium TRAP polypeptide fragment; (iii) an antigenic Plasmodium UIS3 polypeptide fragment; (iv) an antigenic Plasmodium ETRAMP10.3 polypeptide fragment; (v) an antigenic Plasmodium LSAP2 polypeptide fragment; (vi) an antigenic Plasmodium LISP-2 polypeptide fragment; and (vii) an antigenic Plasmodium LISP-1 polypeptide fragment, wherein the Plasmodium is preferably Plasmodium falciparum and more preferably Plasmodium falciparum isolate 3D7. In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes in order: (i) an antigenic Plasmodium CSP polypeptide fragment; (ii) an antigenic Plasmodium TRAP polypeptide fragment; (iii) an antigenic Plasmodium UIS3 polypeptide fragment; (iv) an antigenic Plasmodium ETRAMP10.3 polypeptide fragment; (v) an antigenic Plasmodium LSAP2 polypeptide fragment; (vi) an antigenic Plasmodium LISP-2 polypeptide fragment; and (vii) an antigenic Plasmodium LISP-1 polypeptide fragment, wherein the Plasmodium is preferably Plasmodium falciparum and more preferably Plasmodium falciparum isolate 3D7. In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes an amino acid sequence with at least 85% (e.g., at least 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99%) sequence identity to an amino acid sequence according to SEQ ID NO: 194. In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes the amino acid sequence of SEQ ID NO: 194. Constructs including CSP, TRAP, LSA-1(b), LSAP2, UIS3, ETRAMP10.3, LISP-1 [0439] In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes a CSP polypeptide (or one or more antigenic Plasmodium CSP polypeptide fragments) as described above, a Plasmodium TRAP polypeptide (or one or more antigenic Plasmodium TRAP polypeptide fragments) as described above, a Plasmodium LSA-1(b) polypeptide (or one or more antigenic Plasmodium LSA-1(b) polypeptide fragments) as described above, a Plasmodium LSAP2 polypeptide (or one or more antigenic Plasmodium LSAP2 polypeptide fragments) as described above, a Plasmodium UIS3 polypeptide (or one or more antigenic Plasmodium UIS3 polypeptide fragments) as described above, a Plasmodium ETRAMP10.3 polypeptide (or one or more antigenic Plasmodium ETRAMP10.3 polypeptide fragments) as described above, and a Plasmodium LISP-1 polypeptide (or one or more antigenic Plasmodium LISP-1 polypeptide fragments) as described above, wherein the Plasmodium is preferably Plasmodium falciparum and more preferably Plasmodium falciparum isolate 3D7. [0440] In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes: (i) an antigenic Plasmodium CSP polypeptide fragment; (ii) an antigenic Plasmodium TRAP polypeptide fragment; (iii) an antigenic Plasmodium UIS3 polypeptide fragment; (iv) an antigenic Plasmodium ETRAMP10.3 polypeptide fragment; (v) an antigenic Plasmodium LSAP2 polypeptide fragment; (vi) an antigenic Plasmodium LSA-1(b) polypeptide fragment; and (vii) an antigenic Plasmodium LISP-1 polypeptide fragment, wherein the Plasmodium is preferably Plasmodium falciparum and more preferably Plasmodium falciparum isolate 3D7. In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes in order: (i) an antigenic Plasmodium CSP polypeptide fragment; (ii) an antigenic Plasmodium TRAP polypeptide fragment; (iii) an antigenic Plasmodium UIS3 polypeptide fragment; (iv) an antigenic Plasmodium ETRAMP10.3 polypeptide fragment; (v) an antigenic Plasmodium LSAP2 polypeptide fragment; (vi) an antigenic Plasmodium LSA-1(b) polypeptide fragment; and (vii) an antigenic Plasmodium LISP-1 polypeptide fragment, wherein the Plasmodium is preferably Plasmodium falciparum and more preferably Plasmodium falciparum isolate 3D7. In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes an amino acid sequence with at least 85% (e.g., at least 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99%) sequence identity to an amino acid sequence according to SEQ ID NO: 197. In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes the amino acid sequence of SEQ ID NO: 197. Constructs including CSP, TRAP, LSA-1(a), LSA-1(b), LSA-3, LSAP2, UIS3, ETRAMP10.3, LISP-1, LISP-2 [0441] In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes a CSP polypeptide (or one or more antigenic Plasmodium CSP polypeptide fragments) as described above, a Plasmodium TRAP polypeptide (or one or more antigenic Plasmodium TRAP polypeptide fragments) as described above, a Plasmodium LSA-1(a) polypeptide (or one or more antigenic Plasmodium LSA-1(a) polypeptide fragments) as described above, a Plasmodium LSA-1(b) polypeptide (or one or more antigenic Plasmodium LSA-1(b) polypeptide fragments) as described above, a Plasmodium LSA-3 polypeptide (or one or more antigenic Plasmodium LSA-3 polypeptide fragments) as described above, a Plasmodium LSAP2 polypeptide (or one or more antigenic Plasmodium LSAP2 polypeptide fragments) as described above, a Plasmodium UIS3 polypeptide (or one or more antigenic Plasmodium UIS3 polypeptide fragments) as described above, a Plasmodium ETRAMP10.3 polypeptide (or one or more antigenic Plasmodium ETRAMP10.3 polypeptide fragments) as described above, a Plasmodium LISP-1 polypeptide (or one or more antigenic Plasmodium LISP-1 polypeptide fragments) as described above, and a Plasmodium LISP-2 polypeptide (or one or more antigenic Plasmodium LISP-2 polypeptide fragments) as described above, wherein the Plasmodium is preferably Plasmodium falciparum and more preferably Plasmodium falciparum isolate 3D7. [0442] In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes: (i) an antigenic Plasmodium CSP polypeptide fragment; (ii) an antigenic Plasmodium TRAP polypeptide fragment; (iii) an antigenic Plasmodium UIS3 polypeptide fragment; (iv) an antigenic Plasmodium ETRAMP10.3 polypeptide fragment; (v) an antigenic Plasmodium LSAP2 polypeptide fragment; (vi) an antigenic Plasmodium LSA-1(a) polypeptide fragment; (vii) an antigenic Plasmodium LSA-1(b) polypeptide fragment; (viii) an antigenic Plasmodium LISP-2 polypeptide fragment; (ix) an antigenic Plasmodium LISP-1 polypeptide fragment; and (x) an antigenic Plasmodium LSA-3 polypeptide fragment, wherein the Plasmodium is preferably Plasmodium falciparum and more preferably Plasmodium falciparum isolate 3D7. In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes in order: (i) an antigenic Plasmodium CSP polypeptide fragment; (ii) an antigenic Plasmodium TRAP polypeptide fragment; (iii) an antigenic Plasmodium UIS3 polypeptide fragment; (iv) an antigenic Plasmodium ETRAMP10.3 polypeptide fragment; (v) an antigenic Plasmodium LSAP2 polypeptide fragment; (vi) an antigenic Plasmodium LSA-1(a) polypeptide fragment; (vii) an antigenic Plasmodium LSA-1(b) polypeptide fragment; (viii) an antigenic Plasmodium LISP-2 polypeptide fragment; (ix) an antigenic Plasmodium LISP-1 polypeptide fragment; and (x) an antigenic Plasmodium LSA-3 polypeptide fragment, wherein the Plasmodium is preferably Plasmodium falciparum and more preferably Plasmodium falciparum isolate 3D7. In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes an amino acid sequence with at least 85% (e.g., at least 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99%) sequence identity to an amino acid sequence according to SEQ ID NO: 200. In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes the amino acid sequence of SEQ ID NO: 200. Constructs including LSA-1(a), LSA-1(b), LISP-1, LISP-2 [0443] In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes a Plasmodium LSA-1(a) polypeptide (or one or more antigenic Plasmodium LSA-1(a) polypeptide fragments) as described above, a Plasmodium LSA-1(b) polypeptide (or one or more antigenic Plasmodium LSA-1(b) polypeptide fragments) as described above, a Plasmodium LISP-1 polypeptide (or one or more antigenic Plasmodium LISP-1 polypeptide fragments) as described above, and a Plasmodium LISP-2 polypeptide (or one or more antigenic Plasmodium LISP-2 polypeptide fragments) as described above, wherein the Plasmodium is preferably Plasmodium falciparum and more preferably Plasmodium falciparum isolate 3D7. [0444] In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes: (i) an antigenic Plasmodium LSA-1(a) polypeptide fragment; (ii) an antigenic Plasmodium LSA-1(b) polypeptide fragment; (iii) an antigenic Plasmodium LISP-2 polypeptide fragment; and (iv) an antigenic Plasmodium LISP-1 polypeptide fragment, wherein the Plasmodium is preferably Plasmodium falciparum and more preferably Plasmodium falciparum isolate 3D7. In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes in order: (i) an antigenic Plasmodium LSA-1(a) polypeptide fragment; (ii) an antigenic Plasmodium LSA-1(b) polypeptide fragment; (iii) an antigenic Plasmodium LISP-2 polypeptide fragment; and (iv) an antigenic Plasmodium LISP-1 polypeptide fragment, wherein the Plasmodium is preferably Plasmodium falciparum and more preferably Plasmodium falciparum isolate 3D7. In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes an amino acid sequence with at least 85% (e.g., at least 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99%) sequence identity to an amino acid sequence according to SEQ ID NO: 209. In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes the amino acid sequence of SEQ ID NO: 209. Constructs including LSA-1(a), LSA-1(b), LSA-3, LISP-1, LISP-2 [0445] In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes a Plasmodium LSA-1(a) polypeptide (or one or more antigenic Plasmodium LSA-1(a) polypeptide fragments) as described above, a Plasmodium LSA-1(b) polypeptide (or one or more antigenic Plasmodium LSA-1(b) polypeptide fragments) as described above, a Plasmodium LSA-3 polypeptide (or one or more antigenic Plasmodium LSA-3 polypeptide fragments) as described above, a Plasmodium LISP-1 polypeptide (or one or more antigenic Plasmodium LISP-1 polypeptide fragments) as described above, and a Plasmodium LISP-2 polypeptide (or one or more antigenic Plasmodium LISP-2 polypeptide fragments) as described above, wherein the Plasmodium is preferably Plasmodium falciparum and more preferably Plasmodium falciparum isolate 3D7. [0446] In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes: (i) an antigenic Plasmodium LSA-1(a) polypeptide fragment; (ii) an antigenic Plasmodium LSA-1(b) polypeptide fragment; (iii) an antigenic Plasmodium LISP-2 polypeptide fragment; (iv) an antigenic Plasmodium LISP-1 polypeptide fragment; and (v) an antigenic Plasmodium LSA-3 polypeptide fragment, wherein the Plasmodium is preferably Plasmodium falciparum and more preferably Plasmodium falciparum isolate 3D7. In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes in order: (i) an antigenic Plasmodium LSA- 1(a) polypeptide fragment; (ii) an antigenic Plasmodium LSA-1(b) polypeptide fragment; (iii) an antigenic Plasmodium LISP-2 polypeptide fragment; (iv) an antigenic Plasmodium LISP-1 polypeptide fragment; and (v) an antigenic Plasmodium LSA-3 polypeptide fragment, wherein the Plasmodium is preferably Plasmodium falciparum and more preferably Plasmodium falciparum isolate 3D7. In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes an amino acid sequence with at least 85% (e.g., at least 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99%) sequence identity to an amino acid sequence according to SEQ ID NO: 212. In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes the amino acid sequence of SEQ ID NO: 212. Constructs including TRAP, LSA-1(a), LSA-1(b), LSAP2, UIS3, ETRAMP10.3, LISP-1, LISP-2 [0447] In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes a Plasmodium TRAP polypeptide (or one or more antigenic Plasmodium TRAP polypeptide fragments) as described above, a Plasmodium LSA-1(a) polypeptide (or one or more antigenic Plasmodium LSA-1(a) polypeptide fragments) as described above, a Plasmodium LSA-1(b) polypeptide (or one or more antigenic Plasmodium LSA-1(b) polypeptide fragments) as described above, a Plasmodium LSAP2 polypeptide (or one or more antigenic Plasmodium LSAP2 polypeptide fragments) as described above, a Plasmodium UIS3 polypeptide (or one or more antigenic Plasmodium UIS3 polypeptide fragments) as described above, a Plasmodium ETRAMP10.3 polypeptide (or one or more antigenic Plasmodium ETRAMP10.3 polypeptide fragments) as described above, a Plasmodium LISP-1 polypeptide (or one or more antigenic Plasmodium LISP-1 polypeptide fragments) as described above, and a Plasmodium LISP-2 polypeptide (or one or more antigenic Plasmodium LISP-2 polypeptide fragments) as described above, wherein the Plasmodium is preferably Plasmodium falciparum and more preferably Plasmodium falciparum isolate 3D7. [0448] In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes: (i) an antigenic Plasmodium TRAP polypeptide fragment; (ii) an antigenic Plasmodium UIS3 polypeptide fragment; (iii) an antigenic Plasmodium ETRAMP10.3 polypeptide fragment; (iv) an antigenic Plasmodium LSAP2 polypeptide fragment; (v) an antigenic Plasmodium LSA-1(a) polypeptide fragment; (vi) an antigenic Plasmodium LSA-1(b) polypeptide fragment; (vii) an antigenic Plasmodium LISP-2 polypeptide fragment; and (viii) an antigenic Plasmodium LISP-1 polypeptide fragment, wherein the Plasmodium is preferably Plasmodium falciparum and more preferably Plasmodium falciparum isolate 3D7. In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes in order: (i) an antigenic Plasmodium TRAP polypeptide fragment; (ii) an antigenic Plasmodium UIS3 polypeptide fragment; (iii) an antigenic Plasmodium ETRAMP10.3 polypeptide fragment; (iv) an antigenic Plasmodium LSAP2 polypeptide fragment; (v) an antigenic Plasmodium LSA-1(a) polypeptide fragment; (vi) an antigenic Plasmodium LSA-1(b) polypeptide fragment; (vii) an antigenic Plasmodium LISP-2 polypeptide fragment; and (viii) an antigenic Plasmodium LISP-1 polypeptide fragment, wherein the Plasmodium is preferably Plasmodium falciparum and more preferably Plasmodium falciparum isolate 3D7. In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes an amino acid sequence with at least 85% (e.g., at least 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99%) sequence identity to an amino acid sequence according to SEQ ID NO: 215. In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes the amino acid sequence of SEQ ID NO: 215. Constructs including TRAP, LSAP2, UIS3, ETRAMP10.3 [0449] In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes a Plasmodium TRAP polypeptide (or one or more antigenic Plasmodium TRAP polypeptide fragments) as described above, a Plasmodium LSAP2 polypeptide (or one or more antigenic Plasmodium LSAP2 polypeptide fragments) as described above, a Plasmodium UIS3 polypeptide (or one or more antigenic Plasmodium UIS3 polypeptide fragments) as described above, and a Plasmodium ETRAMP10.3 polypeptide (or one or more antigenic Plasmodium ETRAMP10.3 polypeptide fragments) as described above, wherein the Plasmodium is preferably Plasmodium falciparum and more preferably Plasmodium falciparum isolate 3D7. [0450] In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes: (i) an antigenic Plasmodium TRAP polypeptide fragment; (ii) an antigenic Plasmodium UIS3 polypeptide fragment; (iii) an antigenic Plasmodium ETRAMP10.3 polypeptide fragment; and (iv) an antigenic Plasmodium LSAP2 polypeptide fragment, wherein the Plasmodium is preferably Plasmodium falciparum and more preferably Plasmodium falciparum isolate 3D7. In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes in order: (i) an antigenic Plasmodium TRAP polypeptide fragment; (ii) an antigenic Plasmodium UIS3 polypeptide fragment; (iii) an antigenic Plasmodium ETRAMP10.3 polypeptide fragment; and (iv) an antigenic Plasmodium LSAP2 polypeptide fragment, wherein the Plasmodium is preferably Plasmodium falciparum and more preferably Plasmodium falciparum isolate 3D7. In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes an amino acid sequence with at least 85% (e.g., at least 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99%) sequence identity to an amino acid sequence according to SEQ ID NO: 218. In some embodiments, a Plasmodium T-cell string polypeptide construct described herein includes the amino acid sequence of SEQ ID NO: 218. Exemplary Construct Sequences [0451] In some embodiments, a Plasmodium T-cell string polypeptide construct described herein has an amino acid sequence provided in Table 3, and/or is encoded by a nucleotide sequence provided in Table 9. Exemplary Plasmodium T-cell string polypeptide constructs are also shown schematically in FIG.3. Table 3: Amino Acid Sequences Encoding Exemplary Plasmodium T-cell String Polypeptide Constructs

B. Plasmodium CSP Polypeptide Constructs [0452] The present disclosure, among other things, utilizes RNA technologies as a modality to express one or more Plasmodium CSP polypeptide constructs (also referred to as “Plasmodium CSP polypeptides,” “malaria CSP polypeptide constructs” or “malarial polypeptide constructs”). A Plasmodium CSP polypeptide construct as described herein can include one or more Plasmodium CSP polypeptide regions or portions (e.g., antigenic portions) thereof. A Plasmodium CSP polypeptide construct as described herein includes one or more polypeptides or antigenic portions thereof that are expressed during a Plasmodium sporozoite stage. In some embodiments, a Plasmodium CSP polypeptide construct as described herein is capable of eliciting antibody responses, preferably strong antibody responses. Methods to determine antibody responses are well known in the art and described in the examples. In some embodiments, Plasmodium CSP polypeptide constructs as described herein can be (i) full length Plasmodium CSP protein including the Plasmodium secretory signal and GPI anchor or (ii) only contain selected regions or portions (such as antigenic portions) of a Plasmodium CSP protein. [0453] A portion of a CSP polypeptide or region can be a characteristic portion of CSP polypeptide or region. In some embodiments, a Plasmodium CSP polypeptide construct additionally includes one or more additional amino acid sequences, such as a secretory signal (e.g., a heterologous secretory signal), a transmembrane region (e.g., a heterologous transmembrane region), a helper antigen, a multimerization region, and/or a linker, as described herein. [0454] In some embodiments, a Plasmodium CSP polypeptide construct described herein includes one or more regions or portions (e.g., antigenic portions) of a CSP, e.g., Plasmodium CSP, e.g., P. falciparum CSP (SEQ ID NO: 1), or a variant thereof (e.g., one or more antigenic portions of a CSP, e.g., Plasmodium CSP, e.g., P. falciparum CSP, or antigenic variants thereof). A region of CSP (or CSP polypeptide region) may refer to a N-terminal region, a N- terminal end region, a junction region (or its sub-regions: an R1 region or a junction), a minor repeat region, a major repeat region or a C-terminal region. A portion of CSP (or CSP polypeptide portion) may refer to parts of a CSP polypeptide region or parts spanning two or more CSP polypeptide regions. For example, a portion of CSP may refer to an N-terminal domain, a central domain, or a C-terminal domain. In some embodiments, a CSP polypeptide portion (e.g., antigenic portions) comprises 25, 30, 35, 40, or 45 contiguous amino acids of the amino acid sequence according to SEQ ID NO: 1. In some embodiments, a Plasmodium CSP polypeptide construct does not include a secretory signal or a transmembrane region, e.g., corresponds to amino acids 19-375 of the amino acid sequence according to SEQ ID NO: 1 or corresponds to amino acids 19-376 or 19-377 of the amino acid sequence according to SEQ ID NO: 1 (i.e., includes a serine or a serine and valine immediately after the C-terminal region). [0455] In some embodiments, a Plasmodium CSP polypeptide construct described herein includes a CSP minor repeat region. In some embodiments, a Plasmodium CSP polypeptide construct described herein includes a portion (e.g., an antigenic portion) of a CSP minor repeat region. In some embodiments, a portion (e.g., an antigenic portion) of a CSP minor repeat region is about 10, 15, 20, 21, 22, or 23 contiguous amino acids in length. In some embodiments, a Plasmodium CSP polypeptide construct described herein includes a CSP major repeat region. In some embodiments, a Plasmodium CSP polypeptide construct described herein includes a portion (e.g., an antigenic portion) of a CSP major repeat region. In some embodiments, a portion (e.g., an antigenic portion) of a CSP major repeat region is about 100, 110, 120, 130, 135, 140, 141, or 142 amino acids in length. In some embodiments, a Plasmodium CSP polypeptide construct described herein includes a CSP C-terminal region. In some embodiments, a Plasmodium CSP polypeptide construct described herein includes a portion (e.g., an antigenic portion) of a CSP C- terminal region. In some embodiments, a portion (e.g., an antigenic portion) of a CSP C-terminal region is about 80, 90, 95, 100, 101, or 102 amino acids in length. In some embodiments, a Plasmodium CSP polypeptide construct described herein includes a CSP N-terminal region. In some embodiments, a Plasmodium CSP polypeptide construct described herein includes a portion (e.g., an antigenic portion) of a CSP N-terminal region. In some embodiments, a portion (e.g., an antigenic portion) of a CSP N-terminal region is about 45, 50, 55, 60, or 61 amino acids in length. In some embodiments, a Plasmodium CSP polypeptide construct described herein includes a CSP N-terminal end region. In some embodiments, a Plasmodium CSP polypeptide construct described herein includes a portion (e.g., an antigenic portion) of a CSP N-terminal end region. In some embodiments, a portion (e.g., an antigenic portion) of a CSP N-terminal end region is about 8, 9, 10, or 11 amino acids in length. In some embodiments, a Plasmodium CSP polypeptide construct described herein includes a CSP junction region. In some embodiments, a Plasmodium CSP polypeptide construct described herein includes a portion (e.g., an antigenic portion) of a CSP junction region. In some embodiments, a portion (e.g., an antigenic portion) of a CSP junction region is about 8, 9, 10, or 11 amino acids in length. 1. CSP Regions Minor Repeat Region [0456] In some embodiments, a Plasmodium CSP polypeptide construct described herein includes one or more Plasmodium CSP minor repeat regions or portions (e.g., antigenic portions) thereof comprising one or more repeats of an amino acid sequence of NANPNVDP (SEQ ID NO: 223), and wherein the polypeptide does not comprise an amino acid sequence of NPNA (SEQ ID NO: 228), NPNANP (SEQ ID NO: 231) or NANPNA (SEQ ID NO: 232). [0457] In some embodiments, a Plasmodium CSP polypeptide construct described herein includes one or more Plasmodium CSP polypeptide regions or portions (e.g., antigenic portions) thereof comprising one or more (e.g., 2, 3, 4, 5, 6, 7, 8, 9, 10, 11 or 12) repeats of an amino acid sequence of NANPNVDP (SEQ ID NO: 223). In some embodiments, a Plasmodium CSP polypeptide construct described herein includes one or more Plasmodium CSP polypeptide regions or portions (e.g., antigenic portions) thereof comprising two or more (e.g., between 2 and 12, or between 2 and 10, or between 2 and 9, or between 2 and 8, or between 4 and 12, or between 4 and 10) repeats of an amino acid sequence of NANPNVDP (SEQ ID NO: 223). In some embodiments, a Plasmodium CSP polypeptide construct described herein includes one or more Plasmodium CSP polypeptide regions or portions (e.g., antigenic portions) thereof comprising exactly three repeats of an amino acid sequence of NANPNVDP (SEQ ID NO: 223). In some embodiments, a Plasmodium CSP polypeptide construct described herein includes one or more Plasmodium CSP polypeptide regions or portions (e.g., antigenic portions) thereof comprising exactly eight repeats of an amino acid sequence of NANPNVDP (SEQ ID NO: 223). In some embodiments, a Plasmodium CSP polypeptide construct described herein includes one or more Plasmodium CSP polypeptide regions or portions (e.g., antigenic portions) thereof comprising exactly nine repeats of an amino acid sequence of NANPNVDP (SEQ ID NO: 223). [0458] In some embodiments, the repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223) are all contiguous with each other. In some embodiments, the repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223) are not all contiguous with each other. In some embodiments, a Plasmodium CSP polypeptide construct described herein comprises four portions (e.g., antigenic portions) of a Plasmodium CSP minor repeat region, and wherein each portion (e.g., antigenic portion) of a Plasmodium CSP polypeptide comprises two contiguous repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223). [0459] In some embodiments, a Plasmodium CSP minor repeat region comprises or consists of an amino acid sequence that is at least 85%, at least 90%, at least 95%, or 100% identical to the amino acid sequence of SEQ ID NO: 226 (NANPNVDPNANPNVDPNANPNVDP). In some embodiments, a Plasmodium CSP minor repeat region comprises or consists of an amino acid sequence according to SEQ ID NO: 226. [0460] In some embodiments, a Plasmodium CSP polypeptide construct described herein does not comprise one or more portions of one or more Plasmodium CSP minor repeat regions (i.e., lacks or excludes a Plasmodium CSP minor repeat region or any portion thereof). C-terminal Region [0461] In some embodiments, a Plasmodium CSP polypeptide construct described herein includes one or more Plasmodium CSP C-terminal regions (e.g., amino acids 273-375 of SEQ ID NO: 1), one or more Plasmodium CSP C- terminal region variants, or one or more portions (e.g., antigenic portions) thereof, wherein the C-terminal region does not include a transmembrane region. In some embodiments, a Plasmodium CSP polypeptide construct described herein includes exactly one Plasmodium CSP C-terminal region, and wherein the Plasmodium CSP C-terminal region comprises or consists of an amino acid sequence with at least 85% (e.g., at least 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%) sequence identity to amino acids 273-375 of SEQ ID NO: 1. In some embodiments, a malarial polypeptide construct described herein includes one or more Plasmodium CSP C- terminal region variants. In some embodiments, a Plasmodium CSP C-terminal region variant comprises or consists of an amino acid sequence with at least 85% (e.g., at least 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%) sequence identity to amino acid sequence of SEQ ID NO: 994. In some embodiments, a Plasmodium CSP polypeptide construct described herein includes exactly one portion (e.g., antigenic portion) of a Plasmodium CSP C-terminal region, and wherein the portion (e.g., antigenic portion) of a Plasmodium CSP C-terminal region comprises or consists of an amino acid sequence with at least 85% (e.g., at least 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%) sequence identity to amino acid sequence of SEQ ID NO: 241 (PSDKHIKEYLNKIQNSLSTEWSPCSVTCGNGIQVRIKPGSANKPKDELDYANDIEKKICKMEK). In some embodiments, a Plasmodium CSP polypeptide construct described herein includes two or more portions (e.g., antigenic portions) of a Plasmodium CSP C-terminal region (e.g., amino acids 273-375 of SEQ ID NO: 1). [0462] In some embodiments, a Plasmodium CSP polypeptide construct described herein includes one or more portions (e.g., antigenic portions) of the Plasmodium CSP C-terminal region, wherein each of the one or more portions (e.g., antigenic portions) comprises or consists of: (i) amino acids 314-327 of SEQ ID NO:1 (or amino acids 314-327 of SEQ ID NO: 1 having 1, 2, 3, 4, or 5 amino acid substitutions); (ii) amino acids 352-363 of SEQ ID NO: 1 (or amino acids 352-363 of SEQ ID NO: 1 having 1, 2, 3, 4, or 5 amino acid substitutions); (iii) amino acids 326-374 of SEQ ID NO: 1 (or amino acids 326-374 of SEQ ID NO:1 having 1, 2, 3, 4, or 5 amino acid substitutions), (iv) amino acids 364-377 of SEQ ID NO: 1 (or amino acids 364-377 of SEQ ID NO: 1 having 1, 2, 3, 4, or 5 amino acid substitutions), or (v) a combination thereof. [0463] In some embodiments, a Plasmodium CSP polypeptide construct described herein includes one portion (e.g., antigenic portion) of the Plasmodium CSP C-terminal region, wherein the portion (e.g., antigenic portion) comprises or consists of: (i) amino acids 314-327 of SEQ ID NO: 1 (or amino acids 314-327 of SEQ ID NO:1 having 1, 2, 3, 4, or 5 amino acid substitutions); (ii) amino acids 352-363 of SEQ ID NO: 1 (or amino acids 352-363 of SEQ ID NO:1 having 1, 2, 3, 4, or 5 amino acid substitutions); (iii) amino acids 326-374 of SEQ ID NO:1 (or amino acids 326-374 of SEQ ID NO: 1 having 1, 2, 3, 4, or 5 amino acid substitutions), (iv) amino acids 364-377 of SEQ ID NO: 1 (or amino acids 364-377 of SEQ ID NO: 1 having 1, 2, 3, 4, or 5 amino acid substitutions), or (v) a combination thereof. [0464] In some embodiments, a Plasmodium CSP polypeptide construct described herein includes one or more portions (e.g., antigenic portions) of the Plasmodium CSP C-terminal region, wherein the one or more portions (e.g., antigenic portions) collectively comprise or consist of: (i) amino acids 314-327 of SEQ ID NO: 1 (or amino acids 314- 327 of SEQ ID NO: 1 having 1, 2, 3, 4, or 5 amino acid substitutions); (ii) amino acids 352-363 of SEQ ID NO: 1 (or amino acids 352-363 of SEQ ID NO: 1 having 1, 2, 3, 4, or 5 amino acid substitutions); (iii) amino acids 326-374 of SEQ ID NO: 1 (or amino acids 326-374 of SEQ ID NO: 1 having 1, 2, 3, 4, or 5 amino acid substitutions), (iv) amino acids 364-377 of SEQ ID NO: 1 (or amino acids 364-377 of SEQ ID NO: 1 having 1, 2, 3, 4, or 5 amino acid substitutions), or (v) a combination thereof. [0465] In some embodiments, a Plasmodium CSP polypeptide construct described herein comprises a serine amino acid residue immediately following a Plasmodium CSP C-terminal region described herein. In some embodiments, a Plasmodium CSP polypeptide construct described herein comprises a serine-valine amino acid sequence immediately following a Plasmodium CSP C-terminal region described herein. [0466] In some embodiments, a Plasmodium CSP polypeptide construct described herein includes one or more portions (e.g., antigenic portions) of the Plasmodium CSP C-terminal region, wherein the one or more portions (e.g., antigenic portions) comprise or consist of a portion (e.g., antigenic portion) of a Plasmodium CSP C-terminal region, wherein the portion (e.g., antigenic portion) of a Plasmodium CSP C-terminal region comprises an amino acid sequence according to SEQ ID NO: 261 (YLX₃X₄IQX₅SLST), wherein X₃ is N or K, X₄ is K, I, or R, and X₅ is N or Y. In some embodiments, a Plasmodium CSP polypeptide construct described herein includes one or more portions (e.g., antigenic portions) of the Plasmodium CSP C-terminal region, wherein the one or more portions (e.g., antigenic portions) comprise or consist of a portion (e.g., antigenic portion) of a Plasmodium CSP C-terminal region, wherein the portion (e.g., antigenic portion) of a Plasmodium CSP C-terminal region comprises an amino acid sequence according to SEQ ID NO: 262 (YLX₃X₄IQX₅SLSTEW), wherein X₃ is N or K, X₄ is K, I, or R, and X₅ is N or Y. In some embodiments, a Plasmodium CSP polypeptide construct described herein includes one or more portions (e.g., antigenic portions) of the Plasmodium CSP C-terminal region, wherein the one or more portions (e.g., antigenic portions) comprise or consist of a portion (e.g., antigenic portion) of a Plasmodium CSP C-terminal region, wherein the portion (e.g., antigenic portion) of a Plasmodium CSP C-terminal region comprises an amino acid sequence according to SEQ ID NO: 263 (YLX₃X₄IQX₅SLSTEWS), wherein X₃ is N or K, X₄ is K, I, or R, and X₅ is N or Y. In some embodiments, a Plasmodium CSP polypeptide construct described herein includes one or more portions (e.g., antigenic portions) of the Plasmodium CSP C-terminal region, wherein the one or more portions (e.g., antigenic portions) comprise or consist of a portion (e.g., antigenic portion) of a Plasmodium CSP C-terminal region, wherein the portion (e.g., antigenic portion) of a Plasmodium CSP C-terminal region comprises an amino acid sequence according to SEQ ID NO: 264 (IX1X2YLX3X4IQX5SLST), wherein X1X2 is EK or KE, X3 is N or K, X4 is K, I, or R, and X5 is N or Y. In some embodiments, a Plasmodium CSP polypeptide construct described herein includes one or more portions (e.g., antigenic portions) of the Plasmodium CSP C-terminal region, wherein the one or more portions (e.g., antigenic portions) comprise or consist of a portion (e.g., antigenic portion) of a Plasmodium CSP C-terminal region, wherein the portion (e.g., antigenic portion) of a Plasmodium CSP C-terminal region comprises an amino acid sequence according to SEQ ID NO: 265 (IX₁X₂YLX₃X₄IQX₅SLSTEW), wherein X₁X₂ is EK or KE, X₃ is N or K, X₄ is K, I, or R, and X₅ is N or Y. In some embodiments, a Plasmodium CSP polypeptide construct described herein includes one or more portions (e.g., antigenic portions) of the Plasmodium CSP C-terminal region, wherein the one or more portions comprise or consist of a portion (e.g., antigenic portion) of a Plasmodium CSP C-terminal region, wherein the portion (e.g., antigenic portion) of a Plasmodium CSP C-terminal region comprises an amino acid sequence according to SEQ ID NO: 266 (IX₁X₂YLX₃X₄IQX₅SLSTEWS), wherein X₁X₂ is EK or KE, X₃ is N or K, X₄ is K, I, or R, and X₅ is N or Y. In some embodiments, a Plasmodium CSP polypeptide construct described herein includes one or more portions (e.g., antigenic portions) of a Plasmodium CSP C-terminal region, wherein the one or more portions (e.g., antigenic portions) comprise or consist of a portion (e.g., antigenic portion) of a Plasmodium CSP C-terminal region, wherein the portion (e.g., antigenic portion) of a Plasmodium CSP C-terminal region comprises an amino acid sequence according to SEQ ID NO: 267 (IKEYLNKIQNSLSTEWS). In some embodiments, a Plasmodium CSP polypeptide construct described herein includes one or more portions (e.g., antigenic portions) of the Plasmodium CSP C-terminal region, wherein the one or more portions (e.g., antigenic portions) comprise or consist of a portion (e.g., antigenic portion) of a Plasmodium CSP C-terminal region, wherein the portion (e.g., antigenic portion) of a Plasmodium CSP C-terminal region comprises or consists of an amino acid sequence that is at least 85%, at least 90%, at least 95%, at least 98%, or 100% identical to the amino acid sequence of SEQ ID NO: 241 (PSDKHIKEYLNKIQNSLSTEWSPCSVTCGNGIQVRIKPGSANKPKDELDYANDIEKKICKMEK). [0467] In some embodiments, one or more Plasmodium CSP polypeptide regions or antigenic portions thereof comprise a Plasmodium CSP C-terminal region variant or antigenic portion thereof. In some embodiments, a Plasmodium CSP C-terminal region variant or antigenic portion thereof comprises one or more amino acid substitutions, insertions, or deletions. In some embodiments, a Plasmodium CSP C-terminal region variant or antigenic portion thereof comprises one or more amino acid substitutions. In some embodiments, one or more amino acid substitutions comprise S301N, K317E, E318Q, N321K, E357Q, A361E, or any combination thereof, wherein the amino acid numbering is relative to SEQ ID NO: 1. In some embodiments, one or more amino acid substitutions comprise S301N, K317E, E318Q, N321K, E357Q, and A361E, wherein the amino acid numbering is relative to SEQ ID NO: 1. In some embodiments, a Plasmodium CSP C-terminal region variant comprises or consists of an amino acid sequence that is at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identical to the amino acid sequence of SEQ ID NO: 994. [0468] In some embodiments, a malarial polypeptide construct described herein includes one or more portions (e.g., antigenic portions) of a Plasmodium CSP C-terminal region variant, wherein the one or more portions comprise or consist of a portion (e.g., antigenic portion) of a Plasmodium CSP C-terminal region variant. In some embodiments, a portion of a Plasmodium CSP C-terminal region comprises an amino acid sequence according to SEQ ID NO: 992. In some embodiments, a portion of a Plasmodium CSP C-terminal region comprises an amino acid sequence according to SEQ ID NO: 993. In some embodiments, a Plasmodium CSP C-terminal region variant comprises or consists of an amino acid sequence with at least 85% (e.g., at least 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%) sequence identity to amino acid sequence of SEQ ID NO: 994. [0469] In some embodiments, a Plasmodium CSP polypeptide construct described herein comprises a serine amino acid residue immediately following a Plasmodium CSP C-terminal region, Plasmodium CSP C-terminal region variant, or one or more portions (e.g., antigenic portions) thereof, as described herein. In some embodiments, a Plasmodium CSP polypeptide construct described herein comprises a serine-valine amino acid sequence immediately following a Plasmodium CSP C-terminal region, Plasmodium CSP C-terminal region variant, or one or more portions (e.g., antigenic portions) thereof, as described herein. [0470] In some embodiments, a Plasmodium CSP polypeptide construct described herein does not comprise one or more portions of one or more Plasmodium CSP C-terminal regions (i.e., lacks or excludes a Plasmodium CSP C-terminal region or any portion thereof). Junction Region [0471] In some embodiments, a Plasmodium CSP polypeptide construct described herein includes one or more Plasmodium CSP junction regions or portions (e.g., antigenic portions) thereof. In some embodiments, a junction region includes an R1 region (amino acids 93-97) and a junction (SEQ ID NO: 277) at positions 98-104. [0472] In some embodiments, a Plasmodium CSP polypeptide construct described herein includes two or more Plasmodium CSP junction regions or portions (e.g., antigenic portions) thereof. [0473] In some embodiments, a Plasmodium CSP polypeptide construct described herein includes exactly one Plasmodium CSP junction region. In some embodiments, a Plasmodium CSP junction region comprises or consists of amino acids 93-104 of SEQ ID NO: 1 (or amino acids 93-104 of SEQ ID NO: 1 having 1, 2, 3, 4, or 5 amino acid substitutions). In some embodiments, a Plasmodium CSP junction region comprises or consists of an amino acid sequence that is at least 90% or at least 100% identical to the amino acid sequence of SEQ ID NO: 277. In some embodiments, a Plasmodium CSP polypeptide construct described herein includes one or more portions (e.g., antigenic portions) of a Plasmodium CSP junction region. In some embodiments, a portion (e.g., antigenic portion) of a Plasmodium CSP junction region comprises or consists of amino acids 93-97 of SEQ ID NO: 1. In some embodiments, a portion (e.g., an antigenic portion) of a Plasmodium CSP junction region comprises or consists of amino acids 98-104 of SEQ ID NO: 1. [0474] In some embodiments, a Plasmodium CSP polypeptide construct described herein includes one or more Plasmodium CSP junction regions or portions (e.g., antigenic portions) thereof, wherein the Plasmodium CSP junction region comprises or consists of an amino acid sequence that is at least 90% or 100% identical to the amino acid sequence of SEQ ID NO: 272 (KLKQPADGNPDP). In some embodiments, a Plasmodium CSP polypeptide construct described herein includes one or more Plasmodium CSP junction regions or portions (e.g., antigenic portions) thereof, wherein the Plasmodium CSP junction region comprises or consists of an amino acid sequence according to SEQ ID NO: 272. [0475] In some embodiments, a Plasmodium CSP polypeptide construct described herein includes one or more portions (e.g., antigenic portions) of a Plasmodium CSP junction region. In some embodiments, one or more portions (e.g., antigenic portions) of a Plasmodium CSP junction region comprise a deletion of one or more of K93, L94, K95, Q96 and P97, wherein the amino acid numbering is relative to SEQ ID NO: 1. In some embodiments, one or more portions (e.g., antigenic portions) of a Plasmodium CSP junction region comprise a deletion of K93, L94, K95, and Q96, wherein the amino acid numbering is relative to SEQ ID NO: 1. In some embodiments, one or more portions (e.g., antigenic portions) of a Plasmodium CSP junction region comprise a deletion of K93, L94, K95, Q96 and P97, wherein the amino acid numbering is relative to SEQ ID NO: 1. [0476] In some embodiments, a Plasmodium CSP polypeptide construct described herein includes one or more Plasmodium CSP junction region variants. In some embodiments, a Plasmodium CSP junction region variant comprises one or more amino acid substitution mutations. In some embodiments, one or more substitution mutations comprise a K93A mutation, an L94A mutation, or both, wherein the amino acid numbering is relative to SEQ ID NO: 1. In some embodiments, a Plasmodium CSP junction region variant comprises the amino acid sequence of AAKQ (SEQ ID NO: 283). [0477] In some embodiments, a Plasmodium CSP polypeptide construct described herein does not comprise one or more portions of one or more Plasmodium CSP junction regions (i.e., lacks or excludes a Plasmodium CSP junction region or any portion thereof). N-terminal End Region [0478] In some embodiments, a Plasmodium CSP polypeptide construct described herein includes one or more Plasmodium CSP N-terminal end regions or portions (e.g., antigenic portions) thereof. In some embodiments, a Plasmodium CSP polypeptide construct described herein includes two or more Plasmodium CSP N-terminal end regions or portions (e.g., antigenic portions) thereof. In some embodiments, a Plasmodium CSP N-terminal end region comprises or consists of amino acids 81-92 of SEQ ID NO: 1 (or amino acids 81-92 of SEQ ID NO: 1 having 1, 2, 3, 4, or 5 amino acid substitutions). [0479] In some embodiments, a Plasmodium CSP N-terminal end region comprises or consists of an amino acid sequence that is at least 90% or at least 100% identical to the amino acid sequence of SEQ ID NO: 285 (EDNEKLRKPKHK). In some embodiments, a Plasmodium CSP N-terminal end region comprises or consists of an amino acid sequence according to SEQ ID NO: 285. [0480] In some embodiments, a Plasmodium CSP polypeptide construct described herein does not comprise a Plasmodium CSP N-terminal end region or any portion thereof (i.e., lacks or excludes a Plasmodium CSP N-terminal end region or any portion thereof). N-terminal Region [0481] In some embodiments, a Plasmodium CSP polypeptide construct described herein includes one or more Plasmodium CSP N-terminal regions or portions (e.g., antigenic portions) thereof. In some embodiments, a Plasmodium CSP polypeptide construct described herein includes two or more Plasmodium CSP N-terminal regions or portions (e.g., antigenic portions) thereof. [0482] In some embodiments, a Plasmodium CSP N-terminal region comprises or consists of amino acids 19-80 of SEQ ID NO: 1. In some embodiments, a Plasmodium CSP N-terminal region comprises or consists of an amino acid sequence with at least 85% (e.g., at least 86%, 87%, 88%, 89%, 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100%) sequence identity to amino acids 19-80 of SEQ ID NO: 1. [0483] In some embodiments, a malarial polypeptide construct described herein includes one or more Plasmodium CSP polypeptide regions or antigenic portions thereof comprise an antigenic portion of a Plasmodium CSP N-terminal region. In some embodiments, an antigenic portion of a Plasmodium CSP N-terminal region comprises or consists of an N-terminal start region. In some embodiments, an antigenic portion of a Plasmodium CSP N-terminal region comprises or consists of an amino acid sequence with at least 85% (e.g., at least 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99%) sequence identity to the amino acid sequence of SEQ ID NO: 1010. [0484] In some embodiments, a Plasmodium CSP polypeptide construct described herein does not comprise a Plasmodium CSP N-terminal region or any portion thereof (i.e., lacks or excludes a Plasmodium CSP N-terminal region or any portion thereof). Major Repeat Region [0485] In some embodiments, a Plasmodium CSP polypeptide construct described herein includes one or more Plasmodium CSP major repeat regions or portions (e.g., antigenic portions) thereof. In some embodiments, a Plasmodium CSP polypeptide construct described herein includes exactly one Plasmodium CSP major repeat region or portion (e.g., antigenic portion) thereof, and the Plasmodium CSP major repeat region or portion (e.g., antigenic portion) thereof comprises a total of at least 2 and at most 35 repeats of the amino acid sequence NANP (SEQ ID NO: 230). In some embodiments, a Plasmodium CSP major repeat region or portion (e.g., antigenic portion) thereof comprises two contiguous stretches of repeats of the amino acid sequence NANP (SEQ ID NO: 230), and wherein the two contiguous stretches of the repeats of the amino acid sequence NANP (SEQ ID NO: 230) flank an amino acid sequence of NVDP (SEQ ID NO: 229). In some embodiments, a Plasmodium CSP major repeat region comprises, in N-terminus to C-terminus order, 17 repeats of the amino acid sequence NANP (SEQ ID NO: 230), an amino acid sequence of NVDP (SEQ ID NO: 229), and 18 repeats of the amino acid sequence NANP (SEQ ID NO: 230). In some embodiments, a portion (e.g., antigenic portion) of the Plasmodium CSP major repeat region consists of at most 18 contiguous repeats of the amino acid sequence NANP (SEQ ID NO: 230). In some embodiments, a portion (e.g., antigenic portion) of the Plasmodium CSP major repeat region consists of 2 contiguous repeats of the amino acid sequence NANP (SEQ ID NO: 230). The one or more Plasmodium CSP major repeat region or portion (e.g., antigenic portion) thereof always contains at least one repeat of the amino acid sequence of NPNANP (SEQ ID NO: 231) or NANPNA (SEQ ID NO: 232). In some embodiments, a Plasmodium CSP major repeat region comprises or consists of an amino acid sequence with at least 85% (e.g., at least 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99%) sequence identity to amino acids 129-272 of SEQ ID NO: 1. In some embodiments, a Plasmodium CSP polypeptide construct described herein does not comprise a Plasmodium CSP major repeat region or a portion (e.g., antigenic portion) of a Plasmodium CSP major repeat region comprising the amino acid sequence NPNA (SEQ ID NO: 228) (i.e., lacks or excludes a Plasmodium CSP major repeat region or a portion (e.g., antigenic portion) of a Plasmodium CSP major repeat region comprising the amino acid sequence NPNA (SEQ ID NO: 228)). [0486] In some embodiments, a portion (e.g., antigenic portion) of the Plasmodium CSP major repeat region consists of at most 18 contiguous repeats of the amino acid sequence NANP (SEQ ID NO: 230). In some embodiments, a portion (e.g., antigenic portion) of the Plasmodium CSP major repeat region consists of 18 contiguous repeats of the amino acid sequence NANP (SEQ ID NO: 230). The one or more Plasmodium CSP major repeat region or portion (e.g., antigenic portion) thereof always contains at least one repeat (e.g., one instance) of the amino acid sequence of NANP (SEQ ID NO: 230). In some embodiments, a portion (e.g., antigenic portion) of the Plasmodium CSP major repeat region comprises six (6) repeats of the amino acid sequence of NANP (SEQ ID NO: 230). In some embodiments, a portion (e.g., antigenic portion) of the Plasmodium CSP major repeat region comprises or consists of an asparagine-alanine positioned immediately following the six repeats of the amino acid sequence of NANP. In some embodiments, a portion (e.g., antigenic portion) of the Plasmodium CSP major repeat region comprises or consists of the amino acid sequence SEQ ID NO: 303. In some embodiments, a Plasmodium CSP major repeat region comprises or consists of an amino acid sequence with at least 85% (e.g., at least 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%) sequence identity to SEQ ID NO: 303. [0487] In some embodiments, a Plasmodium CSP polypeptide construct described herein does not comprise a Plasmodium CSP major repeat region or a portion of a Plasmodium CSP major repeat region comprising the amino acid sequence NPNA (SEQ ID NO: 228) (i.e., lacks or excludes a Plasmodium CSP major repeat region or a portion of a Plasmodium CSP major repeat region comprising the amino acid sequence NPNA (SEQ ID NO: 228). In some embodiments, a Plasmodium CSP polypeptide construct described herein does not comprise a Plasmodium CSP major repeat region or a portion of a Plasmodium CSP major repeat region comprising the amino acid sequence NANP (SEQ ID NO: 230) (i.e., lacks or excludes a Plasmodium CSP major repeat region or a portion of a Plasmodium CSP major repeat region comprising the amino acid sequence NANP (SEQ ID NO: 230). Exemplary Region Order [0488] In some embodiments, a Plasmodium CSP polypeptide construct described herein optionally includes one or more of the following Plasmodium CSP polypeptide regions or portions (e.g., antigenic portions) thereof, and if present, are in the following N-terminus to C-terminus order: (i) one or more Plasmodium CSP N-terminal regions or portions (e.g., antigenic portions) thereof, (ii) one or more Plasmodium CSP N-terminal end regions or portions (e.g., antigenic portions) thereof, (iii) one or more Plasmodium CSP junction regions, portions (e.g., antigenic portions) thereof, or variants thereof, (iv) one or more repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223), (v) one or more Plasmodium CSP major repeat regions or portions (e.g., antigenic portions) thereof, and (vi) one or more Plasmodium CSP C-terminal regions or portions (e.g., antigenic portions) thereof. [0489] In some embodiments, a Plasmodium CSP polypeptide construct described herein optionally includes one or more of the following Plasmodium CSP polypeptide regions or portions (e.g., antigenic portions) thereof, and if present, are in the following N-terminus to C-terminus order: (i) one Plasmodium CSP N-terminal region or portion (e.g., antigenic portion) thereof, (ii) one Plasmodium CSP N-terminal end region or portion (e.g., antigenic portion) thereof, (iii) one Plasmodium CSP junction region, portion (e.g., antigenic portion) thereof, or variant thereof, (iv) one or more Plasmodium CSP minor repeat sequences, (v) one Plasmodium CSP major repeat region or portion (e.g., antigenic portion) thereof, and (vi) one Plasmodium CSP C-terminal region or portion (e.g., antigenic portion) thereof. 2. Helper Antigens [0490] In some embodiments, a Plasmodium CSP polypeptide construct described herein includes one or more helper antigens. Those skilled in the art are aware of a variety of potentially useful helper antigens, including those described in, e.g., WO2020128031 (which is incorporated herein by reference in its entirety) (e.g., P2 tetanus toxin, PADRE peptide, Hepatitis B surface antigen (HBsAg)). In some embodiments, a helper antigen is a malarial protein (e.g., a malarial protein described herein), provided that the antigen is not a CSP polypeptide or portion thereof. In some embodiments, a helper antigen is Plasmodium 2-phospho-D-glycerate hydro-lyase antigen, Plasmodium liver stage antigen 1(a), (LSA-1(a)), Plasmodium liver stage antigen 1(b) (LSA-1(b)), Plasmodium thrombospondin-related anonymous protein (TRAP), Plasmodium liver stage associated protein 1 (LSAP1), Plasmodium liver stage associated protein 2 (LSAP2), Plasmodium UIS3, Plasmodium UIS4, Plasmodium ETRAMP10.3, Plasmodium liver specific protein 1 (LISP-1), Plasmodium liver specific protein 2 (LISP-2), Plasmodium liver stage antigen 3 (LSA-3), Plasmodium EXP1, Plasmodium E140, Plasmodium reticulocyte-binding protein homolog 5 (Rh5), Plasmodium glutamic acid-rich protein (GARP), Plasmodium parasite-infected erythrocyte surface protein 2 (PIESP2), Plasmodium Cysteine-Rich Protective Antigen (CyRPA), Plasmodium Ripr, Plasmodium P113, or a combination thereof. [0491] In some embodiments, a helper antigen comprises or consists of a P. falciparum 2-phospho-D-glycerate hydro-lyase antigen, e.g., comprising or consisting of amino acid sequence of ELDGSKNEWGWSKSKLGANA (SEQ ID NO: 388). In some embodiments, a helper antigen comprises or consists of a P. falciparum liver-stage antigen 3, e.g., comprising or consisting of amino acid sequence of ENVQVSDELFNELLNSVDVNGEVKENILEESQVNDDIFNSLVKSVQQEQQHNVEEKVEESVEENDEESVEENVEENVEENDDESVAS SVEESIASSVDESIDSSIEENVAPTVEEIVAPTVEEIVAPSVVESVAPSVEESVEENVEESVAENVEESVAENVEESVAENVEESVAENV EESVAENVEESVA (SEQ ID NO: 391). In some embodiments, a helper antigen comprises or consists of an Anopheles antigen, e.g., an Anopheles gambiae TRIO, e.g., comprising or consisting of amino acid sequence of MCRGLSAVLILLVSLSAQLHVVVGEEAPKPEKEICGLKVGRLLDSVKGWLSVSQQEKCPLNKYCENKIQADQYNLVPLTCIRWRSLNP ASPTGSLGGKDVVSKIDAAMSNFKTLFEPMKADLAKLEEEVKRQVLDAWKALEPLQKEVYRSTLASGRIERAVFYSFMEMGDNVKLD NYFQPANVEELLKYAWALPMHKKQRSMYDLIGQLVQSSKSPMLQTLHAVELATVVNPELENRENLLNDQVVQLRDNLYKNSFATLV SIARHFPDHFDTLRQRLFKLPDGSKPGADTLPNIVNFIAQLPSDELRLSSVDLLLQSLTAENGTLVQDPEYVYRLSQLAHAMPSLVDVK AHPDLQQSVDDLMAKFNTPIDGKTLQYFQNIGISPSSSVAT (SEQ ID NO: 393). [0492] In some embodiments, a Plasmodium CSP polypeptide construct described herein comprises a secretory signal (e.g., a secretory signal described herein) and a helper antigen immediately follows the secretory signal. [0493] In some embodiments, a Plasmodium CSP polypeptide construct described herein comprises a helper antigen located at the C-terminus. [0494] In some embodiments, a Plasmodium CSP polypeptide construct described herein comprises a linker between the CSP portion and the helper antigen. 3. Multimerization Regions [0495] In some embodiments, a Plasmodium CSP polypeptide construct described herein includes one or more multimerization regions (e.g., a heterologous multimerization region). In some embodiments, a heterologous multimerization region comprises a dimerization, trimerization or tetramerization region. [0496] In some embodiments, a multimerization region is one described in WO2017/081082, which is incorporated herein by reference in its entirety (e.g., SEQ ID NOs: 1116-1167, or fragments or variants thereof). Exemplary trimerization and tetramerization regions include, but are not limited to, engineered leucine zippers, fibritin foldon domain from enterobacteria phage T4, GCN4pll, GCN4-pll, and p53. [0497] In some embodiments, a provided Plasmodium CSP polypeptide construct described herein is able to form a trimeric complex. For example, a provided Plasmodium CSP polypeptide construct may comprise a multimerization region allowing formation of a multimeric complex, such as for example a trimeric complex of a Plasmodium CSP polypeptide construct described herein. In some embodiments, a multimerization region allowing formation of a multimeric complex comprises a trimerization region, for example, a trimerization region described herein. In some embodiments, a Plasmodium CSP polypeptide construct includes a T4-fibritin-derived “foldon” trimerization region, for example, to increase its immunogenicity. In some embodiments, a Plasmodium CSP polypeptide construct includes a multimerization region comprising or consisting of the amino acid sequence GYIPEAPRDGQAYVRKDGEWVLLSTFLGRSLEVLFQGPG (SEQ ID NO: 399). 4. Self-Assembling Regions [0498] In some embodiments, a Plasmodium CSP polypeptide construct described herein includes one or more self-assembling regions (e.g., a self-assembling nanoparticle region, e.g., a heterologous self-assembling nanoparticle region). In some embodiments, a self-assembling nanoparticle region is a ferritin region. In some embodiments, a ferritin region is from H. pylori. In some embodiments, a ferritin region comprises or consists of a sequence according to the amino acid sequence of 402). 5. Select Embodiments of Plasmodium CSP Polypeptide Constructs [0499] In some embodiments, a Plasmodium CSP polypeptide construct described herein includes one or more Plasmodium CSP polypeptide regions or portions thereof as described above. Exemplary combinations of regions are described below. In some embodiments, a Plasmodium CSP polypeptide construct described herein includes one or more regions or portions of CSP from Plasmodium falciparum, preferably from Plasmodium falciparum isolate 3D7. Full Length CSP Constructs [0500] In some embodiments, a Plasmodium CSP polypeptide construct described herein includes one or more regions or portions of CSP from Plasmodium falciparum, preferably from Plasmodium falciparum isolate 3D7. In some embodiments, a Plasmodium CSP polypeptide construct described herein includes one or more of a N-terminal region, a N-terminal end region, a junction region, a minor repeat region, a major repeat region and a C-terminal region or corresponding portions thereof of CSP from Plasmodium falciparum, preferably from Plasmodium falciparum isolate 3D7. In some embodiments, a Plasmodium CSP polypeptide construct described herein has the structure: N- terminal region – N-terminal end region – junction region – minor repeat region – major repeat region – C-terminal region, wherein the regions are from CSP from Plasmodium falciparum, preferably from Plasmodium falciparum isolate 3D7. In preferred embodiments, such Plasmodium CSP polypeptide constructs have immediately following the C-terminal region a serine or a serine and a valine. In preferred embodiments, the N-terminal region or portion thereof comprises the amino acid sequence of positions 19 to 80 of SEQ ID NO: 1, or an amino acid sequence having at least 99%, 98%, 97%, 96%, 95%, 90%, 85%, or 80% identity to the amino acid sequence of positions 19 to 80 of SEQ ID NO: 1. In preferred embodiments, the N-terminal end region or portion thereof comprises the amino acid sequence of positions 81 to 92 of SEQ ID NO: 1, or the amino acid sequence of positions 81 to 92 of SEQ ID NO: 1 having 1, 2, 3, 4, or 5 amino acid substitutions. In preferred embodiments, the junction region or portion thereof comprises the amino acid sequence of positions 93 to 104 of SEQ ID NO: 1, or the amino acid sequence of positions 93 to 104 of SEQ ID NO: 1 having 1, 2, 3, 4, or 5 amino acid substitutions. In preferred embodiments, the minor repeat region or portion thereof comprises the amino acid sequence of positions 105 to 128 of SEQ ID NO: 1, or an amino acid sequence having at least 99%, 98%, 97%, 96%, 95%, 90%, 85%, or 80% identity to the amino acid sequence of positions 105 to 128 of SEQ ID NO: 1. In preferred embodiments, the major repeat region or portion thereof comprises the amino acid sequence of positions 129 to 272 of SEQ ID NO: 1, or an amino acid sequence having at least 99%, 98%, 97%, 96%, 95%, 90%, 85%, or 80% identity to the amino acid sequence of positions 129 to 272 of SEQ ID NO: 1. In preferred embodiments, the C-terminal region or portion thereof comprises the amino acid sequence of positions 273 to 375 of SEQ ID NO: 1, or an amino acid sequence having at least 99%, 98%, 97%, 96%, 95%, 90%, 85%, or 80% identity to the amino acid sequence of positions 273 to 375 of SEQ ID NO: 1. In preferred embodiments, a Plasmodium CSP polypeptide construct comprises the amino acid sequence of positions 19-375 of SEQ ID NO: 1, or an amino acid sequence having at least 99%, 98%, 97%, 96%, 95%, 90%, 85%, or 80% identity to the amino acid sequence of positions 19-375 of SEQ ID NO: 1. [0501] Such a Plasmodium CSP polypeptide construct that includes all CSP regions as mentioned before and includes a serine or serine and valine immediately following the C-terminal region is referred to as a full-length CSP construct. [0502] In some embodiments, a Plasmodium CSP polypeptide construct can have the following structure: full-length CSP construct; Secretory signal (sec)-full-length CSP construct; full-length CSP construct-transmembrane region (TMD); sec-full-length CSP construct-TMD; Plasmodium falciparum (Pf) sec-full-length CSP construct; full-length CSP construct-PfTMD; or Pfsec-full-length CSP construct-PfTMD. CSP Constructs with Noncontiguous Minor Repeat Regions [0503] In some embodiments, a Plasmodium CSP polypeptide construct described herein includes one or more of a N-terminal end region, a junction region, a minor repeat region, a major repeat region portion and a C-terminal region or corresponding portions thereof of CSP from Plasmodium falciparum, preferably from Plasmodium falciparum isolate 3D7. [0504] In some embodiments, a Plasmodium CSP polypeptide construct described herein has the structure: N- terminal end region – junction region – [minor repeat region–major repeat region portion]_x – minor repeat region– C- terminal region, wherein the [minor repeat region–major repeat region portion] repeats x times, and wherein the regions are from CSP from Plasmodium falciparum, preferably from Plasmodium falciparum isolate 3D7. In some embodiments, x is 2 to 5 (i.e., the [minor repeat region–major repeat region portion] repeats 2 to 5 times). In preferred embodiments, such Plasmodium CSP polypeptide constructs have two repeats of a [minor repeat region– major repeat region portion], such that a Plasmodium CSP polypeptide construct described herein has the structure: N-terminal end region – junction region – minor repeat region – major repeat region portion – minor repeat region – major repeat region portion – minor repeat region – C-terminal region. In preferred embodiments, the N-terminal end region or portion thereof comprises the amino acid sequence of positions 81 to 92 of SEQ ID NO: 1, or the amino acid sequence of positions 81 to 92 of SEQ ID NO: 1 having 1, 2, 3, 4, or 5 amino acid substitutions. In preferred embodiments, the junction region includes an R1 region (amino acids 93-97) of SEQ ID NO:1. In preferred embodiments, the junction region or portion thereof comprises the amino acid sequence of positions 93 to 104 of SEQ ID NO: 1, or the amino acid sequence of positions 93 to 104 of SEQ ID NO: 1 having 1, 2, 3, 4, or 5 amino acid substitutions. In preferred embodiments, a minor repeat region or portion thereof comprises the amino acid sequence of positions 105 to 128 of SEQ ID NO: 1, or an amino acid sequence having at least 99%, 98%, 97%, 96%, 95%, 90%, 85%, or 80% identity to the amino acid sequence of positions 105 to 128 of SEQ ID NO: 1. In some embodiments, a major repeat region portion comprises at least four repeats, at least five repeats, at least six repeats, at least seven repeats of the sequence NANP (SEQ ID NO: 230). In preferred embodiments, the major repeat region portion comprises a sequence of NANPNANPNANPNANPNANPNANP (SEQ ID NO: 311). In preferred embodiments, the C-terminal region or portion thereof comprises the amino acid sequence of positions 273 to 375 of SEQ ID NO: 1, or an amino acid sequence having at least 99%, 98%, 97%, 96%, 95%, 90%, 85%, or 80% identity to the amino acid sequence of positions 273 to 375 of SEQ ID NO: 1. a Plasmodium CSP polypeptide construct that includes all CSP regions or corresponding portions thereof as mentioned before and includes noncontiguous minor repeat regions (i.e., minor repeat region – major repeat region portion – minor repeat region – major repeat region portion – minor repeat region) is referred to as a 3xMR CSP construct. In some embodiments, a Plasmodium CSP polypeptide construct can have the following structure: 3xMR CSP construct; sec-3xMR CSP construct; 3xMR CSP construct-TMD; or sec-3xMR CSP construct-TMD. N-terminal Region Deleted CSP Constructs [0505] In some embodiments, a Plasmodium CSP polypeptide construct described herein includes one or more of a N-terminal end region, a junction region, a minor repeat region, a major repeat region and a C-terminal region or corresponding portions thereof of CSP from Plasmodium falciparum, preferably from Plasmodium falciparum isolate 3D7. In some embodiments, a Plasmodium CSP polypeptide construct described herein has the structure: N- terminal end region – junction region – minor repeat region – major repeat region – C-terminal region, wherein the regions are from CSP from Plasmodium falciparum, preferably from Plasmodium falciparum isolate 3D7. In preferred embodiments, such Plasmodium CSP polypeptide constructs have immediately following the C-terminal region a serine or a serine and a valine. In preferred embodiments, the N-terminal end region or portion thereof comprises the amino acid sequence of positions 81 to 92 of SEQ ID NO: 1, or the amino acid sequence of positions 81 to 92 of SEQ ID NO: 1 having 1, 2, 3, 4, or 5 amino acid substitutions. In preferred embodiments, the junction region or portion thereof comprises the amino acid sequence of positions 93 to 104 of SEQ ID NO:1, or the amino acid sequence of positions 93 to 104 of SEQ ID NO: 1 having 1, 2, 3, 4, or 5 amino acid substitutions. In preferred embodiments, the minor repeat region or portion thereof comprises the amino acid sequence of positions 105 to 128 of SEQ ID NO: 1, or an amino acid sequence having at least 99%, 98%, 97%, 96%, 95%, 90%, 85%, or 80% identity to the amino acid sequence of positions 105 to 128 of SEQ ID NO:1. In preferred embodiments, the major repeat region or portion thereof comprises the amino acid sequence of positions 129 to 272 of SEQ ID NO: 1, or an amino acid sequence having at least 99%, 98%, 97%, 96%, 95%, 90%, 85%, or 80% identity to the amino acid sequence of positions 129 to 272 of SEQ ID NO: 1. In preferred embodiments, the C-terminal region or portion thereof comprises the amino acid sequence of positions 273 to 375 of SEQ ID NO: 1, or an amino acid sequence having at least 99%, 98%, 97%, 96%, 95%, 90%, 85%, or 80% identity to the amino acid sequence of positions 273 to 375 of SEQ ID NO: 1. Such a Plasmodium CSP polypeptide construct that includes all CSP regions or corresponding portions thereof as mentioned before except the N-terminal region or a portion thereof and includes a serine or serine and valine immediately following the C-terminal region is referred to as a dNT CSP construct. In some embodiments, a Plasmodium CSP polypeptide construct can have the following structure: dNT CSP construct; sec-dNT CSP construct; dNT CSP construct-TMD; or sec-dNT CSP construct-TMD. N-terminal Region and Major Repeat Region Deleted CSP Constructs [0506] In some embodiments, a Plasmodium CSP polypeptide construct described herein includes one or more of a N-terminal end region, a junction region, one or more minor repeat region, and a C-terminal region or corresponding portions thereof of CSP from Plasmodium falciparum, preferably from Plasmodium falciparum isolate 3D7. In some embodiments, a Plasmodium CSP polypeptide construct described herein has the structure: N-terminal end region – junction region – one or more minor repeat region – C-terminal region, wherein the regions are from CSP from Plasmodium falciparum, preferably from Plasmodium falciparum isolate 3D7. In preferred embodiments, such Plasmodium CSP polypeptide constructs have immediately following the C-terminal region a serine or a serine and a valine. In preferred embodiments, the N-terminal end region or portion thereof comprises the amino acid sequence of positions 81 to 92 of SEQ ID NO: 1, or the amino acid sequence of positions 81 to 92 of SEQ ID NO: 1 having 1, 2, 3, 4, or 5 amino acid substitutions. In preferred embodiments, the junction region or portion thereof comprises the amino acid sequence of positions 93 to 104 of SEQ ID NO: 1, or the amino acid sequence of positions 93 to 104 of SEQ ID NO: 1 having 1, 2, 3, 4, or 5 amino acid substitutions. In preferred embodiments, the minor repeat region or portion thereof comprises the amino acid sequence of positions 105 to 128 of SEQ ID NO: 1, or an amino acid sequence having at least 99%, 98%, 97%, 96%, 95%, 90%, 85%, or 80% identity to the amino acid sequence of positions 105 to 128 of SEQ ID NO: 1. In preferred embodiments, the C-terminal region or portion thereof comprises the amino acid sequence of positions 273 to 375 of SEQ ID NO: 1, or an amino acid sequence having at least 99%, 98%, 97%, 96%, 95%, 90%, 85%, or 80% identity to the amino acid sequence of positions 273 to 375 of SEQ ID NO: 1. In some embodiments, such Plasmodium CSP polypeptide constructs have more than one minor repeat region, such as three minor repeat regions. Such a Plasmodium CSP polypeptide construct that includes all CSP regions or corresponding portions thereof as mentioned before except the N-terminal region and the major repeat region or corresponding portions thereof, has one or more minor repeat region and includes a serine or serine and valine immediately following the C-terminal region is referred to as a dNT-dmajor CSP construct. In some embodiments, a Plasmodium CSP polypeptide construct can have the following structure: dNT-dmajor CSP construct; sec-dNT-dmajor CSP construct; dNT-dmajor CSP construct-TMD; or sec-dNT-dmajor CSP construct-TMD. N-terminal Domain Deleted CSP Constructs [0507] In some embodiments, a Plasmodium CSP polypeptide construct described herein includes one or more of a junction region, one or more minor repeat regions, a major repeat region and a C-terminal region or corresponding portions thereof of CSP from Plasmodium falciparum, preferably from Plasmodium falciparum isolate 3D7. In some embodiments, a Plasmodium CSP polypeptide construct described herein has the structure: junction region – one or more minor repeat region – major repeat region - C-terminal region, wherein the regions are from CSP from Plasmodium falciparum, preferably from Plasmodium falciparum isolate 3D7. In preferred embodiments, such Plasmodium CSP polypeptide constructs have immediately following the C-terminal region a serine or a serine and a valine. In preferred embodiments, the junction region or portion thereof comprises the amino acid sequence of positions 93 to 104 of SEQ ID NO: 1, or the amino acid sequence of positions 93 to 104 of SEQ ID NO: 1 having 1, 2, 3, 4, or 5 amino acid substitutions. In preferred embodiments, the minor repeat region or portion thereof comprises the amino acid sequence of positions 105 to 128 of SEQ ID NO: 1, or an amino acid sequence having at least 99%, 98%, 97%, 96%, 95%, 90%, 85%, or 80% identity to the amino acid sequence of positions 105 to 128 of SEQ ID NO: 1. In preferred embodiments, the major repeat region or portion thereof comprises the amino acid sequence of positions 129 to 272 of SEQ ID NO: 1, or an amino acid sequence having at least 99%, 98%, 97%, 96%, 95%, 90%, 85%, or 80% identity to the amino acid sequence of positions 129 to 272 of SEQ ID NO: 1. In preferred embodiments, the C-terminal region or portion thereof comprises the amino acid sequence of positions 273 to 375 of SEQ ID NO:1, or an amino acid sequence having at least 99%, 98%, 97%, 96%, 95%, 90%, 85%, or 80% identity to the amino acid sequence of positions 273 to 375 of SEQ ID NO: 1. In some embodiments, such Plasmodium CSP polypeptide constructs have more than one minor repeat region, such as three minor repeat regions. Such a Plasmodium CSP polypeptide construct that includes all CSP regions or corresponding portions thereof as mentioned before except the N-terminal domain (i.e., exclude the N-terminal region and the N-terminal end region) or a portion thereof, has one or more minor repeat regions and includes a serine or serine and valine immediately following the C-terminal region is referred to as a dND CSP construct. In some embodiments, a Plasmodium CSP polypeptide construct can have the following structure: dND CSP construct; sec-dND CSP construct; dND CSP construct-TMD; or sec-dND CSP construct-TMD. [0508] In some embodiments, a Plasmodium CSP polypeptide construct described herein includes a junction region, one or more minor repeat region, and a C-terminal region or corresponding portions thereof of CSP from Plasmodium falciparum, preferably from Plasmodium falciparum isolate 3D7. In some embodiments, a Plasmodium CSP polypeptide construct described herein has the structure: junction region – one or more minor repeat region – C- terminal region, wherein the regions are from CSP from Plasmodium falciparum, preferably from Plasmodium falciparum isolate 3D7. In preferred embodiments, such Plasmodium CSP polypeptide constructs have immediately following the C-terminal region a serine or a serine and a valine. In preferred embodiments, the junction region or portion thereof comprises the amino acid sequence of positions 93 to 104 of SEQ ID NO: 1, or the amino acid sequence of positions 93 to 104 of SEQ ID NO: 1 having 1, 2, 3, 4, or 5 amino acid substitutions. In preferred embodiments, the minor repeat region or portion thereof comprises the amino acid sequence of positions 105 to 128 of SEQ ID NO: 1, or an amino acid sequence having at least 99%, 98%, 97%, 96%, 95%, 90%, 85%, or 80% identity to the amino acid sequence of positions 105 to 128 of SEQ ID NO: 1. In preferred embodiments, the C- terminal region or portion thereof comprises the amino acid sequence of positions 273 to 375 of SEQ ID NO: 1, or an amino acid sequence having at least 99%, 98%, 97%, 96%, 95%, 90%, 85%, or 80% identity to the amino acid sequence of positions 273 to 375 of SEQ ID NO: 1. In some embodiments, such Plasmodium CSP polypeptide constructs have more than one minor repeat region, such as three minor repeat regions. Such a Plasmodium CSP polypeptide construct that includes all CSP regions or corresponding portions thereof as mentioned before except the N-terminal domain (i.e. exclude the N-terminal region and the N-terminal end region) and the major repeat region or corresponding portions thereof, has one or more minor repeat region and includes a serine or serine and valine immediately following the C-terminal region is referred to as a dND-dmajor CSP construct. In some embodiments, a Plasmodium CSP polypeptide construct can have the following structure: dND-dmajor CSP construct; sec-dND-dmajor CSP construct; dND-dmajor CSP construct-TMD; or sec-dND-dmajor CSP construct-TMD. N-terminal Domain and Major Repeat Region Deleted CSP Constructs with Junction Region Variants or Portions [0509] In some embodiments, a Plasmodium CSP polypeptide construct described herein includes a junction region variant or junction region portion, one or more minor repeat regions, and a C-terminal region or corresponding portions thereof of CSP from Plasmodium falciparum, preferably from Plasmodium falciparum isolate 3D7. In some embodiments, a Plasmodium CSP polypeptide construct described herein has the structure: junction region variant or junction region portion – one or more minor repeat region – C-terminal region, wherein the regions are from CSP from Plasmodium falciparum, preferably from Plasmodium falciparum isolate 3D7. In preferred embodiments, such Plasmodium CSP polypeptide constructs have immediately following the C-terminal region a serine or a serine and a valine. In preferred embodiments, the junction region variant or portion thereof comprises the amino acid sequence of positions 93 to 104 of SEQ ID NO: 1 having 1, 2, 3, 4, or 5 amino acid substitutions. In preferred embodiments, the junction region variant or portion thereof comprises the amino acid sequence of positions 93 to 104 of SEQ ID NO: 1 having a K93A mutation, an L94A mutation, or both. In preferred embodiments, the junction region portion consists of a portion of the amino acid sequence of positions 93 to 104 of SEQ ID NO: 1. In preferred embodiments, the junction region portion consists of the amino acid sequence of positions 97 to 104 of SEQ ID NO: 1. In preferred embodiments, the junction region portion comprises or consists of the amino acid sequence of positions 98 to 104 of SEQ ID NO: 1. In preferred embodiments, the minor repeat region or portion thereof comprises the amino acid sequence of positions 105 to 128 of SEQ ID NO: 1, or an amino acid sequence having at least 99%, 98%, 97%, 96%, 95%, 90%, 85%, or 80% identity to the amino acid sequence of positions 105 to 128 of SEQ ID NO: 1. In preferred embodiments, the C-terminal region or portion thereof comprises the amino acid sequence of positions 273 to 375 of SEQ ID NO: 1, or an amino acid sequence having at least 99%, 98%, 97%, 96%, 95%, 90%, 85%, or 80% identity to the amino acid sequence of positions 273 to 375 of SEQ ID NO: 1. In some embodiments, such Plasmodium CSP polypeptide constructs have more than one minor repeat region, such as three minor repeat regions. Such a Plasmodium CSP polypeptide construct that includes all CSP regions or corresponding portions thereof as mentioned before except the N-terminal domain (i.e. exclude the N-terminal region and the N-terminal end region) and the major repeat region or corresponding portions thereof, has a junction region variant or junction region portion, has one or more minor repeat region and includes a serine or serine and valine immediately following the C-terminal region is referred to as a dND-dmajor-modJ CSP construct. In some embodiments, a Plasmodium CSP polypeptide construct can have the following structure: dND-dmajor-modJ CSP construct; sec-dND-dmajor-modJ CSP construct; dND-dmajor-modJ CSP construct-TMD; or sec-dND-dmajor-modJ CSP construct-TMD. Major Repeat Region Portion and C-terminal Region Containing CSP Constructs [0510] In some embodiments, a Plasmodium CSP polypeptide construct described herein includes a major repeat region portion and a C-terminal region or corresponding portions thereof of CSP from Plasmodium falciparum, preferably from Plasmodium falciparum isolate 3D7. In some embodiments, a Plasmodium CSP polypeptide construct described herein has the structure: major repeat region portion – C-terminal region, wherein the regions are from CSP from Plasmodium falciparum, preferably from Plasmodium falciparum isolate 3D7. In preferred embodiments, such Plasmodium CSP polypeptide constructs have immediately following the C-terminal region a serine or a serine and a valine. In some embodiments, such Plasmodium CSP polypeptide constructs have between 2 and 35 repeats of the amino acid sequence NANP (SEQ ID NO: 230), preferably 18 repeats of the amino acid sequence NANP (SEQ ID NO: 230) as a major repeat portion. In preferred embodiments, the C-terminal region or portion thereof comprises the amino acid sequence of positions 273 to 375 of SEQ ID NO: 1, or an amino acid sequence having at least 99%, 98%, 97%, 96%, 95%, 90%, 85%, or 80% identity to the amino acid sequence of positions 273 to 375 of SEQ ID NO: 1. Such a Plasmodium CSP polypeptide construct that includes only a portion of the CSP major repeat region, a C-terminal region and includes a serine or serine and valine immediately following the C-terminal region, or that includes corresponding portions thereof as mentioned before, is referred to as a pmajor-CT CSP construct. In some embodiments, a Plasmodium CSP polypeptide construct can have the following structure: pmajor-CT CSP construct; sec-pmajor-CT CSP construct; pmajor-CT CSP construct-TMD; or sec- pmajor-CT CSP construct-TMD. N-terminal and C-terminal deleted CSP constructs with noncontiguous minor repeat regions [0511] In some embodiments, a Plasmodium CSP polypeptide construct described herein includes one or more of an N-terminal end region, a junction region, a minor repeat region, a major repeat region portion and a C-terminal region or corresponding portions thereof of CSP from Plasmodium falciparum, preferably from Plasmodium falciparum isolate 3D7. [0512] In some embodiments, a Plasmodium CSP polypeptide construct described herein has the structure: [junction region – minor repeat region – major repeat region portion]_x, wherein the [junction region – minor repeat region – major repeat region portion] repeats x times, and wherein the regions are from CSP from Plasmodium falciparum, preferably from Plasmodium falciparum isolate 3D7. In some embodiments, x is 2 to 5 (i.e., the [junction region – minor repeat region–major repeat region portion] repeats 2 to 5 times). In preferred embodiments, such Plasmodium CSP polypeptide constructs have three repeats of a [junction region – minor repeat region – major repeat region portion], such that the Plasmodium CSP polypeptide construct described herein has the structure: junction region – minor repeat region – major repeat region portion – junction region – minor repeat region – major repeat region portion – junction region – minor repeat region – C-terminal region. In preferred embodiments, the N- terminal end region or portion thereof comprises the amino acid sequence of positions 81 to 92 of SEQ ID NO: 1, or the amino acid sequence of positions 81 to 92 of SEQ ID NO: 1 having 1, 2, 3, 4, or 5 amino acid substitutions. In preferred embodiments, the junction region includes an R1 region (amino acids 93-97) of SEQ ID NO: 1. In preferred embodiments, the junction region repeats twice. In preferred embodiments, the junction region or portion thereof comprises a 2x repeat of the amino acid sequence of positions 93 to 104 of SEQ ID NO: 1, or the amino acid sequence of positions 93 to 104 of SEQ ID NO: 1 having 1, 2, 3, 4, or 5 amino acid substitutions. In preferred embodiments, a minor repeat region or portion thereof comprises the amino acid sequence of positions 105 to 128 of SEQ ID NO: 1, or an amino acid sequence having at least 99%, 98%, 97%, 96%, 95%, 90%, 85%, or 80% identity to the amino acid sequence of positions 105 to 128 of SEQ ID NO: 1. In some embodiments, a major repeat region portion comprises at least four repeats, at least five repeats, at least six repeats, at least seven repeats of the sequence NANP (SEQ ID NO: 230). In preferred embodiments, the major repeat region portion comprises a sequence of NANPNANPNANPNANPNANPNANP (SEQ ID NO: 311). In some embodiments, the malaria construct further comprises one or more linkers (e.g., glycine-serine linkers). In some embodiments, the malaria construct further comprises a linker (e.g., a glycine-serine linker) after each major repeat region portion sequence. In some embodiments, the malaria construct comprises a linker (e.g., a glycine-serine linker) after the last partial major repeat sequence. In some embodiments, a linker has the amino acid sequence GGSGGGGSGG (SEQ ID NO: 404). a Plasmodium CSP polypeptide construct that includes all CSP regions or corresponding portions thereof as mentioned before and includes three repeats of a [junction region – minor repeat region – major repeat region portion] is referred to as a 3xMR-dNC CSP construct. In some embodiments, a Plasmodium CSP polypeptide construct can have the following structure: 3xMR-dNC CSP construct; sec-3xMR-dNC CSP construct; 3xMR-dNC CSP construct-TMD; or sec-3xMR-dNC CSP construct-TMD. 6 NANP and 18 NANP CSP Constructs [0513] In some embodiments, a Plasmodium CSP polypeptide construct described herein includes one or more regions or portions of CSP from Plasmodium falciparum, preferably from Plasmodium falciparum isolate 3D7. [0514] In some embodiments, a Plasmodium CSP polypeptide construct described herein includes at least two repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223), two to eighteen repeats of the amino acid sequence of NANP (SEQ ID NO: 230), and a Plasmodium CSP C-terminal region or portion thereof. [0515] As referred to herein, an “18NANP CSP Construct” includes at least: three repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223), eighteen repeats of the amino acid sequence of NANP (SEQ ID NO: 230), and a Plasmodium CSP C-terminal region or antigenic portion thereof. [0516] In some embodiments, the three repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223) form a Plasmodium CSP minor repeat region. In some embodiments, a Plasmodium minor repeat region comprises or consists of an amino acid sequence having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% identity to SEQ ID NO: 226. [0517] In some embodiments, the eighteen repeats of the amino acid sequence of NANP (SEQ ID NO: 230) form an antigenic portion of the Plasmodium CSP major repeat region. In some embodiments, an antigenic portion of a Plasmodium CSP major repeat region comprises or consists of an amino acid sequence having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% identity to SEQ ID NO: 308. [0518] In some embodiments, an 18NANP CSP Construct comprises a Plasmodium CSP C-terminal region. In some embodiments, a Plasmodium CSP C-terminal region comprises or consists of an amino acid sequence having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% identity to SEQ ID NO: 238. [0519] In some embodiments, an 18NANP CSP Construct comprises a Plasmodium CSP C-terminal region variant. In some embodiments, a Plasmodium CSP C-terminal region variant comprises or consists of an amino acid sequence having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% identity to SEQ ID NO: 994. [0520] In some embodiments, an 18NANP CSP Construct comprises an antigenic portion of a Plasmodium CSP C-terminal region. In some embodiments, an antigenic portion of a Plasmodium CSP C-terminal region comprises or consists of an amino acid sequence having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% identity to SEQ ID NO: 261-267. [0521] In some embodiments, an 18NANP CSP Construct comprises an antigenic portion of a Plasmodium CSP C-terminal region variant. In some embodiments, an antigenic portion of a Plasmodium CSP C-terminal region variant comprises or consists of an amino acid sequence having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% identity to SEQ ID NO: 992-993. [0522] In some embodiments, an 18NANP CSP Construct comprises a serine or serine and valine immediately following the C-terminal region. [0523] In some embodiments, an 18NANP CSP Construct comprises a Plasmodium CSP junction region. In some embodiments, a Plasmodium CSP junction region comprises or consists of an amino acid sequence having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% identity to SEQ ID NO: 272. [0524] In some embodiments, an 18NANP CSP Construct comprises a Plasmodium CSP N-terminal end region. In some embodiments, a Plasmodium CSP N-terminal end region comprises or consists of an amino acid sequence having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% identity to SEQ ID NO: 285. [0525] In some embodiments, an 18NANP CSP Construct comprises a Plasmodium CSP N-terminal region or antigenic portion thereof. In some embodiments, a Plasmodium CSP N-terminal region comprises or consists of an amino acid sequence having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% identity to SEQ ID NO: 288. In some embodiments, an antigenic portion of a Plasmodium CSP N-terminal region comprises or consists of a Plasmodium CSP N-terminal start region. In some embodiments, a Plasmodium CSP N-terminal start region comprises or consists of an amino acid sequence having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% identity to SEQ ID NO: 1010. [0526] In some embodiments, an 18NANP CSP Construct comprises one or more linkers. In some embodiments, one or more linkers are located between regions. In some embodiments, a linker is a cleavage linker. In some embodiments, a cleavage linker is positioned within an 18NANP CSP Construct between an N-terminal region or portion thereof and a C-terminal region or portion thereof. [0527] In some embodiments, a Plasmodium CSP polypeptide construct can have the following structure: 18NANP CSP Construct; Secretory Signal (Sec) - 18NANP CSP Construct; 18NANP CSP Construct – Transmembrane Domain (TMD); Sec - 18NANP CSP Construct – TMD; Plasmodium falciparum (Pf) Sec - 18NANP CSP Construct; 18NANP CSP Construct – Pf TMD Pf Sec - 18NANP CSP Construct Pf Sec - 18NANP CSP Construct – Heterologous TMD; and Pf Sec - 18NANP CSP Construct – HSV TMD. [0528] As referred to herein, a “6NANP CSP Construct” includes at least: three repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223), six repeats of the amino acid sequence of NANP (SEQ ID NO: 230), an asparagine-alanine positioned immediately following the six repeats of the amino acid sequence of NANP (SEQ ID NO: 230), and a Plasmodium CSP C-terminal region or antigenic fragment thereof (referred to herein as a “6NANP CSP Construct”). [0529] In some embodiments, the three repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223) form a Plasmodium CSP minor repeat region. In some embodiments, a Plasmodium CSP minor repeat region comprises or consists of an amino acid sequence having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% identity to SEQ ID NO: 407. [0530] In some embodiments, a major repeat region comprises or consists of an amino acid sequence having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% identity to SEQ ID NO: 303. [0531] In some embodiments, a 6NANP CSP Construct comprises a Plasmodium CSP C-terminal region. In some embodiments, a Plasmodium CSP C-terminal region comprises or consists of an amino acid sequence having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% identity to SEQ ID NO: 238. [0532] In some embodiments, an 6NANP CSP Construct comprises a Plasmodium CSP C-terminal region variant. In some embodiments, a Plasmodium CSP C-terminal region variant comprises or consists of an amino acid sequence having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% identity to SEQ ID NO: 994. [0533] In some embodiments, a 6NANP CSP Construct comprises an antigenic portion of a Plasmodium CSP C- terminal region. In some embodiments, an antigenic portion of a Plasmodium CSP C-terminal region comprises or consists of an amino acid sequence having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% identity to SEQ ID NO: 261-267. [0534] In some embodiments, an 6NANP CSP Construct comprises an antigenic portion of a Plasmodium CSP C-terminal region variant. In some embodiments, an antigenic portion of a Plasmodium CSP C-terminal region variant comprises or consists of an amino acid sequence having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% identity to SEQ ID NO: 992-993. [0535] In some embodiments, a 6NANP CSP Construct comprises a serine or serine and valine immediately following the C-terminal region. [0536] In some embodiments, a 6NANP CSP Construct comprises a Plasmodium CSP junction region. In some embodiments, a Plasmodium CSP junction region comprises or consists of an amino acid sequence having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% identity to SEQ ID NO: 272. [0537] In some embodiments, a 6NANP CSP Construct comprises a Plasmodium CSP N-terminal end region. In some embodiments, a Plasmodium CSP N-terminal end region comprises or consists of an amino acid sequence having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% identity to SEQ ID NO: 285. [0538] In some embodiments, a 6NANP CSP Construct comprises a Plasmodium CSP N-terminal region or antigenic portion thereof. In some embodiments, a Plasmodium CSP N-terminal region comprises or consists of an amino acid sequence having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% identity to SEQ ID NO: 288. [0539] In some embodiments, a 6NANP CSP Construct comprises one or more linkers. In some embodiments, one or more linkers are located between regions. [0540] In some embodiments, a Plasmodium CSP polypeptide construct can have the following structure: 6NANP CSP Construct; Sec - 6NANP CSP Construct; 6NANP CSP Construct – TMD; Sec - 6NANP CSP Construct – TMD; Pf Sec - 6NANP CSP Construct; 6NANP CSP Construct – Pf TMD; Pf Sec - 6NANP CSP Construct – Pf TMD; Pf Sec - 6NANP CSP Construct – Heterologous TMD; Pf Sec - 6NANP CSP Construct – HSV TMD; Heterologous Sec - 6NANP CSP Construct – Heterologous TMD; HSV Sec - 6NANP CSP Construct – HSV TMD; Heterologous Sec - 6NANP CSP Construct – Heterologous TMD; Heterologous Sec - 6NANP CSP Construct – Multimerization Domain; or Heterologous Sec - 6NANP CSP Construct – Self-Assembly Domain. T-Cell C-Term CSP Constructs [0541] In some embodiments, a Plasmodium CSP polypeptide construct described herein includes one or more regions or portions of CSP from Plasmodium falciparum, preferably from Plasmodium falciparum isolate 3D7. [0542] As used herein, a “T-cell C-term CSP Construct” includes at least: a portion of a Plasmodium CSP C- terminal region, wherein the portion of the Plasmodium CSP C-terminal region comprises an amino acid sequence according to SEQ ID NO: 261 (YLX₃X₄IQX₅SLST), wherein X₃ is N or K, X₄ is K, I, or R, and X₅ is N or Y. In some embodiments, a portion of a Plasmodium CSP C-terminal region comprises an amino acid sequence according to SEQ ID NO: 261-267. In some embodiments, a portion of a Plasmodium CSP C-terminal region comprises or consists of an amino acid sequence according to SEQ ID NO: 238. [0543] In some embodiments, a T-cell C-term CSP Construct comprises a serine or serine and valine immediately following the C-terminal region. [0544] In some embodiments, a T-cell C-term CSP Construct further comprises a Plasmodium CSP major repeat region or an antigenic portion thereof. In some embodiments, a T-cell C-term CSP Construct further comprises a Plasmodium CSP major repeat region. In some embodiments, a Plasmodium CSP major repeat region comprises or consists of an amino acid sequence having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% identity to SEQ ID NO: 156. In some embodiments, a T-cell C-term CSP Construct comprises a portion of a Plasmodium CSP major repeat region. In some embodiments, a portion of the Plasmodium CSP major repeat region comprises or consists of six repeats of the amino acid sequence of NANP (SEQ ID NO: 230). In some embodiments, a portion of the Plasmodium CSP major repeat region comprises or consists of an amino acid sequence having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% identity to SEQ ID NO: 303. In some embodiments, an asparagine-alanine is positioned immediately following the six repeats of the amino acid sequence of NANP. In some embodiments, a portion of the Plasmodium CSP major repeat region comprises or consists of 18 repeats of the amino acid sequence of NANP (SEQ ID NO: 230). In some embodiments, a portion of the Plasmodium CSP major repeat region comprises or consists of an amino acid sequence having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% identity to SEQ ID NO: 308. [0545] In some embodiments, a T-cell C-term CSP Construct comprises a Plasmodium CSP minor repeat region. In some embodiments, a Plasmodium CSP minor repeat region comprises or consists of the three repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223). In some embodiments, a Plasmodium CSP minor repeat region comprises or consists of an amino acid sequence having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% identity to SEQ ID NO: 407. [0546] In some embodiments, a T-cell C-term CSP Construct comprises a Plasmodium CSP junction region. In some embodiments, a Plasmodium CSP junction region comprises or consists of an amino acid sequence having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% identity to SEQ ID NO: 272. [0547] In some embodiments, a T-cell C-term CSP Construct comprises a Plasmodium CSP N-terminal end region. In some embodiments, a Plasmodium CSP N-terminal end region comprises or consists of an amino acid sequence having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% identity to SEQ ID NO: 285. [0548] In some embodiments, a T-cell C-term CSP Construct comprises a Plasmodium CSP N-terminal region or antigenic portion thereof. In some embodiments, a Plasmodium CSP N-terminal region comprises or consists of an amino acid sequence having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% identity to SEQ ID NO: 288. [0549] In some embodiments, a T-cell C-term CSP Construct comprises one or more linkers. In some embodiments, one or more linkers are located between regions. [0550] In some embodiments, a Plasmodium CSP polypeptide construct can have the following structure: T-cell C-term CSP Construct; Sec – T-cell C-term CSP Construct; T-cell C-term CSP Construct – TMD; Sec – T-cell C-term CSP Construct – TMD; Heterologous Sec - T-cell C-term CSP Construct – Multimerization Domain; or Heterologous Sec - T-cell C-term CSP Construct – Self-Assembly Domain. Additional Select Exemplary CSP Constructs [0551] In some embodiments, a Plasmodium CSP polypeptide construct can have the following structure: Pf Sec – N-terminal Region – N-terminal End Region – Junction Region – Minor Repeat Region – Antigenic Portion of a Major Repeat Region – C-terminal Region; Pf Sec – N-terminal Region – N-terminal End Region – Junction Region – Minor Repeat Region – Antigenic Portion of a Major Repeat Region – C-terminal Region – Pf TMD; N-terminal Region – N-terminal End Region – Junction Region – Minor Repeat Region –Major Repeat Region – C-terminal Region Variant; Sec – N-terminal Region – N-terminal End Region – Junction Region – Minor Repeat Region – Major Repeat Region – C-terminal Region Variant; N-terminal Region – N-terminal End Region – Junction Region – Minor Repeat Region – Major Repeat Region – C-terminal Region Variant – TMD; Sec – N-terminal Region – N-terminal End Region – Junction Region – Minor Repeat Region – Major Repeat Region – C-terminal Region Variant – TMD; Pf Sec – N-terminal Region – N-terminal End Region – Junction Region – Minor Repeat Region – Major Repeat Region – C-terminal Region Variant; Pf Sec – N-terminal Region – N-terminal End Region – Junction Region – Minor Repeat Region – Major Repeat Region – C-terminal Region Variant – Pf TMD; Pf Sec – N-Terminal Region – N-Terminal End Region – Cleavable Linker – Junction Region – Minor Repeat Region – Antigenic Portion of a Major Repeat Region –C-Terminal Region – HSV TMD; Pf Sec – N-Terminal Region – N-Terminal End Region – Junction Region – Minor Repeat Region – Antigenic Portion of a Major Repeat Region – C-Terminal Region; HSV Sec – Junction Region – Minor Repeat Region – Antigenic Portion of a Major Repeat Region – Antigenic Portion of C-Terminal Region – Multimerization Domain; HSV Sec – Junction Region – Minor Repeat Region – Antigenic Portion of a Major Repeat Region – Antigenic Portion of C-Terminal Region – Self-Assembly Domain; or HSV Sec – Junction Region – Minor Repeat Region – Antigenic Portion of a Major Repeat Region – Antigenic Portion of C-Terminal Region – HSV TMD. Exemplary Construct Sequences [0552] In some embodiments, a Plasmodium CSP polypeptide construct described herein has an amino acid sequence provided in Table 4, and/or is encoded by a nucleotide sequence provided in Table 11. Table 4: Amino Acid Sequences Encoding Exemplary Plasmodium CSP Polypeptide Constructs C. Common Features of Plasmodium Polypeptide Constructs [0553] Plasmodium polypeptide constructs as described herein (e.g., Plasmodium T-cell string polypeptide constructs as described herein, Plasmodium CSP polypeptide constructs as described, or both) can have additional features. 1. Secretory Signals [0554] In some embodiments, a Plasmodium polypeptide construct described herein includes a secretory signal, e.g., that is functional in mammalian cells. In some embodiments, a secretory signal comprises or consists of a Plasmodium secretory signal. In some embodiments, a Plasmodium secretory signal comprises or consists of a Plasmodium CSP secretory signal. In some embodiments, a Plasmodium CSP secretory signal is from Plasmodium falciparum. In some embodiments, a Plasmodium CSP secretory signal is from Plasmodium falciparum isolate 3D7 (SEQ ID NO.332). [0555] In some embodiments, a utilized secretory signal is a heterologous secretory signal. In some embodiments, a heterologous secretory signal comprises or consists of a non-human secretory signal. In some embodiments, a heterologous secretory signal comprises or consists of a viral secretory signal. In some embodiments, a viral secretory signal comprises or consists of an HSV secretory signal (e.g., an HSV-1 or HSV-2 secretory signal). In some embodiments, an HSV secretory signal comprises or consists of an HSV glycoprotein D (gD) secretory signal. In some embodiments, an HSV secretory signal comprises or consists of an HSV glycoprotein D (gD) secretory signal according to SEQ ID NO: 323 (MGGAAARLGAVILFVVIVGLHGVRG). In some embodiments, a secretory signal comprises or consists of an Ebola virus secretory signal. In some embodiments, an Ebola virus secretory signal comprises or consists of an Ebola virus spike glycoprotein (SGP) secretory signal. [0556] In some embodiments, a secretory signal is characterized by a length of about 15 to 30 amino acids. [0557] In some embodiments, a secretory signal is positioned at the N-terminus of a Plasmodium polypeptide construct described herein. In some embodiments, a secretory signal preferably allows transport of a Plasmodium polypeptide construct with which it is associated into a defined cellular compartment, preferably a cell surface, endoplasmic reticulum (ER) or endosomal-lysosomal compartment. [0558] In some embodiments, a secretory signal is selected from an S1S2 secretory signal (aa 1-19), an immunoglobulin secretory signal (aa 1-22), a human SPARC secretory signal, a human insulin isoform 1 secretory signal, a human albumin secretory signal, etc. Those skilled in the art will be aware of other secretory signal such as, for example, as disclosed in WO2017/081082 (e.g., SEQ ID NOs: 1-1115 and 1728, or fragments variants thereof), which is herein incorporated by reference in its entirety. [0559] In some embodiments, a Plasmodium polypeptide construct described herein does not comprise a secretory signal. [0560] In some embodiments, a secretory signal is one listed in Table 5, or a secretory signal having 1, 2, 3, 4, or 5 amino acid differences relative thereto. In some embodiments, a signal sequence is selected from those included in the Table 5 below and/or those encoded by the sequences in Table 6 below. Table 5: Exemplary secretory signals Table 6: Exemplary polynucleotide sequences encoding secretory signals

2. Transmembrane Regions [0561] In some embodiments, a Plasmodium polypeptide construct described herein includes a transmembrane region (also referred to herein as a “transmembrane domain”). In some embodiments, a transmembrane region comprises or consists of a Plasmodium transmembrane region. In some embodiments, a utilized transmembrane region is one that is normally associated with CSP in nature. In some embodiments, a Plasmodium transmembrane region comprises or consists of a Plasmodium CSP glycosylphosphatidylinositol (GPI) anchor region, e.g., SEQ ID NO: 385. [0562] In some embodiments, a utilized transmembrane region is a heterologous transmembrane region. Transmembrane regions are known in the art, any of which can be utilized in a Plasmodium polypeptide construct described herein. In some embodiments, a transmembrane region comprises or is a transmembrane domain of Hemagglutinin (HA) of Influenza virus, Env of HIV-1, equine infectious anaemia virus (EIAV), murine leukaemia virus (MLV), mouse mammary tumor virus, G protein of vesicular stomatitis virus (VSV), Rabies virus, or a seven transmembrane domain receptor. [0563] In some embodiments, a heterologous transmembrane region does not comprise a hemagglutinin transmembrane region. [0564] In some embodiments, a heterologous transmembrane region comprises or consists of a non-human transmembrane region. In some embodiments, a heterologous transmembrane region comprises or consists of a viral transmembrane region. In some embodiments, a heterologous transmembrane region comprises or consists of an HSV transmembrane region, e.g., an HSV-1 or HSV-2 transmembrane region. In some embodiments, an HSV transmembrane region comprises or consists of an HSV gD transmembrane region, e.g., comprising or consisting of an amino acid sequence of GLIAGAVGGSLLAALVICGIVYWMRRHTQKAPKRIRLPHIR (SEQ ID NO: 379). [0565] In some embodiments, a heterologous transmembrane region comprises or consists of a human transmembrane region. In some embodiments, a human transmembrane region comprises or consists of a human decay accelerating factor glycosylphosphatidylinositol (hDAF-GPI) anchor region. In some embodiments, an hDAF- GPI anchor region comprises or consists of an amino acid sequence of PNKGSGTTSGTTRLLSGHTCFTLTGLLGTLVTMGLLT (SEQ ID NO: 382). [0566] In some embodiments, a transmembrane region is located at the N-terminus of a Plasmodium polypeptide construct. In some embodiments, a transmembrane region is located at the C-terminus of a Plasmodium polypeptide construct. In some embodiments, a transmembrane region is not located at the N-terminus or C- terminus of a Plasmodium polypeptide construct. [0567] In some embodiments, a Plasmodium polypeptide construct described herein does not comprise a transmembrane region. 3. Linkers [0568] In some embodiments, a Plasmodium polypeptide construct described herein includes one or more linkers. In some embodiments, a linker is or comprises 2, 3, 4, 5, 6, 7, 8, 9, 10 or more amino acids. In some embodiments, a linker is or comprises no more than about 30, 25, 20, 15, 10 or fewer amino acids. A linker can include any amino acid sequence and is not limited to any particular amino acids. In some embodiments, a linker comprises one or more glycine (G) amino acids. In some embodiments, a linker comprises one or more serine (S) amino acids. In some embodiments, a linker comprises a glycine-serine linker. A “glycine-serine linker” as used herein refers to a linker that comprises predominantly (e.g., 80% or more) glycine and serine amino acids. In some embodiments, a linker includes amino acids selected based on a cleavage predictor to generate highly-cleavable linkers. [0569] In some embodiments, a linker is or comprises S-G4-S-G4-S (SEQ ID NO: 405). In some embodiments, a linker is or comprises GSPGSGSGS (SEQ ID NO: 455). In some embodiments, a linker is or comprises GGSGGGGSGG (SEQ ID NO: 404). In some embodiments, a linker is or comprises AGNRVRRSVG (SEQ ID NO: 412). In some embodiments, a linker is one presented in Table 7. In some embodiments, a linker is or comprises a sequence as set forth in WO2017/081082, which is incorporated herein by reference in its entirety (see SEQ ID NOs: 1509-1565, or a fragment or variant thereof). [0570] In some embodiments, a Plasmodium T-cell string polypeptide construct described herein comprises a linker between two Plasmodium T-cell antigens or between two or more antigenic polypeptide fragments from the same T-cell antigen. In some embodiments, a Plasmodium CSP polypeptide construct described herein comprises a linker between a C-terminal region or portion thereof and a transmembrane region. In some embodiments, a Plasmodium CSP polypeptide construct described herein comprises a linker after a minor repeat sequence. In some embodiments, a Plasmodium CSP polypeptide construct described herein comprises a linker after a major repeat sequence or portion thereof. [0571] Exemplary linkers are provided in the following Table 7: Table 7: Exemplary linkers D. Polyribonucleotide Constructs [0572] Polyribonucleotides described herein encode one or more constructs (e.g., one or more Plasmodium T- cell string polypeptide constructs, one or more Plasmodium CSP polypeptide constructs, or both) as described herein. In some embodiments, polyribonucleotides described herein can be included in an RNA construct. In some embodiments, an RNA construct provided herein comprises a nucleotide sequence that encodes a 5’UTR and/or a 3’ UTR. In some embodiments, polyribonucleotides described herein can comprise a ribonucleotide sequence that encodes a polyA tail. In some embodiments, polyribonucleotides described herein may comprise a 5’ cap, which may be incorporated during transcription, or joined to a polyribonucleotide post-transcription. 1. Exemplary Polyribonucleotides Features 5' Cap [0573] A structural feature of mRNAs is cap structure at five-prime end (5’). Natural eukaryotic mRNA comprises a 7-methylguanosine cap linked to the mRNA via a 5´ to 5´-triphosphate bridge resulting in cap0 structure (m⁷GpppN). In most eukaryotic mRNA and some viral mRNA, further modifications can occur at the 2'-hydroxy-group (2’-OH) (e.g., the 2'-hydroxyl group may be methylated to form 2'-O-Me) of the first and subsequent nucleotides producing “cap1” and “cap2” five-prime ends, respectively). Diamond, et al., (2014) Cytokine & growth Factor Reviews, 25:543–550, which is herein incorporated by reference in its entirety, reported that cap0-mRNA cannot be translated as efficiently as cap1-mRNA in which the role of 2'-O-Me in the penultimate position at the mRNA 5’ end is determinant. Lack of the 2'-O-met has been shown to trigger innate immunity and activate IFN response. Daffis, et al. (2010) Nature, 468:452-456; and Züst et al. (2011) Nature Immunology, 12:137-143, which are herein incorporated by reference in their entirety. [0574] RNA capping is well researched and is described, e.g., in Decroly E et al. (2012) Nature Reviews 10: 51- 65; and in Ramanathan A. et al., (2016) Nucleic Acids Res; 44(16): 7511–7526, the entire contents of each of which is hereby incorporated by reference. For example, in some embodiments, a 5’-cap structure which may be suitable in the context of the present invention is a cap0 (methylation of the first nucleobase, e.g., m⁷GpppN), cap1 (additional methylation of the ribose of the adjacent nucleotide of m⁷GpppN), cap2 (additional methylation of the ribose of the 2nd nucleotide downstream of the m⁷GpppN), cap3 (additional methylation of the ribose of the 3rd nucleotide downstream of the m⁷GpppN), cap4 (additional methylation of the ribose of the 4th nucleotide downstream of the m⁷GpppN), ARCA (“anti-reverse cap analogue”), modified ARCA (e.g. phosphothioate modified ARCA), inosine, N1 - methyl-guanosine, 2’-fluoro-guanosine, 7-deaza-guanosine, 8-oxo-guanosine, 2-amino-guanosine, LNA-guanosine, and 2-azido-guanosine. [0575] The term “5'-cap” as used herein refers to a structure found on the 5'-end of an RNA, e.g., mRNA, and generally includes a guanosine nucleotide connected to an RNA, e.g., mRNA, via a 5'- to 5'-triphosphate linkage (also referred to as Gppp or G(5')ppp(5')). In some embodiments, a guanosine nucleoside included in a 5’ cap may be modified, for example, by methylation at one or more positions (e.g., at the 7-position) on a base (guanine), and/or by methylation at one or more positions of a ribose. In some embodiments, a guanosine nucleoside included in a 5’ cap comprises a 3’O methylation at a ribose (3’OMeG). In some embodiments, a guanosine nucleoside included in a 5’ cap comprises methylation at the 7-position of guanine (m⁷G). In some embodiments, a guanosine nucleoside included in a 5’ cap comprises methylation at the 7-position of guanine and a 3’ O methylation at a ribose (m⁷(3’OMeG)). It will be understood that the notation used in the above paragraph, e.g., “(m₂ ^7,3’-O)G” or “m⁷(3’OMeG)”, applies to other structures described herein. [0576] In some embodiments, providing an RNA with a 5'-cap disclosed herein may be achieved by in vitro transcription, in which a 5'-cap is co-transcriptionally expressed into an RNA strand, or may be attached to an RNA post-transcriptionally using capping enzymes. In some embodiments, co-transcriptional capping with a cap disclosed improves the capping efficiency of an RNA compared to co-transcriptional capping with an appropriate reference comparator. In some embodiments, improving capping efficiency can increase a translation efficiency and/or translation rate of an RNA, and/or increase expression of an encoded polypeptide. In some embodiments, alterations to polynucleotides generates a non-hydrolyzable cap structure which can, for example, prevent decapping and increase RNA half-life. [0577] In some embodiments, a utilized 5’ caps is a cap0, a cap1, or cap2 structure. See, e.g., Fig. 1 of Ramanathan A et al., and Fig. 1 of Decroly E et al., each of which is incorporated herein by reference in its entirety. See, e.g., Fig. 1 of Ramanathan A et al., and Fig. 1 of Decroly E et al., each of which is incorporated herein by reference in its entirety. In some embodiments, an RNA described herein comprises a cap1 structure. In some embodiments, an RNA described herein comprises a cap2. [0578] In some embodiments, an RNA described herein comprises a cap0 structure. In some embodiments, a cap0 structure comprises a guanosine nucleoside methylated at the 7-position of guanine ((m⁷)G). In some embodiments, such a cap0 structure is connected to an RNA via a 5'- to 5'-triphosphate linkage and is also referred to herein as (m⁷)Gppp. In some embodiments, a cap0 structure comprises a guanosine nucleoside methylated at the 2’-position of the ribose of guanosine. In some embodiments, a cap0 structure comprises a guanosine nucleoside methylated at the 3’-position of the ribose of guanosine. In some embodiments, a guanosine nucleoside included in a 5’ cap comprises methylation at the 7-position of guanine and at the 2’-position of the ribose ((m₂ ^7,2’-O)G). In some embodiments, a guanosine nucleoside included in a 5’ cap comprises methylation at the 7-position of guanine and at the 2’-position of the ribose ((m₂ ^7,3’-O)G). [0579] In some embodiments, a cap1 structure comprises a guanosine nucleoside methylated at the 7-position of guanine ((m⁷)G) and optionally methylated at the 2’ or 3’ position of the ribose, and a 2’O methylated first nucleotide in an RNA ((m^2’-O)N₁). In some embodiments, a cap1 structure comprises a guanosine nucleoside methylated at the 7-position of guanine ((m⁷)G) and the 3’ position of the ribose, and a 2’O methylated first nucleotide in an RNA ((m^2’-O)N₁). In some embodiments, a cap1 structure is connected to an RNA via a 5'- to 5'- triphosphate linkage and is also referred to herein as, e.g., ((m⁷)Gppp(^2'-O)N₁) or (m₂ ^7,3’-O)Gppp(^2'-O)N₁), wherein N₁ is as defined and described herein. In some embodiments, a cap1 structure comprises a second nucleotide, N₂, which is at position 2 and is chosen from A, G, C, or U, e.g., (m⁷)Gppp(^2'-O)N₁pN₂ or (m₂ ^7,3’-O)Gppp(^2'-O)N₁pN₂, wherein each of N₁ and N₂ is as defined and described herein. [0580] In some embodiments, a cap2 structure comprises a guanosine nucleoside methylated at the 7-position of guanine ((m⁷)G) and optionally methylated at the 2’ or 3’ position of the ribose, and a 2’O methylated first and second nucleotides in an RNA ((m^2’-O)N₁p(m^2’-O)N₂). In some embodiments, a cap2 structure comprises a guanosine nucleoside methylated at the 7-position of guanine ((m⁷)G) and the 3’ position of the ribose, and a 2’O methylated first and second nucleotide in an RNA. In some embodiments, a cap2 structure is connected to an RNA via a 5'- to 5'- triphosphate linkage and is also referred to herein as, e.g., ((m⁷)Gppp(^2'-O)N₁p(^2'-O)N₂) or (m₂ ^7,3’-O)Gppp(^2'-O)N₁p(^{2'- O})N₂), wherein each of N₁ and N₂ is as defined and described herein. [0581] In some embodiments, the 5’ cap is a dinucleotide cap structure. In some embodiments, the 5’ cap is a dinucleotide cap structure comprising N₁, wherein N₁ is as defined and described herein. In some embodiments, the 5’ cap is a dinucleotide cap G*N₁, wherein N₁ is as defined above and herein, and G* comprises a structure of formula (I): or a salt thereof, wherein each R^{2 3} d X is O o [0582] In some embodiments, R² is -OH. In some embodiments, R² is -OCH₃. In some embodiments, R³ is - OH. In some embodiments, R³ is -OCH₃. In some embodiments, R² is -OH and R³ is -OH. In some embodiments, R² is -OH and R³ is -CH₃. In some embodiments, R² is -CH₃ and R³ is -OH. In some embodiments, R² is -CH₃ and R³ is - CH₃. [0583] In some embodiments, X is O. In some embodiments, X is S. [0584] In some embodiments, the 5’ cap is a dinucleotide cap0 structure (e.g., (m⁷)GpppN₁, (m₂ ^7,2’-O)GpppN₁, (m₂ ^7,3’-O)GpppN₁, (m⁷)GppSpN₁, (m₂ ^7,2’-O)GppSpN₁, or (m₂ ^7,3’-O)GppSpN₁), wherein N₁ is as defined and described herein. In some embodiments, the 5’ cap is a dinucleotide cap0 structure (e.g., (m⁷)GpppN₁, (m₂ ^7,2’-O)GpppN₁, (m₂ ^{7,3’- O})GpppN₁, (m⁷)GppSpN₁, (m₂ ^7,2’-O)GppSpN₁, or (m₂ ^7,3’-O)GppSpN₁), wherein N₁ is G. In some embodiments, the 5’ cap is a dinucleotide cap0 structure (e.g., (m⁷)GpppN₁, (m₂ ^7,2’-O)GpppN₁, (m₂ ^7,3’-O)GpppN₁, (m⁷)GppSpN₁, (m₂ ^{7,2’- O})GppSpN₁, or (m₂ ^7,3’-O)GppSpN₁), wherein N₁ is A, U, or C. In some embodiments, the 5’ cap is a dinucleotide cap1 structure (e.g., (m⁷)Gppp(m^2’-O)N₁, (m₂ ^7,2’-O)Gppp(m^2’-O)N₁, (m₂ ^7,3’-O)Gppp(m^2’-O)N₁, (m⁷)GppSp(m^2’-O)N₁, (m₂ ^{7,2’- O})GppSp(m^2’-O)N₁, or (m₂ ^7,3’-O)GppSp(m^2’-O)N₁), wherein N₁ is as defined and described herein. In some embodiments, the 5’ cap is selected from the group consisting of (m⁷)GpppG (“Ecap0”), (m⁷)Gppp(m^2’-O)G (“Ecap1”), (m₂ ^{7,3’- O})GpppG (“ARCA” or “D1”), and (m₂ ^7,2’-O)GppSpG (“beta-S-ARCA”). In some embodiments, the 5’ cap is (m⁷)GpppG (“Ecap0”), having a structure: or a salt thereof. [0585] In some embodiments, the 5’ cap is (m⁷)Gppp(m^2’-O)G (“Ecap1”), having a structure: or a salt thereof. [0586] In some embodiments, the 5’ cap is (m₂ ^7,3’-O)GpppG (“ARCA” or “D1”), having a structure: or a salt thereof. [0587] In some embodiments, the 5’ cap is (m₂ ^7,3’-O)GppSpG (“beta-S-ARCA”), having a structure:

or a salt thereof. [0588] In some embodiments, the 5’ cap is a trinucleotide cap structure. In some embodiments, the 5’ cap is a trinucleotide cap structure comprising N₁pN₂, wherein N₁ and N₂ are as defined and described herein. In some embodiments, the 5’ cap is a dinucleotide cap G*N₁pN₂, wherein N₁ and N₂ are as defined above and herein, and G* comprises a structure of formula (I): or a salt thereof, wherein R², R³, and X are as defined and described herein. [0589] In some embodiments, the 5’ cap is a trinucleotide cap0 structure (e.g. (m⁷)GpppN₁pN₂, (m₂ ^{7,2’- O})GpppN₁pN₂, or (m₂ ^7,3’-O)GpppN₁pN₂), wherein N₁ and N₂ are as defined and described herein). In some embodiments, the 5’ cap is a trinucleotide cap1 structure (e.g., (m⁷)Gppp(m^2’-O)N₁pN₂, (m₂ ^7,2’-O)Gppp(m^2’-O)N₁pN₂, (m₂ ^7,3’-O)Gppp(m^2’-O)N₁pN₂), wherein N₁ and N₂ are as defined and described herein. In some embodiments, the 5’ cap is a trinucleotide cap2 structure (e.g., (m⁷)Gppp(m^2’-O)N₁p(m^2’-O)N₂, (m₂ ^7,2’-O)Gppp(m^2’-O)N₁p(m^2’-O)N₂, (m₂ ^{7,3’- O})Gppp(m^2’-O)N₁p(m^2’-O)N₂), wherein N₁ and N₂ are as defined and described herein. In some embodiments, the 5’ cap is selected from the group consisting of (m2^7,3’-O)Gppp(m^2’-O)ApG (“CleanCap AG”, “CC413”), (m2^7,3’-O)Gppp(m^{2’- O})GpG (“CleanCap GG”), (m⁷)Gppp(m^2’-O)ApG, (m⁷)Gppp(m^2’-O)GpG, (m₂ ^7,3’-O)Gppp(m₂ ^6,2’-O)ApG, and (m⁷)Gppp(m^{2’- O})ApU. [0590] In some embodiments, the 5’ cap is (m₂ ^7,3’-O)Gppp(m^2’-O)ApG (“CleanCap AG”, “CC413”), having a structure:

or a salt thereof. [0591] In some embodiments, the 5’ cap is (m₂ ^7,3’-O)Gppp(m^2’-O)GpG (“CleanCap GG”), having a structure: or a salt thereof. [0592] In some embodiments, the 5’ cap is (m⁷)Gppp(m^2’-O)ApG, having a structure:

or a salt thereof. [0593] In some embodiments, the 5’ cap is (m⁷)Gppp(m^2’-O)GpG, having a structure: or a salt thereof. [0594] In some embodiments, the 5’ cap is (m₂ ^7,3’-O)Gppp(m₂ ^6,2’-O)ApG, having a structure:

or a salt thereof. [0595] In some embodiments, the 5’ cap is (m⁷)Gppp(m^2’-O)ApU, having a structure: or a salt thereof. [0596] In some embodiments, the 5’ cap is a tetranucleotide cap structure. In some embodiments, the 5’ cap is a tetranucleotide cap structure comprising N₁pN₂pN₃, wherein N₁, N₂, and N₃ are as defined and described herein. In some embodiments, the 5’ cap is a tetranucleotide cap G*N₁pN₂pN₃, wherein N₁, N₂, and N₃ are as defined above and herein, and G* comprises a structure of formula (I): or a salt thereof, wherein R², R³, and X are as defined and described herein. [0597] In some embodiments, the 5’ cap is a tetranucleotide cap0 structure (e.g. (m⁷)GpppN₁pN₂pN₃, (m₂ ^{7,2’- O})GpppN₁pN₂pN₃, or (m₂ ^7,3’-O)GpppN₁N₂pN₃), wherein N₁, N₂, and N₃ are as defined and described herein). In some embodiments, the 5’ cap is a tetranucleotide Cap1 structure (e.g., (m⁷)Gppp(m^2’-O)N₁pN₂pN₃, (m₂ ^7,2’-O)Gppp(m^{2’- O})N₁pN₂pN₃, (m₂ ^7,3’-O)Gppp(m^2’-O)N₁pN₂N₃), wherein N₁, N₂, and N₃ are as defined and described herein. In some embodiments, the 5’ cap is a tetranucleotide Cap2 structure (e.g., (m⁷)Gppp(m^2’-O)N₁p(m^2’-O)N₂pN₃, (m₂ ^{7,2’- O})Gppp(m^2’-O)N₁p(m^2’-O)N₂pN₃, (m₂ ^7,3’-O)Gppp(m^2’-O)N₁p(m^2’-O)N₂pN₃), wherein N₁, N₂, and N₃ are as defined and described herein. In some embodiments, the 5’ cap is selected from the group consisting of (m₂ ^7,3’-O)Gppp(m^{2’- O})Ap(m^2’-O)GpG, (m₂ ^7,3’-O)Gppp(m^2’-O)Gp(m^2’-O)GpC, (m⁷)Gppp(m^2’-O)Ap(m^2’-O)UpA, and (m⁷)Gppp(m^2’-O)Ap(m^2’-O)GpG. [0598] In some embodiments, the 5’ cap is (m₂ ^7,3’-O)Gppp(m^2’-O)Ap(m^2’-O)GpG, having a structure: or a salt thereof. [0599] In some embodiments, the 5’ cap is (m₂ ^7,3’-O)Gppp(m^2’-O)Gp(m^2’-O)GpC, having a structure:

or a salt thereof. [0600] In some embodiments, the 5’ cap is (m⁷)Gppp(m^2’-O)Ap(m^2’-O)UpA, having a structure: or a salt thereof. [0601] In some embodiments, the 5’ cap is (m⁷)Gppp(m^2’-O)Ap(m^2’-O)GpG, having a structure:

[ 0602] In some embodiments, a 5 UTR utilized in accordance with the present disclosure comprises a cap proximal sequence, e.g., as disclosed herein. In some embodiments, a cap proximal sequence comprises a sequence adjacent to a 5’ cap. In some embodiments, a cap proximal sequence comprises nucleotides in positions +1, +2, +3, +4, and/or +5 of an RNA polynucleotide. [0603] In some embodiments, a cap structure comprises one or more polynucleotides of a cap proximal sequence. In some embodiments, a cap structure comprises an m⁷ Guanosine cap and nucleotide +1 (N₁) of an RNA polynucleotide. In some embodiments, a cap structure comprises an m⁷ Guanosine cap and nucleotide +2 (N₂) of an RNA polynucleotide. In some embodiments, a cap structure comprises an m⁷ Guanosine cap and nucleotides +1 and +2 (N₁ and N₂) of an RNA polynucleotide. In some embodiments, a cap structure comprises an m⁷ Guanosine cap and nucleotides +1, +2, and +3 (N₁, N₂, and N₃) of an RNA polynucleotide. [0604] Those skilled in the art, reading the present disclosure, will appreciate that, in some embodiments, one or more residues of a cap proximal sequence (e.g., one or more of residues +1, +2, +3, +4, and/or +5) may be included in an RNA by virtue of having been included in a cap entity (e.g., a cap1 or cap2 structure, etc.); alternatively, in some embodiments, at least some of the residues in a cap proximal sequence may be enzymatically added (e.g., by a polymerase such as a T7 polymerase). For example, in certain exemplified embodiments where a m₂ ^7,3’-OGppp(m₁ ^2’-O)ApG cap is utilized, +1 (i.e., N₁) and +2 (i.e., N₂) are the (m₁ ^2’-O)A and G residues of the cap, and +3, +4, and +5 are added by polymerase (e.g., T7 polymerase). [0605] In some embodiments, the 5’ cap is a dinucleotide cap structure, wherein the cap proximal sequence comprises N₁ of the 5’ cap, where N₁ is any nucleotide, e.g., A, C, G or U. In some embodiments, the 5’ cap is a trinucleotide cap structure (e.g., the trinucleotide cap structures described above and herein), wherein the cap proximal sequence comprises N₁ and N₂ of the 5’ cap, wherein N₁ and N₂ are independently any nucleotide, e.g., A, C, G or U. In some embodiments, the 5’ cap is a tetranucleotide cap structure (e.g., the trinucleotide cap structures described above and herein), wherein the cap proximal sequence comprises N₁, N₂, and N₃ of the 5’ cap, wherein N₁, N₂, and N₃ are any nucleotide, e.g., A, C, G or U. [0606] In some embodiments, e.g., where the 5’ cap is a dinucleotide cap structure, a cap proximal sequence comprises N₁ of a the 5’ cap, and N₂, N₃, N and N₅, wherein N₁ to N₅ correspond to positions +1, +2, +3, +4, and/or +5 of an RNA polynucleotide. In some embodiments, e.g., where the 5’ cap is a trinucleotide cap structure, a cap proximal sequence comprises N₁ and N₂ of a the 5’ cap, and N₃, N₄ and N₅, wherein N₁ to N₅ correspond to positions +1, +2, +3, +4, and/or +5 of an RNA polynucleotide. In some embodiments, e.g., where the 5’ cap is a tetranucleotide cap structure, a cap proximal sequence comprises N₁, N₂, and N₃ of a the 5’ cap, and N₄ and N₅, wherein N₁ to N₅ correspond to positions +1, +2, +3, +4, and/or +5 of an RNA polynucleotide. [0607] In some embodiments, N₁ is A. In some embodiments, N₁ is C. In some embodiments, N₁ is G. In some embodiments, N₁ is U. In some embodiments, N₂ is A. In some embodiments, N₂ is C. In some embodiments, N₂ is G. In some embodiments, N₂ is U. In some embodiments, N₃ is A. In some embodiments, N₃ is C. In some embodiments, N₃ is G. In some embodiments, N₃ is U. In some embodiments, N₄ is A. In some embodiments, N₄ is C. In some embodiments, N₄ is G. In some embodiments, N₄ is U. In some embodiments, N₅ is A. In some embodiments, N₅ is C. In some embodiments, N₅ is G. In some embodiments, N₅ is U. It will be understood that, each of the embodiments described above and herein (e.g., for N₁ through N₅) may be taken singly or in combination and/or may be combined with other embodiments of variables described above and herein (e.g., 5’ caps). 5' UTR [0608] In some embodiments, a nucleic acid (e.g., DNA, RNA) utilized in accordance with the present disclosure comprises a 5'-UTR. In some embodiments, 5’-UTR may comprise a plurality of distinct sequence elements; in some embodiments, such plurality may be or comprise multiple copies of one or more particular sequence elements (e.g., as may be from a particular source or otherwise known as a functional or characteristic sequence element). In some embodiments a 5’ UTR comprises multiple different sequence elements. [0609] The term “untranslated region” or “UTR” is commonly used in the art to a region in a DNA molecule which is transcribed but is not translated into an amino acid sequence, or to the corresponding region in an RNA polynucleotide, such as an mRNA molecule. An untranslated region (UTR) can be present 5' (upstream) of an open reading frame (5'-UTR) and/or 3' (downstream) of an open reading frame (3'-UTR). As used herein, the terms “five prime untranslated region” or “5' UTR” refer to a sequence of a polyribonucleotide between the 5' end of the polyribonucleotide (e.g., a transcription start site) and a start codon of a coding region of the polyribonucleotide. In some embodiments, “5' UTR” refers to a sequence of a polyribonucleotide that begins at the 5' end of the polyribonucleotide (e.g., a transcription start site) and ends one nucleotide (nt) before a start codon (usually AUG) of a coding region of the polyribonucleotide, e.g., in its natural context. In some embodiments, a 5' UTR comprises a Kozak sequence. A 5'-UTR is downstream of the 5'-cap (if present), e.g., directly adjacent to the 5'-cap. In some embodiments, a 5’ UTR disclosed herein comprises a cap proximal sequence, e.g., as defined and described herein. In some embodiments, a cap proximal sequence comprises a sequence adjacent to a 5’ cap. [0610] Exemplary 5’ UTRs include a human alpha globin (hAg) 5’UTR or a fragment thereof, a TEV 5’ UTR or a fragment thereof, a HSP705’ UTR or a fragment thereof, or a c-Jun 5’ UTR or a fragment thereof. In some embodiments, an RNA disclosed herein comprises a hAg 5’ UTR or a fragment thereof. [0611] In some embodiments, an RNA disclosed herein comprises a 5’ UTR having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% identity to a 5’ UTR with the sequence AGAAUAAACUAGUAUUCUUCUGGUCCCCACAGACUCAGAGAGAACCCGCCACC (SEQ ID NO: 563). In some embodiments, an RNA disclosed herein comprises a 5’ UTR having the sequence AGAAUAAACUAGUAUUCUUCUGGUCCCCACAGACUCAGAGAGAACCCGCCACC (SEQ ID NO: 563). PolyA Tail [0612] In some embodiments, a polynucleotide (e.g., DNA, RNA) disclosed herein comprises a polyadenylate (polyA) sequence, e.g., as described herein. In some embodiments, a polyA sequence is situated downstream of a 3'- UTR, e.g., adjacent to a 3'-UTR. [0613] As used herein, the term “poly(A) sequence” or “poly-A tail” refers to an uninterrupted or interrupted sequence of adenylate residues which is typically located at the 3'-end of an RNA polynucleotide. Poly(A) sequences are known to those of skill in the art and may follow the 3’-UTR in the RNAs described herein. An uninterrupted poly(A) sequence is characterized by consecutive adenylate residues. In nature, an uninterrupted poly(A) sequence is typical. In some embodiments, polynucleotides disclosed herein comprise an uninterrupted Poly(A) sequence. In some embodiments, polynucleotides disclosed herein comprise interrupted Poly(A) sequence. In some embodiments, RNAs disclosed herein can have a poly(A) sequence attached to the free 3'-end of the RNA by a template- independent RNA polymerase after transcription or a poly(A) sequence encoded by DNA and transcribed by a template-dependent RNA polymerase. [0614] It has been demonstrated that a poly(A) sequence of about 120 A nucleotides has a beneficial influence on the levels of RNA in transfected eukaryotic cells, as well as on the levels of protein that is translated from an open reading frame that is present upstream (5’) of the poly(A) sequence (Holtkamp et al., 2006, Blood, vol. 108, pp. 4009-4017, which is herein incorporated by reference). [0615] In some embodiments, a poly(A) sequence in accordance with the present disclosure is not limited to a particular length; in some embodiments, a poly(A) sequence is any length. In some embodiments, a poly(A) sequence comprises, essentially consists of, or consists of at least 20, at least 30, at least 40, at least 80, or at least 100 and up to 500, up to 400, up to 300, up to 200, or up to 150 A nucleotides, and, in particular, about 120 A nucleotides. In this context, "essentially consists of" means that most nucleotides in the poly(A) sequence, typically at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% by number of nucleotides in the poly(A) sequence are A nucleotides, but permits that remaining nucleotides are nucleotides other than A nucleotides, such as U nucleotides (uridylate), G nucleotides (guanylate), or C nucleotides (cytidylate). In this context, "consists of" means that all nucleotides in the poly(A) sequence, i.e., 100% by number of nucleotides in the poly(A) sequence, are A nucleotides. The term “A nucleotide” or “A” refers to adenylate. [0616] In some embodiments, a poly(A) sequence is attached during RNA transcription, e.g., during preparation of in vitro transcribed RNA, based on a DNA template comprising repeated dT nucleotides (deoxythymidylate) in the strand complementary to the coding strand. The DNA sequence encoding a poly(A) sequence (coding strand) is referred to as poly(A) cassette. [0617] In some embodiments, the poly(A) cassette present in the coding strand of DNA essentially consists of dA nucleotides but is interrupted by a random sequence of the four nucleotides (dA, dC, dG, and dT). Such random sequence may be 5 to 50, 10 to 30, or 10 to 20 nucleotides in length. Such a cassette is disclosed in WO 2016/005324 A1, hereby incorporated by reference. Any poly(A) cassette disclosed in WO 2016/005324 A1 may be used in accordance with the present disclosure. A poly(A) cassette that essentially consists of dA nucleotides but is interrupted by a random sequence having an equal distribution of the four nucleotides (dA, dC, dG, dT) and having a length of e.g., 5 to 50 nucleotides shows, on DNA level, constant propagation of plasmid DNA in E. coli and is still associated, on RNA level, with the beneficial properties with respect to supporting RNA stability and translational efficiency is encompassed. In some embodiments, the poly(A) sequence contained in an RNA polynucleotide described herein essentially consists of A nucleotides but is interrupted by a random sequence of the four nucleotides (A, C, G, U). Such random sequence may be 5 to 50, 10 to 30, or 10 to 20 nucleotides in length. [0618] In some embodiments, no nucleotides other than A nucleotides flank a poly(A) sequence at its 3'-end, i.e., the poly(A) sequence is not masked or followed at its 3'-end by a nucleotide other than A. [0619] In some embodiments, the poly(A) sequence may comprise at least 20, at least 30, at least 40, at least 80, or at least 100 and up to 500, up to 400, up to 300, up to 200, or up to 150 nucleotides. In some embodiments, the poly(A) sequence may essentially consist of at least 20, at least 30, at least 40, at least 80, or at least 100 and up to 500, up to 400, up to 300, up to 200, or up to 150 nucleotides. In some embodiments, the poly(A) sequence may consist of at least 20, at least 30, at least 40, at least 80, or at least 100 and up to 500, up to 400, up to 300, up to 200, or up to 150 nucleotides. In some embodiments, the poly(A) sequence comprises at least 100 nucleotides. In some embodiments, the poly(A) sequence comprises about 150 nucleotides. In some embodiments, the poly(A) sequence comprises about 120 nucleotides. [0620] In some embodiments, a polyA tail comprises a specific number of Adenosines, such as about 50 or more, about 60 or more, about 70 or more, about 80 or more, about 90 or more, about 100 or more, about 120, or about 150 or about 200. In some embodiments a polyA tail of a string construct may comprise 200 A residues or less. In some embodiments, a polyA tail of a string construct may comprise about 200 A residues. In some embodiments, a polyA tail of a string construct may comprise 180 A residues or less. In some embodiments, a polyA tail of a string construct may comprise about 180 A residues. In some embodiments, a polyA tail may comprise 150 residues or less. [0621] In some embodiments, RNA comprises a poly(A) sequence comprising the nucleotide sequence of AAAAAAAAAAAAAAAAAAAAAAAA (SEQ ID NO: 569), or a nucleotide sequence having at least 99%, 98%, 97%, 96%, 95%, 90%, 85%, or 80% identity to the nucleotide sequence of AAAAAAAAAAAAAAAAAAAAAAAAAAAAAAGCAUAUGACUAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA AAAAAAAAAAAAAAAAAAAAAAAA (SEQ ID NO: 569). In some embodiments, a poly(A) tail comprises a plurality of A residues interrupted by a linker. In some embodiments, a linker comprises the nucleotide sequence GCAUAUGAC (SEQ ID NO: 414). 3' UTR [0622] In some embodiments, an RNA utilized in accordance with the present disclosure comprises a 3'-UTR. As used herein, the terms “three prime untranslated region,” “3' untranslated region,” or “3' UTR” refer to a sequence of an mRNA molecule that begins following a stop codon of a coding region of an open reading frame sequence. In some embodiments, the 3' UTR begins immediately after a stop codon of a coding region of an open reading frame sequence, e.g., in its natural context. In other embodiments, the 3' UTR does not begin immediately after stop codon of the coding region of an open reading frame sequence, e.g., in its natural context. The term “3'- U ” ' CUGGUACUGCAUGCACGCAAUGCUAGCUGCCCCUUUCCCGUCCUGGGUACCCCGAGUCUCCCCCGACCUCGGGUCCCAGGUA UGCUCCCACCUCCACCUGCCCCACUCACCACCUCUGCUAGUUCCAGACACCUCCCAAGCACGCAGCAAUGCAGCUCAAAACGCU UAGCCUAGCCACACCCCCACGGGAAACAGCAGUGAUUAACCUUUAGCAAUAAACGAAAGUUUAACUAAGCUAUACUAACCCCA GGGUUGGUCAAUUUCGUGCCAGCCACACC (SEQ ID NO: 567). In some embodiments, an RNA disclosed herein comprises a 3’ UTR with the sequence of CUGGUACUGCAUGCACGCAAUGCUAGCUGCCCCUUUCCCGUCCUGGGUACCCCGAGUCUCCCCCGACCUCGGGUCCCAGGUA UGCUCCCACCUCCACCUGCCCCACUCACCACCUCUGCUAGUUCCAGACACCUCCCAAGCACGCAGCAAUGCAGCUCAAAACGCU UAGCCUAGCCACACCCCCACGGGAAACAGCAGUGAUUAACCUUUAGCAAUAAACGAAAGUUUAACUAAGCUAUACUAACCCCA GGGUUGGUCAAUUUCGUGCCAGCCACACC (SEQ ID NO: 567). [0626] In some embodiments, a 3’UTR is an FI element as described in WO2017/060314, which is herein incorporated by reference in its entirety. 2. RNA Formats [0627] At least three distinct formats useful for RNA compositions (e.g., pharmaceutical compositions) have been developed, namely non-modified uridine containing mRNA (uRNA), nucleoside-modified mRNA (modRNA), and self-amplifying mRNA (saRNA). Each of these platforms displays unique features. In general, in all three formats, RNA is capped, contains open reading frames (ORFs) flanked by untranslated regions (UTR), and have a polyA-tail at the 3' end. An ORF of an uRNA and modRNA vectors encode an antibody agent or portion thereof. An saRNA has multiple ORFs. [0628] In some embodiments, the RNA described herein may have modified nucleosides. In some embodiments, the RNA comprises a modified nucleoside in place of at least one (e.g., every) uridine. [0629] The term “uracil,” as used herein, describes one of the nucleobases that can occur in the nucleic acid of RNA. The structure of uracil is: . [0630] The term “uridine,” as used herein, describes one of the nucleosides that can occur in RNA. The structure of uridine is: . [0631] UTP (uridine 5’-triphosphate) has the following structure: . [0632] Pseudo-UTP (pseudouridine 5’-triphosphate) has the following structure: . [0633] “Pseudouridine” is one example of a modified nucleoside that is an isomer of uridine, where the uracil is attached to the pentose ring via a carbon-carbon bond instead of a nitrogen-carbon glycosidic bond. [0634] Another exemplary modified nucleoside is N1-methyl-pseudouridine (m1Ψ), which has the structure: . [0635] N1-methyl-pseudo-UTP has the following structure: . [0636] Another exemplary modified nucleoside is 5-methyl-uridine (m5U), which has the structure: . [0637] In some embodiments, one or more uridine in the RNA described herein is replaced by a modified nucleoside. In some embodiments, the modified nucleoside is a modified uridine. [0638] In some embodiments, RNA comprises a modified nucleoside in place of at least one uridine. In some embodiments, RNA comprises a modified nucleoside in place of each uridine. [0639] In some embodiments, the modified nucleoside is independently selected from pseudouridine (ψ), N1- methyl-pseudouridine (m1ψ), and 5-methyl-uridine (m5U). In some embodiments, the modified nucleoside comprises pseudouridine (ψ). In some embodiments, the modified nucleoside comprises N1-methyl-pseudouridine (m1ψ). In some embodiments, the modified nucleoside comprises 5-methyl-uridine (m5U). In some embodiments, RNA may comprise more than one type of modified nucleoside, and the modified nucleosides are independently selected from pseudouridine (ψ), N1-methyl-pseudouridine (m1ψ), and 5-methyl-uridine (m5U). In some embodiments, the modified nucleosides comprise pseudouridine (ψ) and N1-methyl-pseudouridine (m1ψ). In some embodiments, the modified nucleosides comprise pseudouridine (ψ) and 5-methyl-uridine (m5U). In some embodiments, the modified nucleosides comprise N1-methyl-pseudouridine (m1ψ) and 5-methyl-uridine (m5U). In some embodiments, the modified nucleosides comprise pseudouridine (ψ), N1-methyl-pseudouridine (m1ψ), and 5-methyl-uridine (m5U). [0640] In some embodiments, the modified nucleoside replacing one or more, e.g., all, uridine in the RNA may be any one or more of 3-methyl-uridine (m3U), 5-methoxy-uridine (mo5U), 5-aza-uridine, 6-aza-uridine, 2-thio-5- aza-uridine, 2-thio-uridine (s2U), 4-thio-uridine (s4U), 4-thio-pseudouridine, 2-thio-pseudouridine, 5-hydroxy-uridine (ho5U), 5-aminoallyl-uridine, 5-halo-uridine (e.g., 5-iodo-uridine or 5-bromo-uridine), uridine 5-oxyacetic acid (cmo5U), uridine 5-oxyacetic acid methyl ester (mcmo5U), 5-carboxymethyl-uridine (cm5U), 1-carboxymethyl- pseudouridine, 5-carboxyhydroxymethyl-uridine (chm5U), 5-carboxyhydroxymethyl-uridine methyl ester (mchm5U), 5-methoxycarbonylmethyl-uridine (mcm5U), 5-methoxycarbonylmethyl-2-thio-uridine (mcm5s2U), 5-aminomethyl-2- thio-uridine (nm5s2U), 5-methylaminomethyl-uridine (mnm5U), 1-ethyl-pseudouridine, 5-methylaminomethyl-2-thio- uridine (mnm5s2U), 5-methylaminomethyl-2-seleno-uridine (mnm5se2U), 5-carbamoylmethyl-uridine (ncm5U), 5- carboxymethylaminomethyl-uridine (cmnm5U), 5-carboxymethylaminomethyl-2-thio-uridine (cmnm5s2U), 5- propynyl-uridine, 1-propynyl-pseudouridine, 5-taurinomethyl-uridine (τm5U), 1-taurinomethyl-pseudouridine, 5- taurinomethyl-2-thio-uridine(τm5s2U), 1-taurinomethyl-4-thio-pseudouridine), 5-methyl-2-thio-uridine (m5s2U), 1- methyl-4-thio-pseudouridine (m1s4ψ), 4-thio-1-methyl-pseudouridine, 3-methyl-pseudouridine (m3ψ), 2-thio-1- methyl-pseudouridine, 1-methyl-1-deaza-pseudouridine, 2-thio-1-methyl-1-deaza-pseudouridine, dihydrouridine (D), dihydropseudouridine, 5,6-dihydrouridine, 5-methyl-dihydrouridine (m5D), 2-thio-dihydrouridine, 2-thio- dihydropseudouridine, 2-methoxy-uridine, 2-methoxy-4-thio-uridine, 4-methoxy-pseudouridine, 4-methoxy-2-thio- pseudouridine, N1-methyl-pseudouridine, 3-(3-amino-3-carboxypropyl)uridine (acp3U), 1-methyl-3-(3-amino-3- carboxypropyl)pseudouridine (acp3 ψ), 5-(isopentenylaminomethyl)uridine (inm5U), 5-(isopentenylaminomethyl)-2- thio-uridine (inm5s2U), α-thio-uridine, 2′-O-methyl-uridine (Um), 5,2′-O-dimethyl-uridine (m5Um), 2′-O-methyl- pseudouridine (ψm), 2-thio-2′-O-methyl-uridine (s2Um), 5-methoxycarbonylmethyl-2′-O-methyl-uridine (mcm5Um), 5-carbamoylmethyl-2′-O-methyl-uridine (ncm5Um), 5-carboxymethylaminomethyl-2′-O-methyl-uridine (cmnm5Um), 3,2′-O-dimethyl-uridine (m3Um), 5-(isopentenylaminomethyl)-2′-O-methyl-uridine (inm5Um), 1-thio-uridine, deoxythymidine, 2′-F-ara-uridine, 2′-F-uridine, 2′-OH-ara-uridine, 5-(2-carbomethoxyvinyl) uridine, 5-[3-(1-E- propenylamino)uridine, or any other modified uridine known in the art. [0641] In some embodiments, the RNA comprises other modified nucleosides or comprises further modified nucleosides, e.g., modified cytidine. For example, in some embodiments, in the RNA 5-methylcytidine is substituted partially or completely, preferably completely, for cytidine. In some embodiments, the RNA comprises 5- methylcytidine and one or more selected from pseudouridine (ψ), N1-methyl-pseudouridine (m1ψ), and 5-methyl- uridine (m5U). In some embodiments, the RNA comprises 5-methylcytidine and N1-methyl-pseudouridine (m1ψ). In some embodiments, the RNA comprises 5-methylcytidine in place of each cytidine and N1-methyl-pseudouridine (m1ψ) in place of each uridine. [0642] In some embodiments of the present disclosure, the RNA is “replicon RNA” or simply a “replicon,” in particular “self-replicating RNA” or “self-amplifying RNA.” In one particularly preferred embodiment, the replicon or self-replicating RNA is derived from or comprises elements derived from a single-stranded (ss) RNA virus, in particular a positive-stranded ssRNA virus, such as an alphavirus. Alphaviruses are typical representatives of positive- stranded RNA viruses. Alphaviruses replicate in the cytoplasm of infected cells (for review of the alphaviral life cycle see José et al., Future Microbiol., 2009, vol. 4, pp. 837–856, which is incorporated herein by reference in its entirety). The total genome length of many alphaviruses typically ranges between 11,000 and 12,000 nucleotides, and the genomic RNA typically has a 5’-cap, and a 3’ poly(A) tail. The genome of alphaviruses encodes non-structural proteins (involved in transcription, modification and replication of viral RNA and in protein modification) and structural proteins (forming the virus particle). There are typically two open reading frames (ORFs) in the genome. The four non-structural proteins (nsP1–nsP4) are typically encoded together by a first ORF beginning near the 5′ terminus of the genome, while alphavirus structural proteins are encoded together by a second ORF which is found downstream of the first ORF and extends near the 3’ terminus of the genome. Typically, the first ORF is larger than the second ORF, the ratio being roughly 2:1. In cells infected by an alphavirus, only the nucleic acid sequence encoding non-structural proteins is translated from the genomic RNA, while the genetic information encoding structural proteins is translatable from a subgenomic transcript, which is an RNA molecule that resembles eukaryotic messenger RNA (mRNA; Gould et al., 2010, Antiviral Res., vol.87 pp. 111–124, which is herein incorporated by reference in its entirety). Following infection, i.e., at early stages of the viral life cycle, the (+) stranded genomic RNA directly acts like a messenger RNA for the translation of the open reading frame encoding the non-structural poly- protein (nsP1234). [0643] Alphavirus-derived vectors have been proposed for delivery of foreign genetic information into target cells or target organisms. In simple approaches, a first ORF encodes an alphavirus-derived RNA-dependent RNA polymerase (replicase), which upon translation mediates self-amplification of the RNA. A second ORF encoding alphaviral structural proteins is replaced by an open reading frame encoding a malarial T cell peptide string construct described herein. Alphavirus-based trans-replication systems rely on alphavirus nucleotide sequence elements on two separate nucleic acid molecules: one nucleic acid molecule encodes a viral replicase, and the other nucleic acid molecule is capable of being replicated by said replicase in trans (hence the designation trans-replication system). Trans-replication requires the presence of both these nucleic acid molecules in a given host cell. The nucleic acid molecule capable of being replicated by the replicase in trans must comprise certain alphaviral sequence elements to allow recognition and RNA synthesis by the alphaviral replicase. [0644] Features of a non-modified uridine platform may include, for example, one or more of intrinsic adjuvant effect, as well as good tolerability and safety. Features of modified uridine (e.g., pseudouridine) platform may include reduced adjuvant effect, blunted immune innate immune sensor activating capacity and thus good tolerability and safety. Features of self-amplifying platform may include, for example, long duration of protein expression, good tolerability and safety, higher likelihood for efficacy with very low vaccine dose. [0645] The present disclosure provides particular RNA constructs optimized, for example, for improved manufacturability, encapsulation, expression level (and/or timing), etc. Certain components are discussed below, and certain preferred embodiments are exemplified herein. [0646] As used herein, an “ERMA” construct is an “RNA construct,” and, for example, “ERMA 1” corresponds to “RNA Construct 1”, “ERMA 2” corresponds to “RNA construct 2,” etc. 3. Codon Optimization and GC Enrichment [0647] As used herein, the term “codon-optimized” refers to alteration of codons in a coding region of a nucleic acid molecule (e.g., a polyribonucleotide) to reflect the typical codon usage of a host organism (e.g., a subject receiving a nucleic acid molecule (e.g., a polyribonucleotide)) without preferably altering the amino acid sequence encoded by the nucleic acid molecule. Within the context of the present disclosure, in some embodiments, coding regions are codon-optimized for optimal expression in a subject to be treated using the RNA molecules described herein. In some embodiments, codon-optimization may be performed such that codons for which frequently occurring tRNAs are available are inserted in place of “rare codons.” In some embodiments, codon-optimization may include increasing guanosine/cytosine (G/C) content of a coding region of RNA described herein as compared to the G/C content of the corresponding coding sequence of a wild-type RNA, wherein the amino acid sequence encoded by the RNA is preferably not modified compared to the amino acid sequence. [0648] In some embodiments, a coding sequence (also referred to as a “coding region”) is codon optimized for expression in the subject to whom a composition (e.g., a pharmaceutical composition) is to be administered (e.g., a human). Thus, in some embodiments, sequences in such a polynucleotide (e.g., a polyribonucleotide) may differ from wild type sequences encoding the relevant antigen or fragment or epitope thereof, even when the amino acid sequence of the antigen or fragment or epitope thereof is wild type. [0649] In some embodiments, strategies for codon optimization for expression in a relevant subject (e.g., a human), and even, in some cases, for expression in a particular cell or tissue. [0650] Various species exhibit particular bias for certain codons of a particular amino acid. Without wishing to be bound by any one theory, codon bias (differences in codon usage between organisms) often correlates with the efficiency of translation of messenger RNA (mRNA), which is in turn believed to be dependent on, among other things, the properties of the codons being translated and the availability of particular transfer RNA (tRNA) molecules. The predominance of selected tRNAs in a cell may generally be a reflection of the codons used most frequently in peptide synthesis. Accordingly, genes may be tailored for optimal gene expression in a given organism based on codon optimization. Codon usage tables are available, for example, at the "Codon Usage Database" available at www.kazusa.orjp/codon/ and these tables may be adapted in a number of ways. Computer algorithms for codon optimizing a particular sequence for expression in a particular subject or its cells are also available, such as Gene Forge (Aptagen; Jacobus, PA), are also available. [0651] In some embodiments, a polynucleotide (e.g., a polyribonucleotide) of the present disclosure is codon optimized, wherein the codons in the polynucleotide (e.g., the polyribonucleotide) are adapted to human codon usage (herein referred to as “human codon optimized polynucleotide”). Codons encoding the same amino acid occur at different frequencies in a subject, e.g., a human. Accordingly, in some embodiments, the coding sequence of a polynucleotide of the present disclosure is modified such that the frequency of the codons encoding the same amino acid corresponds to the naturally occurring frequency of that codon according to the human codon usage, e.g., as shown in Table 8. For example, in the case of the amino acid Ala, the wild type coding sequence is preferably adapted in a way that the codon “GCC” is used with a frequency of 0.40, the codon “GCT” is used with a frequency of 0.28, the codon “GCA” is used with a frequency of 0.22 and the codon “GCG” is used with 30 a frequency of 0.10 etc. (see Table 8). Accordingly, in some embodiments, such a procedure (as exemplified for Ala) is applied for each amino acid encoded by the coding sequence of a polynucleotide to obtain sequences adapted to human codon usage. Table 8: Human codon usage table with frequencies indicated for each amino acid

[0652] Certain strategies for codon optimization and/or G/C enrichment for human expression are described in WO2002/098443, which is incorporated by reference herein in its entirety. In some embodiments, a coding sequence may be optimized using a multiparametric optimization strategy. In some embodiments, optimization parameters may include parameters that influence protein expression, which can be, for example, impacted on a transcription level, an mRNA level, and/or a translational level. In some embodiments, exemplary optimization parameters include, but are not limited to transcription-level parameters (including, e.g., GC content, consensus splice sites, cryptic splice sites, SD sequences, TATA boxes, termination signals, artificial recombination sites, and combinations thereof); mRNA-level parameters (including, e.g., RNA instability motifs, ribosomal entry sites, repetitive sequences, and combinations thereof); translation-level parameters (including, e.g., codon usage, premature poly(A) sites, ribosomal entry sites, secondary structures, and combinations thereof); or combinations thereof. In some embodiments, a coding sequence may be optimized by a GeneOptimizer algorithm as described in Fath et al. “Multiparameter RNA and Codon Optimization: A Standardized Tool to Assess and Enhance Autologous Mammalian Gene Expression” PLoS ONE 6(3): e17596; Rabb et al., “The GeneOptimizer Algorithm: using a sliding window approach to cope with the vast sequence space in multiparameter DNA sequence optimization” Systems and Synthetic Biology (2010) 4:215- 225; and Graft et al. “Codon-optimized genes that enable increased heterologous expression in mammalian cells and elicit efficient immune responses in mice after vaccination of naked DNA” Methods Mol Med (2004) 94:197-210, the entire content of each of which is incorporated herein for the purposes described herein. In some embodiments, a coding sequence may be optimized by Eurofins’ adaption and optimization algorithm “GENEius” as described in Eurofins’ Application Notes: Eurofins’ adaption and optimization software “GENEius” in comparison to other optimization algorithms, the entire content of which is incorporated by reference for the purposes described herein. [0653] In some embodiments, a coding sequence utilized in accordance with the present disclosure has G/C content that is increased compared to a wild type coding sequence for a malarial construct described herein, or a portion thereof. In some embodiments, guanosine/cytidine (G/C) content of a coding region is modified relative to a wild type coding sequence for a malarial construct described herein, but the amino acid sequence encoded by the polyribonucleotide not modified. [0654] Without wishing to be bound by any particular theory, it is proposed that GC enrichment may improve translation of a payload sequence. Typically, sequences having an increased G (guanosine)/C (cytidine) content are more stable than sequences having an increased A (adenosine)/U (uridine) content. In respect to the fact that several codons code for one and the same amino acid (so-called degeneration of the genetic code), the most favorable codons for the stability can be determined (so-called alternative codon usage). Depending on the amino acid to be encoded by a polyribonucleotide, there are various possibilities for modification of the ribonucleic acid sequence, compared to its wild-type sequence. In particular, codons which contain A and/or U nucleosides can be modified by substituting these codons by other codons, which code for the same amino acids but contain no A and/or U or contain a lower content of A and/or U nucleosides. [0655] In some embodiments, G/C content of a coding region of a polyribonucleotide described herein is increased by at least 1%, at least 2%, at least 3%, at least 4%, at least 5%, at least 6%, or even more compared to the G/C content of the coding region prior to codon optimization, e.g., of the wild type RNA. In some embodiments, G/C content of a coding region of a polyribonucleotide described herein is decreased by at least 1%, at least 2%, at least 3%, at least 4%, at least 5%, at least 6%, or even more compared to the G/C content of the coding region prior to codon optimization, e.g., of the wild type RNA. [0656] In some embodiments, stability and translation efficiency of a polyribonucleotide may incorporate one or more elements established to contribute to stability and/or translation efficiency of the polyribonucleotide; exemplary such elements are described, for example, in PCT/EP2006/009448 incorporated herein by reference. In some embodiments, to increase expression of a polyribonucleotide used according to the present disclosure, a polyribonucleotide may be modified within the coding region, i.e., the sequence encoding the expressed peptide or protein, without altering the sequence of the expressed peptide or protein, for example so as to increase the GC- content to increase mRNA stability and/or to perform a codon optimization and, thus, enhance translation in cells. E. Certain Exemplary Polyribonucleotides Encoding Plasmodium T-Cell String Polypeptide Constructs [0657] In some embodiments, a polyribonucleotide encoding a Plasmodium T-cell string polypeptide construct as described herein has a nucleotide sequence provided in Table 9 or 10. Exemplary Plasmodium T-cell string polypeptide constructs are also shown schematically in FIG.3. Table 9: Exemplary DNA Sequences Encoding a Plasmodium T-cell String Polypeptide Construct 57 57/ Table 10: Exemplary RNA Sequences Encoding a Plasmodium T-cell string Polypeptide Construct

[ : t [0664] Linker: Sequences coding for peptide linkers as described in Section IIC(iii) above. In some embodiments, the linker is selected from an amino acid sequence as defined in Table 7. In some embodiments, a linker has the amino acid sequence GGSGGGGSGG (SEQ ID NO: 404). In some embodiments, a linker has the amino acid sequence GGGS (SEQ ID NO: 411). In some embodiments, a linker has the amino acid sequence GGGGSGGGGSGGGGS (SEQ ID NO: 408). In some embodiments, a linker has the amino acid sequence AGNRVRRSVG (SEQ ID NO: 412). [0665] FI element: The 3'-UTR sequence as described in Section IID(i) above. In some embodiments, FI comprises the nucleotide sequence of SEQ ID NO: 567. [0666] A30L70: A poly(A)-tail as described in Section IID(i) above. In some embodiments, A30L70 comprises the nucleotide sequence of SEQ ID NO: 569. [0667] In some embodiments, a polyribonucleotide encoding a malarial T cell peptide string construct described herein has one of the following structures: cap-hAg-Kozak-Antigen-Linker-Antigen-Linker-Antigen-Linker-Antigen-FI-A30L70; cap-hAg-Kozak-Antigen-Linker-Antigen-Linker-Antigen-Linker-Antigen-Linker-Antigen-FI-A30L70; cap-hAg-Kozak-Antigen-Linker-Antigen-Linker-Antigen-Linker-Antigen-Linker-Antigen-Linker-Antigen-FI- A30L70; cap-hAg-Kozak-Antigen-Linker-Antigen-Linker-Antigen-Linker-Antigen-Linker-Antigen-Linker-Antigen- Linker-Antigen-FI-A30L70; cap-hAg-Kozak-Antigen-Linker-Antigen-Linker-Antigen-Linker-Antigen-Linker-Antigen-Linker-Antigen- Linker-Antigen-Linker-Antigen-FI-A30L70; cap-hAg-Kozak-Antigen-Linker-Antigen-Linker-Antigen-Linker-Antigen-Linker-Antigen-Linker-Antigen- Linker-Antigen-Linker-Antigen-Linker-Antigen-FI-A30L70; cap-hAg-Kozak-Antigen-Linker-Antigen-Linker-Antigen-Linker-Antigen-Linker-Antigen-Linker-Antigen- Linker-Antigen-Linker-Antigen-Linker-Antigen-Linker-Antigen-FI-A30L70; cap-hAg- Kozak-sec-Antigen-Linker-Antigen-Linker-Antigen-Linker-Antigen-FI-A30L70; cap-hAg- Kozak-sec-Antigen-Linker-Antigen-Linker-Antigen-Linker-Antigen-Linker-Antigen-FI-A30L70; cap-hAg- Kozak-sec-Antigen-Linker-Antigen-Linker-Antigen-Linker-Antigen-Linker-Antigen-Linker- Antigen-FI-A30L70; cap-hAg- Kozak-sec-Antigen-Linker-Antigen-Linker-Antigen-Linker-Antigen-Linker-Antigen-Linker- Antigen-Linker-Antigen-FI-A30L70; cap-hAg- Kozak-sec-Antigen-Linker-Antigen-Linker-Antigen-Linker-Antigen-Linker-Antigen-Linker- Antigen-Linker-Antigen-Linker-Antigen-FI-A30L70; cap-hAg- Kozak-sec-Antigen-Linker-Antigen-Linker-Antigen-Linker-Antigen-Linker-Antigen-Linker- Antigen-Linker-Antigen-Linker-Antigen-Linker-Antigen-FI-A30L70; cap-hAg- Kozak-sec-Antigen-Linker-Antigen-Linker-Antigen-Linker-Antigen-Linker-Antigen-Linker- Antigen-Linker-Antigen-Linker-Antigen-Linker-Antigen-Linker-Antigen-FI-A30L70; cap-hAg-Kozak-Antigen-Linker-Antigen-Linker-Antigen-Linker-Antigen-MITD-FI-A30L70; cap-hAg-Kozak-Antigen-Linker-Antigen-Linker-Antigen-Linker-Antigen-Linker-Antigen- MITD -FI-A30L70; cap-hAg-Kozak-Antigen-Linker-Antigen-Linker-Antigen-Linker-Antigen-Linker-Antigen-Linker-Antigen- MITD -FI-A30L70; cap-hAg-Kozak-Antigen-Linker-Antigen-Linker-Antigen-Linker-Antigen-Linker-Antigen-Linker-Antigen- Linker-Antigen- MITD -FI-A30L70; cap-hAg-Kozak-Antigen-Linker-Antigen-Linker-Antigen-Linker-Antigen-Linker-Antigen-Linker-Antigen- Linker-Antigen-Linker-Antigen- MITD -FI-A30L70; cap-hAg-Kozak-Antigen-Linker-Antigen-Linker-Antigen-Linker-Antigen-Linker-Antigen-Linker-Antigen- Linker-Antigen-Linker-Antigen-Linker-Antigen- MITD -FI-A30L70; cap-hAg-Kozak-Antigen-Linker-Antigen-Linker-Antigen-Linker-Antigen-Linker-Antigen-Linker-Antigen- Linker-Antigen-Linker-Antigen-Linker-Antigen-Linker-Antigen- MITD -FI-A30L70; cap-hAg- Kozak-sec-Antigen-Linker-Antigen-Linker-Antigen-Linker-Antigen- MITD -FI-A30L70; cap-hAg- Kozak-sec-Antigen-Linker-Antigen-Linker-Antigen-Linker-Antigen-Linker-Antigen- MITD -FI- A30L70; cap-hAg- Kozak-sec-Antigen-Linker-Antigen-Linker-Antigen-Linker-Antigen-Linker-Antigen-Linker- Antigen- MITD -FI-A30L70; cap-hAg- Kozak-sec-Antigen-Linker-Antigen-Linker-Antigen-Linker-Antigen-Linker-Antigen-Linker- Antigen-Linker-Antigen- MITD -FI-A30L70; cap-hAg- Kozak-sec-Antigen-Linker-Antigen-Linker-Antigen-Linker-Antigen-Linker-Antigen-Linker- Antigen-Linker-Antigen-Linker-Antigen- MITD -FI-A30L70; cap-hAg- Kozak-sec-Antigen-Linker-Antigen-Linker-Antigen-Linker-Antigen-Linker-Antigen-Linker- Antigen-Linker-Antigen-Linker-Antigen-Linker-Antigen- MITD -FI-A30L70; or cap-hAg- Kozak-sec-Antigen-Linker-Antigen-Linker-Antigen-Linker-Antigen-Linker-Antigen-Linker- Antigen-Linker-Antigen-Linker-Antigen-Linker-Antigen-Linker-Antigen- MITD -FI-A30L70. [0668] In some embodiments, the sequence encoding a malarial T cell peptide string construct described herein comprises a modified nucleoside replacing (partially or completely, preferably completely) uridine, wherein the modified nucleoside is selected from the group consisting of pseudouridine (ψ), N1-methyl-pseudouridine (m1ψ), and 5-methyl-uridine. [0669] In some embodiments, the sequence encoding a malarial T cell peptide string construct described herein is codon-optimized. [0670] In some embodiments, the G/C content of the sequence encoding a malarial T cell peptide string construct described herein is increased compared to the wild type coding sequence. [0671] In some embodiments, the RNA (in particular, mRNA) described herein comprises: a 5’ UTR comprising the nucleotide sequence of SEQ ID NO: 563, or a nucleotide sequence having at least 99%, 98%, 97%, 96%, 95%, 90%, 85%, or 80% identity to the nucleotide sequence of SEQ ID NO: 562; a 3’ UTR comprising the nucleotide sequence of SEQ ID NO: 567, or a nucleotide sequence having at least 99%, 98%, 97%, 96%, 95%, 90%, 85%, or 80% identity to the nucleotide sequence of SEQ ID NO: 566; and a poly-A sequence comprising the nucleotide sequence of SEQ ID NO: 569. [0672] In some embodiments, the RNA (in particular, mRNA) described herein comprises: m27,3’-OGppp(m12’-O) ApG as capping structure at the 5'-end of the mRNA; a 5’ UTR comprising the nucleotide sequence of SEQ ID NO: 563, or a nucleotide sequence having at least 99%, 98%, 97%, 96%, 95%, 90%, 85%, or 80% identity to the nucleotide sequence of SEQ ID NO: 563; a 3’ UTR comprising the nucleotide sequence of SEQ ID NO: 567, or a nucleotide sequence having at least 99%, 98%, 97%, 96%, 95%, 90%, 85%, or 80% identity to the nucleotide sequence of SEQ ID NO: 567; and a poly-A sequence comprising the nucleotide sequence of SEQ ID NO: 569. [0673] In some embodiments, the RNA is unmodified. In some embodiments, the RNA is modified. In some embodiments, the RNA comprises N1-methyl-pseudouridine (m1ψ) in place of at least one uridine (e.g., in place of each uridine). [0674] In some embodiments, the RNA (in particular, mRNA) described herein comprises: m27,3’-OGppp(m12’-O) ApG as capping structure at the 5'-end of the mRNA; a 5’ UTR comprising the nucleotide sequence of SEQ ID NO: 563, or a nucleotide sequence having at least 99%, 98%, 97%, 96%, 95%, 90%, 85%, or 80% identity to the nucleotide sequence of SEQ ID NO: 563; a 3’ UTR comprising the nucleotide sequence of SEQ ID NO: 567, or a nucleotide sequence having at least 99%, 98%, 97%, 96%, 95%, 90%, 85%, or 80% identity to the nucleotide sequence of SEQ ID NO: 567; a poly-A sequence comprising the nucleotide sequence of SEQ ID NO: 569; and N1-methyl-pseudouridine (m1ψ) in place of at least one uridine (e.g., in place of each uridine). [0675] In some embodiments, a malarial T cell peptide string construct described herein includes one or more T-cell antigens from proteins of Plasmodium falciparum. F. Certain Exemplary Polyribonucleotides Encoding Plasmodium CSP Polypeptide Constructs [0676] In some embodiments, a polyribonucleotide encoding a Plasmodium CSP polypeptide construct as described herein has a nucleotide sequence provided in Table 11. Table 11: Exemplary RNA Sequences Encoding a Plasmodium CSP Polypeptide Construct

[0677] In the following, exemplary embodiments of polyribonucleotides encoding Plasmodium CSP polypeptide constructs are described, wherein certain terms used when describing elements thereof have the following meanings: [0678] cap: 5'-cap structure as described in Section IID(i) above, e.g.,(m₂ ^7,3’-O)Gppp(m^2’-O)ApG. [0679] hAg-Kozak: 5'-UTR sequence as described in Section IID(i) above. In some embodiments, hAg- Kozak/5’UTR comprises the nucleotide sequence of SEQ ID NO: 565. In some embodiments, hAg-Kozak comprises the nucleotide sequence of SEQ ID NO: 565. [0680] sec: Sequences encoding a secretory signal as described in Section IIC(i) above. In some embodiments, the secretory signal is from Plasmodium falciparum, preferably Plasmodium falciparum isolate 3D7, and referred to herein as Pfsec and has the sequence as defined in Table 5 (SEQ ID NO: 332). In some embodiments, the secretory signal is heterologous and selected from the amino acid sequences as defined in Table 5. In some embodiments, the secretory signal is HSV1-gD and referred to herein as HSV-1gDsec and has the sequence as defined in Table 5 (SEQ ID NO: 314, SEQ ID NO: 317, SEQ ID NO: 320). [0681] Antigen: Sequences encoding a Plasmodium CSP polypeptide construct, including regions from Plasmodium falciparum, preferably Plasmodium falciparum isolate 3D7, as described herein. [0682] TMD: Sequences encoding a transmembrane region as described in Section IIC(ii) above. In some embodiments, the TMD is a glycosylphosphatidylinositol (GPI) anchor region from Plasmodium CSP, preferably from Plasmodium falciparum isolate 3D7, and referred to herein as PfTMD and has the amino acid sequence of SEQ ID NO: 385. In some embodiments, the TMD is heterologous. In some embodiments, the TMD is from HSV1-gD and referred to herein as HSV-1TMD and has the amino acid sequence of SEQ ID NO: 379. [0683] Linker: Sequences coding for peptide linkers as described in Section IIC(iii) above. [0684] FI element: The 3'-UTR sequence as described in Section IID(i) above. In some embodiments, FI comprises the nucleotide sequence of SEQ ID NO: 567. [0685] A30L70: A poly(A)-tail sequence as described in Section IID(i) above. In some embodiments, A30L70 comprises the nucleotide sequence of SEQ ID NO: 569. [0686] In some embodiments, a polyribonucleotide encoding a Plasmodium CSP polypeptide construct described herein has one of the following structures: cap-hAg-Kozak-Antigen-FI-A30L70; cap-hAg-Kozak-sec-Antigen-FI-A30L70; cap-hAg-Kozak-Antigen-TMD-FI-A30L70; or cap-hAg-Kozak-sec-Antigen-TMD-FI-A30L70. [0687] In some embodiments, the Antigen comprises a full-length CSP construct as defined above, a CSP construct with noncontiguous minor repeat regions as defined above, a N-terminal region deletion CSP construct as defined above, a N-terminal region and major region deleted CSP construct as defined above, a N-terminal domain deleted CSP construct as defined above, a N-terminal domain and major repeat region deleted CSP construct as defined above, a N-terminal domain and major repeat region deleted CSP construct with modified junction region variants or portions as defined above, a major repeat region portion and C-terminal region containing CSP constructs as defined above, an N-terminal and C-terminal deleted CSP construct with noncontiguous minor repeat regions as defined above, a 6NANP CSP construct as defined above, an 18 NANP CSP construct as defined above, a T-Cell C- term CSP construct as defined above, or a CSP construct set out in the Additional Select Exemplary CSP construct list. In some embodiments, a polyribonucleotide described herein has one of the following structures: cap-hAg-Kozak-Antigen-FI-A30L70; cap-hAg-Kozak-sec-Antigen-FI-A30L70; cap-hAg-Kozak-Antigen-TMD-FI-A30L70; cap-hAg-Kozak-sec-Antigen-TMD-FI-A30L70; cap-hAg-Kozak-Pfsec-Antigen-FI-A30L70; cap-hAg-Kozak-Antigen-PfTMD-FI-A30L70; cap-hAg-Kozak-Pfsec-Antigen-PfTMD-FI-A30L70; cap-hAg-Kozak-HSV-1gDsec-Antigen-FI-A30L70; cap-hAg-Kozak-Antigen-HSV-1TMD-FI-A30L70; cap-hAg-Kozak-HSV-1gDsec-Antigen-HSV-1TMD-FI-A30L70; cap-hAg-Kozak-Pfsec-Antigen-HSV-1TMD-FI-A30L70; cap-hAg-Kozak-HSV-1gDsec-Antigen-PfTMD-FI-A30L70; cap-hAg-Kozak-heterologoussec- Antigen -FI-A30L70; cap-hAg-Kozak-Antigen-heterologousTMD-FI-A30L70; or cap-hAg-Kozak-heterologoussec-Antigen-heterologousTMD-FI-A30L70. [0688] In some embodiments, the different elements (sec, Antigen, TMD) may be linked by one or more linkers, e.g., a linker selected from an amino acid sequence as defined in Table 7. In some embodiments, a linker has the amino acid sequence GGSGGGGSGG (SEQ ID NO: 404). In some embodiments, a linker has the amino acid sequence GGGS. In some embodiments, a linker has the amino acid sequence GGGGSGGGGSGGGGS (SEQ ID NO: 408). In some embodiments, a linker has the amino acid sequence AGNRVRRSVG (SEQ ID NO: 412). [0689] In some embodiments, the sequence encoding a Plasmodium CSP polypeptide construct described herein comprises a modified nucleoside replacing (partially or completely, preferably completely) uridine, wherein the modified nucleoside is selected from the group consisting of pseudouridine (ψ), N1-methyl-pseudouridine (m1ψ), and 5-methyl-uridine. [0690] In some embodiments, the sequence encoding a Plasmodium CSP polypeptide construct described herein is codon-optimized. [0691] In some embodiments, the G/C content of the sequence encoding a Plasmodium CSP polypeptide construct described herein is increased compared to the wild type coding sequence. [0692] In some embodiments, the RNA (in particular, mRNA) described herein comprises: a 5’ UTR comprising the nucleotide sequence of SEQ ID NO: 565, or a nucleotide sequence having at least 99%, 98%, 97%, 96%, 95%, 90%, 85%, or 80% identity to the nucleotide sequence of SEQ ID NO: 565; a 3’ UTR comprising the nucleotide sequence of SEQ ID NO: 567, or a nucleotide sequence having at least 99%, 98%, 97%, 96%, 95%, 90%, 85%, or 80% identity to the nucleotide sequence of SEQ ID NO: 567; and a poly-A sequence comprising the nucleotide sequence of SEQ ID NO: 569. [0693] In some embodiments, the RNA (in particular, mRNA) described herein comprises: m27,3’-OGppp(m12’-O) ApG as capping structure at the 5'-end of the mRNA; a 5’ UTR comprising the nucleotide sequence of SEQ ID NO: 565, or a nucleotide sequence having at least 99%, 98%, 97%, 96%, 95%, 90%, 85%, or 80% identity to the nucleotide sequence of SEQ ID NO: 565; a 3’ UTR comprising the nucleotide sequence of SEQ ID NO: 567, or a nucleotide sequence having at least 99%, 98%, 97%, 96%, 95%, 90%, 85%, or 80% identity to the nucleotide sequence of SEQ ID NO: 567; and a poly-A sequence comprising the nucleotide sequence of SEQ ID NO: 569. [0694] In some embodiments, the RNA is unmodified. In some embodiments, the RNA is modified. In some embodiments, the RNA comprises N1-methyl-pseudouridine (m1ψ) in place of at least one uridine (e.g., in place of each uridine). [0695] In some embodiments, the RNA (in particular, mRNA) described herein comprises: m27,3’-OGppp(m12’-O) ApG as capping structure at the 5'-end of the mRNA; a 5’ UTR comprising the nucleotide sequence of SEQ ID NO: 565, or a nucleotide sequence having at least 99%, 98%, 97%, 96%, 95%, 90%, 85%, or 80% identity to the nucleotide sequence of SEQ ID NO: 565; a 3’ UTR comprising the nucleotide sequence of SEQ ID NO: 567, or a nucleotide sequence having at least 99%, 98%, 97%, 96%, 95%, 90%, 85%, or 80% identity to the nucleotide sequence of SEQ ID NO: 567; and a poly-A sequence comprising the nucleotide sequence of SEQ ID NO: 569; and N1-methyl-pseudouridine (m1ψ) in place of at least one uridine (e.g., in place of each uridine). [0696] In some embodiments, a Plasmodium CSP polypeptide construct described herein includes one or more malarial polypeptides or portions thereof from Plasmodium falciparum. [0697] In some embodiments, a Plasmodium CSP polypeptide construct described herein includes one or more regions or portions thereof derived from a Plasmodium falciparum CSP protein, an immunogenic variant thereof, or an immunogenic fragment of the Plasmodium falciparum CSP protein or the immunogenic variant thereof. Thus, in some embodiments, the RNA, e.g., mRNA, used in the present disclosure encodes an amino acid sequence comprising an Plasmodium falciparum CSP protein, an immunogenic variant thereof, or an immunogenic fragment of the Plasmodium falciparum CSP protein or the immunogenic variant thereof. G. Certain Exemplary Combination of Plasmodium Polypeptide Constructs [0698] The present disclosure provides combinations of polyribonucleotides that can be used to express two or more Plasmodium polypeptide constructs. In some embodiments, a combination as described herein comprises two or more polyribonucleotides that encode one or more Plasmodium T-cell string polypeptide constructs as described herein and one or more polyribonucleotides that encode one or more Plasmodium CSP polypeptide constructs as described herein. In some embodiments, a combination as described herein comprises two or more polyribonucleotides that encode a Plasmodium T-cell string polypeptide construct as described herein and a Plasmodium CSP polypeptide construct as described herein. In a preferred embodiment, a combination as described herein comprises one or two polyribonucleotides that encode a Plasmodium T-cell string polypeptide construct as described herein and one Plasmodium CSP polypeptide construct as described herein. [0699] Certain exemplary combinations of Plasmodium T-cell string polypeptide constructs and Plasmodium CSP polypeptide constructs expressed by the one or more polyribonucleotides are included in Table 12 below. In some embodiments, combinations of polyribonucleotides can be used to express two Plasmodium polypeptide constructs, wherein the two Plasmodium polypeptide constructs expressed from the combination comprise amino acid sequences listed in the third and fourth columns of Table 12 below or amino acid sequences with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% identity with the amino acid sequences listed in the third and fourth columns of Table 12 below. Table 12: Certain Exemplary Combinations [0700] The present disclosure also provides combinations comprising three or more polyribonucleotides that encode a first Plasmodium T-cell string polypeptide construct as described herein, a second Plasmodium T-cell string polypeptide construct as described herein, and a Plasmodium CSP polypeptide construct as described herein. [0701] Certain exemplary combinations of Plasmodium T-cell string polypeptide constructs and Plasmodium CSP polypeptide constructs expressed by a combination of the three or more polyribonucleotides are included in Table 13 below. In some embodiments, combinations of polyribonucleotides can be used to express three Plasmodium polypeptide constructs, wherein the three Plasmodium polypeptide constructs expressed from the combination comprise amino acid sequences listed in the fourth, fifth and sixth columns of Table 13 below or amino acid sequences with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% identity with the amino acid sequences listed in the fourth, fifth and sixth columns of Table 13 below. Table 13: Certain Exemplary Combinations

[0702] In some embodiments, a combination as described herein comprises a first polyribonucleotide encoding a Plasmodium T-cell string polypeptide construct and a second polyribonucleotide encoding a Plasmodium CSP polypeptide construct. In some embodiments, a first polyribonucleotide comprises the antigens included in Mas3a and a second polyribonucleotide comprises Plasmodium full-length CSP polypeptide construct including the Plasmodium CSP secretory signal and the Plasmodium CSP GPI anchor region. In some embodiments, the combination further comprises a third polyribonucleotide encoding a Plasmodium T-cell string polypeptide construct that comprises the antigens included in Mas4f. [0703] In some embodiments, a combination as described herein comprises a first polyribonucleotide encoding a Plasmodium T-cell string polypeptide construct and a second polyribonucleotide encoding a Plasmodium CSP polypeptide construct. In some embodiments, a Plasmodium T-cell string polypeptide construct comprises: (i) an antigenic Plasmodium CSP polypeptide fragment, (ii) an antigenic Plasmodium TRAP polypeptide fragment, (iii) an antigenic Plasmodium UIS3 polypeptide fragment, (iv) an antigenic Plasmodium ETRAMP10.3 polypeptide fragment, and (v) an antigenic Plasmodium LSAP2 polypeptide fragment. In some embodiments, a Plasmodium T-cell string polypeptide construct comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 203. In some embodiments, a Plasmodium CSP polypeptide construct comprises (i) a secretory signal, (ii) a Plasmodium CSP N-terminal region, (iii) a Plasmodium CSP N-terminal end region, (iv) a Plasmodium CSP junction region, (v) three repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223), (vi) a Plasmodium CSP major repeat region, (vii) a Plasmodium CSP C- terminal region, and (viii) a transmembrane region. In some embodiments, a Plasmodium CSP polypeptide construct comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 33. In some embodiments, a Plasmodium CSP polypeptide construct comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 33. In some embodiments, a combination further comprises a third polyribonucleotide that encodes a second Plasmodium T-cell string polypeptide construct. In some embodiments, a second Plasmodium T-cell string polypeptide construct comprises (i) an antigenic Plasmodium LSA-1(a) polypeptide fragment, (ii) an antigenic Plasmodium LSA-1(b) polypeptide fragment, (iii) an antigenic Plasmodium LISP-2 polypeptide fragment, and (iv) an antigenic Plasmodium LISP-1 polypeptide fragment. In some embodiments, a second Plasmodium T-cell string polypeptide construct comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 209. [0704] In some embodiments, a combination as described herein comprises a first polyribonucleotide encoding a Plasmodium T-cell string polypeptide construct and a second polyribonucleotide encoding a Plasmodium CSP polypeptide construct. In some embodiments, a Plasmodium T-cell string polypeptide construct comprises (i) an antigenic Plasmodium CSP polypeptide fragment, (ii) an antigenic Plasmodium TRAP polypeptide fragment, (iii) an antigenic Plasmodium UIS3 polypeptide fragment, (iv) an antigenic Plasmodium ETRAMP10.3 polypeptide fragment, and (v) an antigenic Plasmodium LSAP2 polypeptide fragment. In some embodiments, a Plasmodium T-cell string polypeptide construct comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 203. In some embodiments, a Plasmodium CSP polypeptide construct comprises (i) a secretory signal, (ii) a Plasmodium CSP N-terminal end region, (iii) a Plasmodium CSP junction region, (iv) nine repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223), (v) a Plasmodium CSP C-terminal region, (vi) a serine-valine sequence immediately following the Plasmodium CSP C-terminal region, (vii) a linker, and (viii) a transmembrane region, and wherein the Plasmodium CSP polypeptide construct does not comprise any of (a) a Plasmodium CSP N-terminal region or portion thereof, and (b) an amino acid sequence of NPNA (SEQ ID NO: 228). In some embodiments, a Plasmodium CSP polypeptide construct comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 81. In some embodiments, a combination further comprises a third polyribonucleotide that encodes a second Plasmodium T-cell string polypeptide construct. In some embodiments, a second Plasmodium T-cell string polypeptide construct comprises (i) an antigenic Plasmodium LSA-1(a) polypeptide fragment, (ii) an antigenic Plasmodium LSA-1(b) polypeptide fragment, (iii) an antigenic Plasmodium LISP-2 polypeptide fragment, and (iv) an antigenic Plasmodium LISP-1 polypeptide fragment. In some embodiments, a second Plasmodium T-cell string polypeptide construct comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 209. [0705] In some embodiments, a combination as described herein comprises a first polyribonucleotide encoding a Plasmodium T-cell string polypeptide construct and a second polyribonucleotide encoding a Plasmodium CSP polypeptide construct. In some embodiments, a Plasmodium T-cell string polypeptide construct comprises (i) an antigenic Plasmodium LSA-1(a) polypeptide fragment, (ii) an antigenic Plasmodium LSA-1(b) polypeptide fragment, (iii) an antigenic Plasmodium LISP-2 polypeptide fragment, and (iv) an antigenic Plasmodium LISP-1 polypeptide fragment. In some embodiments, a Plasmodium T-cell string polypeptide construct comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 209. In some embodiments, a Plasmodium CSP polypeptide construct comprises (i) a secretory signal, (ii) a Plasmodium CSP N-terminal region, (iii) a Plasmodium CSP N-terminal end region, (iv) a Plasmodium CSP junction region, (v) three repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223), (vi) a Plasmodium CSP major repeat region, (vii) a Plasmodium CSP C-terminal region, and (viii) a transmembrane region. In some embodiments, a Plasmodium CSP polypeptide construct comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 33. In some embodiments, a Plasmodium CSP polypeptide construct comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 33. [0706] In some embodiments, a combination as described herein comprises a first polyribonucleotide encoding a Plasmodium T-cell string polypeptide construct and a second polyribonucleotide encoding a Plasmodium CSP polypeptide construct. In some embodiments, a Plasmodium T-cell string polypeptide construct comprises (i) an antigenic Plasmodium LSA-1(a) polypeptide fragment, (ii) an antigenic Plasmodium LSA-1(b) polypeptide fragment, (iii) an antigenic Plasmodium LISP-2 polypeptide fragment, and (iv) an antigenic Plasmodium LISP-1 polypeptide fragment. In some embodiments, a Plasmodium T-cell string polypeptide construct comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 209. In some embodiments, a Plasmodium CSP polypeptide construct comprises (i) a secretory signal, (ii) a Plasmodium CSP N-terminal end region, (iii) a Plasmodium CSP junction region, (iv) nine repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223), (v) a Plasmodium CSP C-terminal region, (vi) a serine-valine sequence immediately following the Plasmodium CSP C-terminal region, (vii) a linker, and (viii) a transmembrane region, and wherein the Plasmodium CSP polypeptide construct does not comprise any of (a) a Plasmodium CSP N-terminal region or portion thereof, and (b) an amino acid sequence of NPNA (SEQ ID NO: 228). In some embodiments, a Plasmodium CSP polypeptide construct comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 81. H. Certain Exemplary Combination of Polyribonucleotide Constructs [0707] As discussed throughout, the present disclosure provides combinations of polyribonucleotides that can be used to express one or more Plasmodium polypeptide constructs. In some embodiments, a combination as described herein comprises one or more polyribonucleotides that encode one or more Plasmodium T-cell string polypeptide constructs as described herein and one or more polyribonucleotides that encode one or more Plasmodium CSP polypeptide constructs as described herein. In some embodiments, a combination as described herein comprises a first polyribonucleotide that encodes a Plasmodium T-cell string polypeptide construct as described herein and a second polyribonucleotide that encodes a Plasmodium CSP polypeptide construct as described herein. [0708] Certain exemplary combinations of polyribonucleotides described herein are included in Table 12 above. In some embodiments, two polyribonucleotides in a combination can have a ribonucleic acid sequence as listed in the third and fourth columns of Table 12 above or ribonucleic acid sequences with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% identity with the ribonucleic acid sequences listed in the third and fourth columns of Table 12 above. [0709] The present disclosure also provides combinations a first polyribonucleotide that encodes a first Plasmodium T-cell string polypeptide construct as described herein, a second polyribonucleotide that encodes a second Plasmodium T-cell string polypeptide construct as described herein, and a third polyribonucleotide that encodes a Plasmodium CSP polypeptide construct as described herein. [0710] Certain exemplary combinations of Plasmodium T-cell string polypeptide constructs and Plasmodium CSP polypeptide constructs expressed by a combination of the three or more polyribonucleotides are included in Table 13 above. In some embodiments, three polyribonucleotides in a combination can have a ribonucleic acid sequences as listed in the fourth, fifth, and sixth columns of Table 13 above or ribonucleic acid sequences with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% identity with the ribonucleic acid sequences listed in the fourth, fifth, and sixth columns of Table 13 above. [0711] In some embodiments, a combination as described herein comprises a first polyribonucleotide encoding a Plasmodium T-cell string polypeptide construct and a second polyribonucleotide encoding a Plasmodium CSP polypeptide construct. In some embodiments, a first polyribonucleotide comprises a ribonucleic acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to a ribonucleic acid sequence according to SEQ ID NO: 204. In some embodiments, a first polyribonucleotide comprises a ribonucleic acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to a ribonucleic acid sequence according to SEQ ID NOs: 34, 145, 147, 149, 151, 153, 155, and 157. In some embodiments, a first polyribonucleotide comprises a ribonucleic acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to a ribonucleic acid sequence according to SEQ ID NO: 147. In some embodiments, a combination as described herein further comprises a third polyribonucleotide encoding a second Plasmodium T-cell string polypeptide construct. In some embodiments, a third polyribonucleotide comprises a ribonucleic acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to a ribonucleic acid sequence according to SEQ ID NO: 210. [0712] In some embodiments, a combination as described herein comprises a first polyribonucleotide encoding a Plasmodium T-cell string polypeptide construct and a second polyribonucleotide encoding a Plasmodium CSP polypeptide construct. In some embodiments, a first polyribonucleotide comprises a ribonucleic acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to a ribonucleic acid sequence according to SEQ ID NO: 204. In some embodiments, a first polyribonucleotide comprises a ribonucleic acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to a ribonucleic acid sequence according to SEQ ID NO: 82. In some embodiments, a combination as described herein further comprises a third polyribonucleotide encoding a second Plasmodium T-cell string polypeptide construct. In some embodiments, a third polyribonucleotide comprises a ribonucleic acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to a ribonucleic acid sequence according to SEQ ID NO: 210. [0713] In some embodiments, a combination as described herein comprises a first polyribonucleotide encoding a Plasmodium T-cell string polypeptide construct and a second polyribonucleotide encoding a Plasmodium CSP polypeptide construct. In some embodiments, a first polyribonucleotide comprises a ribonucleic acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to a ribonucleic acid sequence according to SEQ ID NO: 210. In some embodiments, a first polyribonucleotide comprises a ribonucleic acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to a ribonucleic acid sequence according to SEQ ID NOs: 34, 145, 147, 149, 151, 153, 155, and 157. In some embodiments, a first polyribonucleotide comprises a ribonucleic acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to a ribonucleic acid sequence according to SEQ ID NO: 147. [0714] In some embodiments, a combination as described herein comprises a first polyribonucleotide encoding a Plasmodium T-cell string polypeptide construct and a second polyribonucleotide encoding a Plasmodium CSP polypeptide construct. In some embodiments, a first polyribonucleotide comprises a ribonucleic acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to a ribonucleic acid sequence according to SEQ ID NO: 210. In some embodiments, a first polyribonucleotide comprises a ribonucleic acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to a ribonucleic acid sequence according to SEQ ID NO: 82. III. RNA Delivery Technologies [0715] Provided polyribonucleotides may be delivered for therapeutic applications described herein using any appropriate methods known in the art, including, e.g., delivery as naked RNAs, or delivery mediated by viral and/or non-viral vectors, polymer-based vectors, lipid compositions, nanoparticles (e.g., lipid nanoparticles, polymeric nanoparticles, lipid-polymer hybrid nanoparticles, etc.), and/or polypeptide-based vectors. See, e.g., Wadhwa et al. “Opportunities and Challenges in the Delivery of mRNA-Based Vaccines” Pharmaceutics (2020) 102 (27 pages), the content of which is incorporated herein by reference, for information on various approaches that may be useful for delivery polyribonucleotides described herein. [0716] In some embodiments, one or more polyribonucleotides can be formulated with lipid nanoparticles for delivery (e.g., administration). [0717] In some embodiments, lipid nanoparticles can be designed to protect polyribonucleotides from extracellular RNases and/or engineered for systemic delivery of the RNA to target cells (e.g., liver cells). In some embodiments, such lipid nanoparticles may be particularly useful to deliver polyribonucleotides when polyribonucleotides are intravenously or intramuscularly administered to a subject. A. Lipid Compositions 1. Lipids and Lipid-Like Materials [0718] The terms "lipid" and "lipid-like material" are broadly defined herein as molecules which comprise one or more hydrophobic moieties or groups and optionally also one or more hydrophilic moieties or groups. Molecules comprising hydrophobic moieties and hydrophilic moieties are also frequently denoted as amphiphiles. Lipids are usually poorly soluble in water. In an aqueous environment, the amphiphilic nature allows the molecules to self- assemble into organized structures and different phases. One of those phases consists of lipid bilayers, as they are present in vesicles, multilamellar/unilamellar liposomes, or membranes in an aqueous environment. Hydrophobicity can be conferred by the inclusion of a polar groups that include, but are not limited to, long-chain saturated and unsaturated aliphatic hydrocarbon groups and such groups substituted by one or more aromatic, cycloaliphatic, or heterocyclic group(s). The hydrophilic groups may comprise polar and/or charged groups and include carbohydrates, phosphate, carboxylic, sulfate, amino, sulfhydryl, nitro, hydroxyl, and other like groups. [0719] Often, an amphiphilic compound has a polar head attached to a long hydrophobic tail. In some embodiments, the polar portion is soluble in water, while the non-polar portion is insoluble in water. In addition, the polar portion may have either a formal positive charge, or a formal negative charge. Alternatively, the polar portion may have both a formal positive and a negative charge, and be a zwitterion or inner salt. For purposes of the disclosure, the amphiphilic compound can be, but is not limited to, one or a plurality of natural or non-natural lipids and lipid-like compounds. [0720] A "lipid-like material" is a substance that is structurally and/or functionally related to a lipid but may not be considered a lipid in a strict sense. For example, the term includes compounds that are able to form amphiphilic layers as they are present in vesicles, multilamellar/unilamellar liposomes, or membranes in an aqueous environment and includes surfactants, or synthesized compounds with both hydrophilic and hydrophobic moieties. Generally speaking, the term refers to molecules, which comprise hydrophilic and hydrophobic moieties with different structural organization, which may or may not be similar to that of lipids. [0721] Specific examples of amphiphilic compounds that may be included in an amphiphilic layer include, but are not limited to, phospholipids, aminolipids and sphingolipids. [0722] Generally, lipids may be divided into eight categories: fatty acids, glycerolipids, glycerophospholipids, sphingolipids, saccharolipids, polyketides (derived from condensation of ketoacyl subunits), sterols and prenol lipids (derived from condensation of isoprene subunits). Although the term "lipid" is sometimes used as a synonym for fats, fats are a subgroup of lipids called triglycerides. Lipids also encompass molecules such as fatty acids and their derivatives (including tri-, di-, monoglycerides, and phospholipids), as well as sterol-containing metabolites such as cholesterol. [0723] Fatty acids are a diverse group of molecules made of a hydrocarbon chain that terminates with a carboxylic acid group; this arrangement confers the molecule with a polar, hydrophilic end, and a nonpolar, hydrophobic end that is insoluble in water. The carbon chain, typically between four and 24 carbons long, may be saturated or unsaturated, and may be attached to functional groups containing oxygen, halogens, nitrogen, and sulfur. If a fatty acid contains a double bond, there is the possibility of either a cis or trans geometric isomerism, which significantly affects the molecule's configuration. Cis-double bonds cause the fatty acid chain to bend, an effect that is compounded with more double bonds in the chain. Other major lipid classes in the fatty acid category are the fatty esters and fatty amides. [0724] Glycerolipids are composed of mono-, di-, and tri-substituted glycerols, the best-known being the fatty acid triesters of glycerol, called triglycerides. The word "triacylglycerol" is sometimes used synonymously with "triglyceride". In these compounds, the three hydroxyl groups of glycerol are each esterified, typically by different fatty acids. Additional subclasses of glycerolipids are represented by glycosylglycerols, which are characterized by the presence of one or more sugar residues attached to glycerol via a glycosidic linkage. [0725] Glycerophospholipids are amphipathic molecules (containing both hydrophobic and hydrophilic regions) that contain a glycerol core linked to two fatty acid-derived "tails" by ester linkages and to one "head" group by a phosphate ester linkage. Examples of glycerophospholipids, usually referred to as phospholipids (though sphingomyelins are also classified as phospholipids) are phosphatidylcholine (also known as PC, GPCho or lecithin), phosphatidylethanolamine (PE or GPEtn) and phosphatidylserine (PS or GPSer). [0726] Sphingolipids are members of a complex family of compounds that share a common structural feature, a sphingoid base backbone. The major sphingoid base in mammals is commonly referred to as sphingosine. Ceramides (N-acyl-sphingoid bases) are a major subclass of sphingoid base derivatives with an amide-linked fatty acid. The fatty acids are typically saturated or mono-unsaturated with chain lengths from 16 to 26 carbon atoms. The major phosphosphingolipids of mammals are sphingomyelins (ceramide phosphocholines), whereas insects contain mainly ceramide phosphoethanolamines and fungi have phytoceramide phosphoinositols and mannose-containing headgroups. The glycosphingolipids are a diverse family of molecules composed of one or more sugar residues linked via a glycosidic bond to the sphingoid base. Examples of these are the simple and complex glycosphingolipids such as cerebrosides and gangliosides. [0727] Sterols, such as cholesterol and its derivatives, or tocopherol and its derivatives, are important components of membrane lipids, along with the glycerophospholipids and sphingomyelins. [0728] Saccharolipids are compounds in which fatty acids are linked directly to a sugar backbone, forming structures that are compatible with membrane bilayers. In the saccharolipids, a monosaccharide substitutes for the glycerol backbone present in glycerolipids and glycerophospholipids. The most familiar saccharolipids are the acylated glucosamine precursors of the Lipid A component of the lipopolysaccharides in Gram-negative bacteria. Typical lipid A molecules are disaccharides of glucosamine, which are derivatized with as many as seven fatty-acyl chains. The minimal lipopolysaccharide required for growth in E. coli is Kdo2-Lipid A, a hexa-acylated disaccharide of glucosamine that is glycosylated with two 3-deoxy-D-manno-octulosonic acid (Kdo) residues. [0729] Polyketides are synthesized by polymerization of acetyl and propionyl subunits by classic enzymes as well as iterative and multimodular enzymes that share mechanistic features with the fatty acid synthases. They comprise a large number of secondary metabolites and natural products from animal, plant, bacterial, fungal and marine sources, and have great structural diversity. Many polyketides are cyclic molecules whose backbones are often further modified by glycosylation, methylation, hydroxylation, oxidation, or other processes. [0730] Lipids and lipid-like materials may be cationic, anionic or neutral. Neutral lipids or lipid-like materials exist in an uncharged or neutral zwitterionic form at a selected pH. [0731] In some embodiments, suitable lipids or lipid-like materials for use in the present disclosure include those described in WO2020/128031 and US20200163878, the entire contents of each of which are incorporated herein by reference for the purposes described herein. 2. Cationic or Cationically Ionizable Lipids or Lipid-Like Materials [0732] In some embodiments cationic or cationically ionizable lipids or lipid-like materials contemplated for use herein include any cationic or cationically ionizable lipids or lipid-like materials which are able to electrostatically bind nucleic acid. In some embodiments, cationic or cationically ionizable lipids or lipid-like materials contemplated for use herein can be associated with nucleic acid, e.g. by forming complexes with the nucleic acid or forming vesicles in which the nucleic acid is enclosed or encapsulated. [0733] Cationic lipids or lipid-like materials are characterized in that they have a net positive charge (e.g., at a relevant pH). Cationic lipids or lipid-like materials bind negatively charged nucleic acid by electrostatic interaction. Generally, cationic lipids possess a lipophilic moiety, such as a sterol, an acyl chain, a diacyl or more acyl chains, and the head group of the lipid typically carries the positive charge. [0734] In certain embodiments, a cationic lipid or lipid-like material has a net positive charge only at certain pH, in particular acidic pH, while it has preferably no net positive charge, preferably has no charge, i.e., it is neutral, at a different, preferably higher pH such as physiological pH. This ionizable behavior is thought to enhance efficacy through helping with endosomal escape and reducing toxicity as compared with particles that remain cationic at physiological pH. [0735] In some embodiments, a cationic or cationically ionizable lipid or lipid-like material comprises a head group which includes at least one nitrogen atom (N) which is positive charged or capable of being protonated. [0736] Examples of cationic lipids include, but are not limited to 1,2-dioleoyl-3-trimethylammonium propane (DOTAP); N,N-dimethyl-2,3-dioleyloxypropylamine (DODMA), 1,2-di-O-octadecenyl-3-trimethylammonium propane (DOTMA), 3-(N—(N′,N′-dimethylaminoethane)-carbamoyl)cholesterol (DC-Chol), dimethyldioctadecylammonium (DDAB); 1,2-dioleoyl-3-dimethylammonium-propane (DODAP); 1,2-diacyloxy-3-dimethylammonium propanes; 1,2- dialkyloxy-3-dimethylammonium propanes; dioctadecyldimethyl ammonium chloride (DODAC), 1,2-distearyloxy-N,N- dimethyl-3-aminopropane (DSDMA), 2,3-di(tetradecoxy)propyl-(2-hydroxyethyl)-dimethylazanium (DMRIE), 1,2- dimyristoyl-sn-glycero-3-ethylphosphocholine (DMEPC), l,2-dimyristoyl-3-trimethylammonium propane (DMTAP), 1,2- dioleyloxypropyl-3-dimethyl-hydroxyethyl ammonium bromide (DORIE), and 2,3-dioleoyloxy- N-[2(spermine carboxamide)ethyl]-N,N-dimethyl-l-propanamium trifluoroacetate (DOSPA), 1,2-dilinoleyloxy-N,N- dimethylaminopropane (DLinDMA), 1,2-dilinolenyloxy-N,N-dimethylaminopropane (DLenDMA), dioctadecylamidoglycyl spermine (DOGS), 3-dimethylamino-2-(cholest-5-en-3-beta-oxybutan-4-oxy)-1-(cis,cis-9,12-oc- tadecadienoxy)propane (CLinDMA), 2-[5′-(cholest-5-en-3-beta-oxy)-3′-oxapentoxy)-3-dimethyl-1-(cis,cis-9′,12′- octadecadienoxy)propane (CpLinDMA), N,N-dimethyl-3,4-dioleyloxybenzylamine (DMOBA), 1,2-N,N′-dioleylcarbamyl- 3-dimethylaminopropane (DOcarbDAP), 2,3-Dilinoleoyloxy-N,N-dimethylpropylamine (DLinDAP), 1,2-N,N′- Dilinoleylcarbamyl-3-dimethylaminopropane (DLincarbDAP), 1,2-Dilinoleoylcarbamyl-3-dimethylaminopropane (DLinCDAP), 2,2-dilinoleyl-4-dimethylaminomethyl-[1,3]-dioxolane (DLin-K-DMA), 2,2-dilinoleyl-4-dimethylaminoethyl- [1,3]-dioxolane (DLin-K-XTC2-DMA), 2,2-dilinoleyl-4-(2-dimethylaminoethyl)-[1,3]-dioxolane (DLin-KC2-DMA), heptatriaconta-6,9,28,31-tetraen-19-yl-4-(dimethylamino)butanoate (DLin-MC3-DMA), N-(2-Hydroxyethyl)-N,N- dimethyl-2,3-bis(tetradecyloxy)-1-propanaminium bromide (DMRIE), (±)-N-(3-aminopropyl)-N,N-dimethyl-2,3-bis(cis- 9-tetradecenyloxy)-1-propanaminium bromide (GAP-DMORIE), (±)-N-(3-aminopropyl)-N,N-dimethyl-2,3- bis(dodecyloxy)-1-propanaminium bromide (GAP-DLRIE), (±)-N-(3-aminopropyl)-N,N-dimethyl-2,3- bis(tetradecyloxy)-1-propanaminium bromide (GAP-DMRIE), N-(2-Aminoethyl)-N,N-dimethyl-2,3-bis(tetradecyloxy)-1- propanaminium bromide (βAE-DMRIE), N-(4-carboxybenzyl)-N,N-dimethyl-2,3-bis(oleoyloxy)propan-1-aminium (DOBAQ), 2-({8-[(3β)-cholest-5-en-3-yloxy]octyl}oxy)-N,N-dimethyl-3-[(9Z,12Z)-octadeca-9,12-dien-1-yloxy]propan- 1-amine (Octyl-CLinDMA), 1,2-dimyristoyl-3-dimethylammonium-propane (DMDAP), 1,2-dipalmitoyl-3- dimethylammonium-propane (DPDAP), N1-[2-((1S)-1-[(3-aminopropyl)amino]-4-[di(3-amino- propyl)amino]butylcarboxamido)ethyl]-3,4-di[oleyloxy]-benzamide (MVL5), 1,2-dioleoyl-sn-glycero-3- ethylphosphocholine (DOEPC), 2,3-bis(dodecyloxy)-N-(2-hydroxyethyl)-N,N-dimethylpropan-1-amonium bromide (DLRIE), N-(2-aminoethyl)-N,N-dimethyl-2,3-bis(tetradecyloxy)propan-1-aminium bromide (DMORIE), di((Z)-non-2- en-1-yl) 8,8'-((((2(dimethylamino)ethyl)thio)carbonyl)azanediyl)dioctanoate (ATX), N,N-dimethyl-2,3- bis(dodecyloxy)propan-1-amine (DLDMA), N,N-dimethyl-2,3-bis(tetradecyloxy)propan-1-amine (DMDMA), Di((Z)-non- 2-en-1-yl)-9-((4-(dimethylaminobutanoyl)oxy)heptadecanedioate (L319), N-Dodecyl-3-((2-dodecylcarbamoyl-ethyl)- {2-[(2-dodecylcarbamoyl-ethyl)-2-{(2-dodecylcarbamoyl-ethyl)-[2-(2-dodecylcarbamoyl-ethylamino)-ethyl]-amino}- ethylamino)propionamide (lipidoid 98N12-5), 1-[2-[bis(2-hydroxydodecyl)amino]ethyl-[2-[4-[2-[bis(2 hydroxydodecyl)amino]ethyl]piperazin-1-yl]ethyl]amino]dodecan-2-ol (lipidoid C12-200), LIPOFECTIN® (commercially available cationic liposomes comprising DOTMA and 1 ,2-dioleoyl-sn-3phosphoethanolamine (DOPE), from GIBCO/BRL, Grand Island, N.Y.); LIPOFECTAMINE® (commercially available cationic liposomes comprising N-(1 -(2,3dioleyloxy)propyl)-N-(2-(sperminecarboxamido)ethyl)-N,N-dimethylammonium trifluoroacetate (DOSPA) and (DOPE), from GIBCO/BRL); and TRANSFECTAM® (commercially available cationic lipids comprising dioctadecylamidoglycyl carboxyspermine (DOGS) in ethanol from Promega Corp., Madison, Wis.) or any combination of any of the foregoing. Further suitable cationic lipids for use in the present disclosure include those described in WO2020/128031 and US20200163878, the entire contents of each of which are incorporated herein by reference for the purposes described herein. Further suitable cationic lipids for use in the present disclosure include those described in WO2010/053572 (including Cl 2-200 described at paragraph [00225]) and WO2012/170930, both of which are incorporated herein by reference for the purposes described herein. Additional suitable cationic lipids for use in the present disclosure include HGT4003, HGT5000, HGTS001, HGT5001, HGT5002 (see US20150140070A1, which is incorporated herein by reference in its entirety). [0737] In some embodiments, formulations that are useful for pharmaceutical compositions (e.g., immunogenic compositions, e.g., vaccines) compositions as described herein can comprise at least one cationic lipid. Representative cationic lipids include, but are not limited to, 1 ,2-dilinoleyoxy-3-(dimethylamino)acetoxypropane (DLin-DAC), 1 ,2-dilinoleyoxy-3morpholinopropane (DLin-MA), 1,2-dilinoleoyl-3-dimethylaminopropane (DLinDAP), 1 ,2-dilinoleylthio-3-dimethylaminopropane (DLin-S-DMA), 1 -linoleoyl-2-linoleyloxy-3dimethylaminopropane (DLin-2- DMAP), 1 ,2-dilinoleyloxy-3-trimethylaminopropane chloride salt (DLin-TMA.CI), 1 ,2-dilinoleoyl-3- trimethylaminopropane chloride salt (DLin-TAP.CI), 1 ,2-dilinoleyloxy-3-(N-methylpiperazino)propane (DLin-MPZ), 3- (N,Ndilinoleylamino)-1 ,2-propanediol (DLinAP), 3-(N,N-dioleylamino)-1 ,2-propanediol (DOAP), 1 ,2-dilinoleyloxo-3- (2-N,N-dimethylamino)ethoxypropane (DLin-EG-DMA), and 2,2-dilinoleyl-4-dimethylaminomethyl-[1 ,3]-dioxolane (DLin-K-DMA), 2,2-dilinoleyl-4-(2-dimethylaminoethyl)-[1 ,3]-dioxolane (DLin-KC2-DMA); dilinoleyl-methyl-4- dimethylaminobutyrate (DLin-MC3-DMA); MC3 (US20100324120, which is incorporated herein by reference in its entirety). [0738] In some embodiments, amino or cationic lipids useful in accordance with the present disclosure have at least one protonatable or deprotonatable group, such that the lipid is positively charged at a pH at or below physiological pH (e.g. pH 7.4), and neutral at a second pH, preferably at or above physiological pH. It will, of course, be understood that the addition or removal of protons as a function of pH is an equilibrium process, and that the reference to a charged or a neutral lipid refers to the nature of the predominant species and does not require that all of lipids have to be present in the charged or neutral form. Lipids having more than one protonatable or deprotonatable group, or which are zwitterionic, are not excluded and may likewise be suitable in the context of the present invention. [0739] In some embodiments, a protonatable lipid has a pKa of the protonatable group in the range of about 4 to about 11, e.g., a pKa of about 5 to about 7. [0740] In some embodiments, a cationic lipid may comprise from about 10 mol % to about 100 mol %, about 20 mol % to about 100 mol %, about 30 mol % to about 100 mol %, about 40 mol % to about 100 mol %, or about 50 mol % to about 100 mol % of total lipid present in a lipid composition utilized in accordance with the present disclosure. 3. Additional Lipids or Lipid-Like Materials [0741] In some embodiments, formulations utilized in accordance with the present disclosure may comprise lipids or lipid-like materials other than cationic or cationically ionizable lipids or lipid-like materials, i.e., non-cationic lipids or lipid-like materials (including non-cationically ionizable lipids or lipid-like materials). Collectively, anionic and neutral lipids or lipid-like materials are referred to herein as non-cationic lipids or lipid-like materials. In some embodiments, optimizing a formulation of nucleic acid particles by addition of other hydrophobic moieties, such as cholesterol and lipids, in addition to an ionizable/cationic lipid or lipid-like material may, for example, enhance particle stability and efficacy of nucleic acid delivery. [0742] In some embodiments, a lipid or lipid-like material may be incorporated which may or may not affect the overall charge of particles. In certain embodiments, such lipid or lipid-like material is a non-cationic lipid or lipid- like material. [0743] In some embodiments, a non-cationic lipid may comprise, e.g., one or more anionic lipids and/or neutral lipids. An "anionic lipid" is negatively charged (e.g., at a selected pH). [0744] A "neutral lipid" exists either in an uncharged or neutral zwitterionic form (e.g., at a selected pH). In some embodiments, a formulation comprises one of the following neutral lipid components: (1) a phospholipid, (2) cholesterol or a derivative thereof; or (3) a mixture of a phospholipid and cholesterol or a derivative thereof. Examples of cholesterol derivatives include, but are not limited to, cholestanol, cholestanone, cholestenone, coprostanol, cholesteryl-2'-hydroxyethyl ether, cholesteryl-4'- hydroxybutyl ether, tocopherol and derivatives thereof, and mixtures thereof. [0745] Specific exemplary phospholipids that can be used include, but are not limited to, phosphatidylcholines, phosphatidylethanolamines, phosphatidylglycerols, phosphatidic acids, phosphatidylserines or sphingomyelin. Such phospholipids include in particular diacylphosphatidylcholines, such as distearoylphosphatidylcholine (DSPC), dioleoylphosphatidylcholine (DOPC), dimyristoylphosphatidylcholine (DMPC), dipentadecanoylphosphatidylcholine, dilauroylphosphatidylcholine, dipalmitoylphosphatidylcholine (DPPC), diarachidoylphosphatidylcholine (DAPC), dibehenoylphosphatidylcholine (DBPC), ditricosanoylphosphatidylcholine (DTPC), dilignoceroylphatidylcholine (DLPC), palmitoyloleoyl-phosphatidylcholine (POPC), 1,2-di-O-octadecenyl-sn-glycero-3-phosphocholine (18:0 Diether PC), 1- oleoyl-2-cholesterylhemisuccinoyl-sn-glycero-3-phosphocholine (OChemsPC), 1-hexadecyl-sn-glycero-3- phosphocholine (C16 Lyso PC) and phosphatidylethanolamines, in particular diacylphosphatidylethanolamines, such as dioleoylphosphatidylethanolamine (DOPE), distearoyl-phosphatidylethanolamine (DSPE), dipalmitoyl- phosphatidylethanolamine (DPPE), dimyristoyl-phosphatidylethanolamine (DMPE), dilauroyl- phosphatidylethanolamine (DLPE), diphytanoyl-phosphatidylethanolamine (DPyPE), and further phosphatidylethanolamine lipids with different hydrophobic chains. [0746] In certain embodiments, a formulation utilized in accordance with the present disclosure includes DSPC or DSPC and cholesterol. [0747] In certain embodiments, formulations utilized in accordance with the present disclosure include both a cationic lipid and an additional (non-cationic) lipid. [0748] In some embodiments, formulations herein include a polymer conjugated lipid such as a pegylated lipid. "Pegylated lipids" comprise both a lipid portion and a polyethylene glycol portion. Pegylated lipids are known in the art. [0749] Without wishing to be bound by theory, the amount of (total) cationic lipid compared to the amount of other lipid(s) in formulation may affect important characteristics, such as charge, particle size, stability, tissue selectivity, and bioactivity of the nucleic acid. In some embodiments, the molar ratio of the at least one cationic lipid to the at least one additional lipid is from about 10:0 to about 1:9, about 4:1 to about 1:2, or about 3:1 to about 1:1. [0750] In some embodiments, a non-cationic lipid, in particular a neutral lipid, (e.g., one or more phospholipids and/or cholesterol) may comprise from about 0 mol % to about 90 mol %, from about 0 mol % to about 80 mol %, from about 0 mol % to about 70 mol %, from about 0 mol % to about 60 mol %, or from about 0 mol % to about 50 mol %, of the total lipid present in a formulation. 4. Lipoplex Particles [0751] In certain embodiments of the present disclosure, the RNA described herein may be present in RNA lipoplex particles. [0752] An "RNA lipoplex particle" contains lipid, in particular cationic lipid, and RNA. Electrostatic interactions between positively charged liposomes and negatively charged RNA results in complexation and spontaneous formation of RNA lipoplex particles. Positively charged liposomes may be generally synthesized using a cationic lipid, such as DOTMA, and additional lipids, such as DOPE. In some embodiments, an RNA lipoplex particle is a nanoparticle. [0753] In certain embodiments, RNA lipoplex particles include both a cationic lipid and an additional lipid. In an exemplary embodiment, the cationic lipid is DOTMA and the additional lipid is DOPE. [0754] In some embodiments, the molar ratio of the at least one cationic lipid to the at least one additional lipid is from about 10:0 to about 1:9, about 4:1 to about 1:2, or about 3:1 to about 1:1. In specific embodiments, the molar ratio may be about 3:1, about 2.75:1, about 2.5:1, about 2.25:1, about 2:1, about 1.75:1, about 1.5:1, about 1.25:1, or about 1:1. In an exemplary embodiment, the molar ratio of the at least one cationic lipid to the at least one additional lipid is about 2:1. [0755] In some embodiments, RNA lipoplex particles have an average diameter that in one embodiment ranges from about 200 nm to about 1000 nm, from about 200 nm to about 800 nm, from about 250 to about 700 nm, from about 400 to about 600 nm, from about 300 nm to about 500 nm, or from about 350 nm to about 400 nm. In specific embodiments, the RNA lipoplex particles have an average diameter of about 200 nm, about 225 nm, about 250 nm, about 275 nm, about 300 nm, about 325 nm, about 350 nm, about 375 nm, about 400 nm, about 425 nm, about 450 nm, about 475 nm, about 500 nm, about 525 nm, about 550 nm, about 575 nm, about 600 nm, about 625 nm, about 650 nm, about 700 nm, about 725 nm, about 750 nm, about 775 nm, about 800 nm, about 825 nm, about 850 nm, about 875 nm, about 900 nm, about 925 nm, about 950 nm, about 975 nm, or about 1000 nm. In an embodiment, the RNA lipoplex particles have an average diameter that ranges from about 250 nm to about 700 nm. In another embodiment, the RNA lipoplex particles have an average diameter that ranges from about 300 nm to about 500 nm. In an exemplary embodiment, the RNA lipoplex particles have an average diameter of about 400 nm. [0756] RNA lipoplex particles and compositions comprising RNA lipoplex particles described herein are useful for delivery of RNA to a target tissue after parenteral administration, in particular after intravenous administration. The RNA lipoplex particles may be prepared using liposomes that may be obtained by injecting a solution of the lipids in ethanol into water or a suitable aqueous phase. In some embodiments, the aqueous phase has an acidic pH. In some embodiments, the aqueous phase comprises acetic acid, e.g., in an amount of about 5 mM. Liposomes may be used for preparing RNA lipoplex particles by mixing the liposomes with RNA. In some embodiments, the liposomes and RNA lipoplex particles comprise at least one cationic lipid and at least one additional lipid. In some embodiments, the at least one cationic lipid comprises 1,2-di-O-octadecenyl-3-trimethylammonium propane (DOTMA) and/or 1,2- dioleoyl-3-trimethylammonium-propane (DOTAP). In some embodiments, the at least one additional lipid comprises 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine (DOPE), cholesterol (Chol) and/or 1,2-dioleoyl-sn- glycero-3-phosphocholine (DOPC). In some embodiments, the at least one cationic lipid comprises 1,2-di-O- octadecenyl-3-trimethylammonium propane (DOTMA) and the at least one additional lipid comprises 1,2-di-(9Z- octadecenoyl)-sn-glycero-3-phosphoethanolamine (DOPE). In some embodiments, the liposomes and RNA lipoplex particles comprise 1,2-di-O-octadecenyl-3-trimethylammonium propane (DOTMA) and 1,2-di-(9Z-octadecenoyl)-sn- glycero-3-phosphoethanolamine (DOPE). [0757] Spleen targeting RNA lipoplex particles are described in WO 2013/143683, herein incorporated by reference. It has been found that RNA lipoplex particles having a net negative charge may be used to preferentially target spleen tissue or spleen cells such as antigen-presenting cells, in particular dendritic cells. Accordingly, following administration of the RNA lipoplex particles, RNA accumulation and/or RNA expression in the spleen occurs. Thus, RNA lipoplex particles of the disclosure may be used for expressing RNA in the spleen. In an embodiment, after administration of the RNA lipoplex particles, no or essentially no RNA accumulation and/or RNA expression in the lung and/or liver occurs. In some embodiments, after administration of the RNA lipoplex particles, RNA accumulation and/or RNA expression in antigen presenting cells, such as professional antigen presenting cells in the spleen occurs. Thus, RNA lipoplex particles of the disclosure may be used for expressing RNA in such antigen presenting cells. In some embodiments, the antigen presenting cells are dendritic cells and/or macrophages. 5. Lipid Nanoparticles (LNPs) [0758] In some embodiments, nucleic acid such as RNA described herein is administered in the form of lipid nanoparticles (LNPs). In some embodiments, LNPs may comprise any lipid capable of forming a particle to which the one or more nucleic acid molecules are attached, or in which the one or more nucleic acid molecules are encapsulated. [0759] In some embodiments, an LNP comprises one or more cationic lipids, and one or more stabilizing lipids. Stabilizing lipids include neutral lipids and pegylated lipids. [0760] In some embodiments, an LNP comprises a cationic lipid, a neutral lipid, a sterol, a polymer conjugated lipid; and an RNA, encapsulated within or associated with the lipid nanoparticle. [0761] In some embodiments, a neutral lipid is selected from the group consisting of DSPC, DPPC, DMPC, DOPC, POPC, DOPE, DOPG, DPPG, POPE, DPPE, DMPE, DSPE, and SM. In some embodiments, the neutral lipid is selected from the group consisting of DSPC, DPPC, DMPC, DOPC, POPC, DOPE and SM. In some embodiments, the neutral lipid is DSPC. [0762] In some embodiments, a sterol is cholesterol. [0763] In some embodiments, a polymer conjugated lipid is a pegylated lipid. In some embodiments, a pegylated lipid has the following structure: or a pharmaceutically acceptable salt, tautomer or stereoisomer thereof, wherein: R12 and R13 are each independently a straight or branched, saturated or unsaturated alkyl chain containing from 10 to 30 carbon atoms, wherein the alkyl chain is optionally interrupted by one or more ester bonds; and w has a mean value ranging from 30 to 60. In some embodiments, R12 and R13 are each independently straight, saturated alkyl chains containing from 12 to 16 carbon atoms. In some embodiments, w has a mean value ranging from 40 to 55. In some embodiments, the average w is about 45. In some embodiments, R12 and R13 are each independently a straight, saturated alkyl chain containing about 14 carbon atoms, and w has a mean value of about 45. [0764] In some embodiments, a pegylated lipid is DMG-PEG 2000, e.g., having the following structure: . [0765] In some embodiments, a cationic lipid component of LNPs has the structure of Formula (III): or a pharmaceutically acceptable salt, tautomer, prodrug or stereoisomer thereof, wherein: one of L1 or L2 is –O(C=O)-, -(C=O)O-, -C(=O)-, -O-, -S(O)x-, -S-S-, C(=O)S-, SC(=O)-, -NRaC(=O)-, -C(=O)NRa-, NRaC(=O)NRa , -OC(=O)NRa- or -NRaC(=O)O-, and the other of L1 or L2 is –O(C=O)-, -(C=O)O-, -C(=O)-, -O-, - S(O)x-, -S S-, -C(=O)S-, SC(=O)-, -NRaC(=O)-, -C(=O)NRa-, NRaC(=O)NRa , -OC(=O)NRa- or -NRaC(=O)O- or a direct bond; G1 and G2 are each independently unsubstituted C1-C12 alkylene or C1-C12 alkenylene; G3 is C1-C24 alkylene, C1-C24 alkenylene, C3-C8 cycloalkylene, C3-C8 cycloalkenylene; Ra is H or C1-C12 alkyl; R1 and R2 are each independently C6-C24 alkyl or C6-C24 alkenyl; R3 is H, OR5, CN, C(=O)OR4, OC(=O)R4 or –NR5C(=O)R4; R4 is C1-C12 alkyl; R5 is H or C1-C6 alkyl; and x is 0, 1 or 2. [0766] In some of the foregoing embodiments of Formula (III), the lipid has one of the following structures (IIIA) or (IIIB): (IIIA) (IIIB) wherein: A is a 3 to 8-membered cycloalkyl or cycloalkylene ring; R6 is, at each occurrence, independently H, OH or C1-C24 alkyl; n is an integer ranging from 1 to 15. [0767] In some of the foregoing embodiments of Formula (III), the lipid has structure (IIIA), and in other embodiments, the lipid has structure (IIIB). [0768] In other embodiments of Formula (III), the lipid has one of the following structures (IIIC) or (IIID): (IIIC) (IIID) wherein y and z are each independently integers ranging from 1 to 12.In any of the foregoing embodiments of Formula (III), one of L¹ or L² is -O(C=O)-. For example, in some embodiments each of L¹ and L² are -O(C=O)-. In some different embodiments of any of the foregoing, L¹ and L² are each independently -(C=O)O- or -O(C=O)-. For example, in some embodiments each of L¹ and L² is -(C=O)O-. [0769] In some different embodiments of Formula (III), the lipid has one of the following structures (IIIE) or (IIIF): (IIIE) (IIIF) [0770] In some of the foregoing embodiments of Formula (III), the lipid has one of the following structures ( (IIII) (IIIJ) [0771] In some of the foregoing embodiments of Formula (III), n is an integer ranging from 2 to 12, for example from 2 to 8 or from 2 to 4. For example, in some embodiments, n is 3, 4, 5 or 6. In some embodiments, n is 3. In some embodiments, n is 4. In some embodiments, n is 5. In some embodiments, n is 6. [0772] In some other of the foregoing embodiments of Formula (III), y and z are each independently an integer ranging from 2 to 10. For example, in some embodiments, y and z are each independently an integer ranging from 4 to 9 or from 4 to 6. [0773] In some of the foregoing embodiments of Formula (III), R6 is H. In other of the foregoing embodiments, R6 is C1-C24 alkyl. In other embodiments, R6 is OH. [0774] In some embodiments of Formula (III), G3 is unsubstituted. In other embodiments, G3 is substituted. In various different embodiments, G3 is linear C1-C24 alkylene or linear C1-C24 alkenylene. [0775] In some other foregoing embodiments of Formula (III), R1 or R2, or both, is C6-C24 alkenyl. For example, in some embodiments, R1 and R2 each, independently have the following structure: , wherein: R^7a and R^7b are, at each occurrence, independently H or C₁-C₁₂ alkyl; and a is an integer from 2 to 12, wherein R^7a, R^7b and a are each selected such that R¹ and R² each independently comprise from 6 to 20 carbon atoms. For example, in some embodiments a is an integer ranging from 5 to 9 or from 8 to 12. [0776] In some of the foregoing embodiments of Formula (III), at least one occurrence of R7a is H. For example, in some embodiments, R7a is H at each occurrence. In other different embodiments of the foregoing, at least one occurrence of R7b is C1-C8 alkyl. For example, in some embodiments, C1-C8 alkyl is methyl, ethyl, n- propyl, iso-propyl, n-butyl, iso-butyl, tert-butyl, n-hexyl or n-octyl. [0777] In different embodiments of Formula (III), R1 or R2, or both, has one of the following structures: ; [0778] In some of the foregoing embodiments of Formula (III), R3 is OH, CN, C(=O)OR4, OC(=O)R4 or – NHC(=O)R4. In some embodiments, R4 is methyl or ethyl. [0779] In various different embodiments, the cationic lipid of Formula (III) has one of the structures set forth in in Table 14 below. Table 14: Exemplary Compounds of Formula (III)

[0780] In various different embodiments, a cationic lipid has one of the structures set forth in Table 15 below. Table 15: Exemplary Cationic Lipid Structures

[0781] In some embodiments, an LNP comprises a cationic lipid that is an ionizable lipid-like material (lipidoid). In some embodiments, a cationic lipid has the following structure: . [0782] In some embodiments, lipid nanoparticles can have an average size (e.g., mean diameter) of about 30 nm to about 150 nm, about 40 nm to about 150 nm, about 50 nm to about 150 nm, about 60 nm to about 130 nm, about 70 nm to about 110 nm, about 70 nm to about 100 nm, about 70 to about 90 nm, or about 70 nm to about 80 nm. In some embodiments, lipid nanoparticles in accordance with the present disclosure can have an average size (e.g., mean diameter) of about 50 nm to about 100 nm. In some embodiments, lipid nanoparticles may have an average size (e.g., mean diameter) of about 50 nm to about 150 nm. In some embodiments, lipid nanoparticles may have an average size (e.g., mean diameter) of about 60 nm to about 120 nm. In some embodiments, lipid nanoparticles in accordance with the present disclosure can have an average size (e.g., mean diameter) of about 30 nm, 35 nm, 40 nm, 45 nm, 50 nm, 55 nm, 60 nm, 65 nm, 70 nm, 75 nm, 80 nm, 85 nm, 90 nm, 95 nm, 100 nm, 105 nm, 110 nm, 115 nm, 120 nm, 125 nm, 130 nm, 135 nm, 140 nm, 145 nm, or 150 nm. The term “average diameter” or “mean diameter” refers to the mean hydrodynamic diameter of particles as measured by dynamic laser light scattering (DLS) with data analysis using the so-called cumulant algorithm, which provides as results the so- called Z-average with the dimension of a length, and the polydispersity index (PI), which is dimensionless (Koppel, D., J. Chem. Phys.57, 1972, pp 4814-4820, ISO 13321, which is herein incorporated by reference). Here “average diameter,” “mean diameter,” “diameter,” or “size” for particles is used synonymously with this value of the Z- average. [0783] In some embodiments, lipid nanoparticles described herein may exhibit a polydispersity index less than about 0.5, less than about 0.4, less than about 0.3, or about 0.2 or less. By way of example, lipid nanoparticles can exhibit a polydispersity index in a range of about 0.1 to about 0.3 or about 0.2 to about 0.3. The “polydispersity index” is preferably calculated based on dynamic light scattering measurements by the so-called cumulant analysis as mentioned in the definition of the “average diameter.” Under certain prerequisites, it can be taken as a measure of the size distribution of an ensemble of ribonucleic acid nanoparticles (e.g., ribonucleic acid nanoparticles). [0784] Lipid nanoparticles described herein can be characterized by an “N/P ratio,” which is the molar ratio of cationic (nitrogen) groups (the “N” in N/P) in the cationic polymer to the anionic (phosphate) groups (the “P” in N/P) in RNA. It is understood that a cationic group is one that is either in cationic form (e.g., N+), or one that is ionizable to become cationic. Use of a single number in an N/P ratio (e.g., an N/P ratio of about 5) is intended to refer to that number over 1, e.g., an N/P ratio of about 5 is intended to mean 5:1. In some embodiments, a lipid nanoparticle described herein has an N/P ratio greater than or equal to 5. In some embodiments, a lipid nanoparticle described herein has an N/P ratio that is about 5, 6, 7, 8, 9, or 10. In some embodiments, an N/P ratio for a lipid nanoparticle described herein is from about 10 to about 50. In some embodiments, an N/P ratio for a lipid nanoparticle described herein is from about 10 to about 70. In some embodiments, an N/P ratio for a lipid nanoparticle described herein is from about 10 to about 120. B. Exemplary Methods of Making Lipid Nanoparticles [0785] Lipids and lipid nanoparticles comprising nucleic acids and their method of preparation are known in the art, including, e.g., as described in U.S. Patent Nos. 8,569,256, 5,965,542 and U.S. Patent Publication Nos. 2016/0199485, 2016/0009637, 2015/0273068, 2015/0265708, 2015/0203446, 2015/0005363, 2014/0308304, 2014/0200257, 2013/086373, 2013/0338210, 2013/0323269, 2013/0245107, 2013/0195920, 2013/0123338, 2013/0022649, 2013/0017223, 2012/0295832, 2012/0183581, 2012/0172411, 2012/0027803, 2012/0058188, 2011/0311583, 2011/0311582, 2011/0262527, 2011/0216622, 2011/0117125, 2011/0091525, 2011/0076335, 2011/0060032, 2010/0130588, 2007/0042031, 2006/0240093, 2006/0083780, 2006/0008910, 2005/0175682, 2005/017054, 2005/0118253, 2005/0064595, 2004/0142025, 2007/0042031, 1999/009076 and PCT Pub. Nos. WO 99/39741, WO 2018/081480, WO 2017/004143, WO 2017/075531, WO 2015/199952, WO 2014/008334, WO 2013/086373, WO 2013/086322, WO 2013/016058, WO 2013/086373, W02011/141705, and WO 2001/07548, the full disclosures each of which are herein incorporated by reference in their entirety for the purposes described herein. [0786] For example, in some embodiments, cationic lipids, neutral lipids (e.g., DSPC, and/or cholesterol) and polymer-conjugated lipids can be solubilized in ethanol at a pre-determined molar ratio (e.g., ones described herein). In some embodiments, lipid nanoparticles (lipid nanoparticle) are prepared at a total lipid to polyribonucleotides weight ratio of approximately 10: 1 to 30: 1. In some embodiments, such polyribonucleotides can be diluted to 0.2 mg/mL in acetate buffer. [0787] In some embodiments, using an ethanol injection technique, a colloidal lipid dispersion comprising polyribonucleotides can be formed as follows: an ethanol solution comprising lipids, such as cationic lipids, neutral lipids, and polymer-conjugated lipids, is injected into an aqueous solution comprising polyribonucleotides (e.g., ones described herein). [0788] In some embodiments, lipid and polyribonucleotide solutions can be mixed at room temperature by pumping each solution at controlled flow rates into a mixing unit, for example, using piston pumps. In some embodiments, the flow rates of a lipid solution and an RNA solution into a mixing unit are maintained at a ratio of 1:3. Upon mixing, nucleic acid-lipid particles are formed as the ethanolic lipid solution is diluted with aqueous polyribonucleotides. The lipid solubility is decreased, while cationic lipids bearing a positive charge interact with the negatively charged RNA. [0789] In some embodiments, a solution comprising RNA-encapsulated lipid nanoparticles can be processed by one or more of concentration adjustment, buffer exchange, formulation, and/or filtration. [0790] In some embodiments, RNA-encapsulated lipid nanoparticles can be processed through filtration. [0791] In some embodiments, particle size and/or internal structure of lipid nanoparticles (with or without RNAs) may be monitored by appropriate techniques such as, e.g., small-angle X-ray scattering (SAXS) and/or transmission electron cryomicroscopy (CryoTEM). IV. Pharmaceutical Compositions [0792] The present disclosure provides compositions, e.g., pharmaceutical compositions comprising one or more polyribonucleotides described herein. Pharmaceutical formulations may additionally comprise a pharmaceutically acceptable excipient, which, as used herein, includes any and all solvents, dispersion media, diluents, or other liquid vehicles, dispersion or suspension aids, surface active agents, isotonic agents, thickening or emulsifying agents, preservatives, solid binders, lubricants and the like, as suited to the particular dosage form desired. Remington's The Science and Practice of Pharmacy, 21st Edition, A. R. Gennaro (Lippincott, Williams & Wilkins, Baltimore, MD, 2006; incorporated herein by reference) discloses various excipients used in formulating pharmaceutical compositions and known techniques for the preparation thereof. Except insofar as any conventional excipient medium is incompatible with a substance or its derivatives, such as by producing any undesirable biological effect or otherwise interacting in a deleterious manner with any other component(s) of the pharmaceutical composition, its use is contemplated to be within the scope of this disclosure. [0793] In some embodiments, an excipient is approved for use in humans and for veterinary use. In some embodiments, an excipient is approved by the United States Food and Drug Administration. In some embodiments, an excipient is pharmaceutical grade. In some embodiments, an excipient meets the standards of the United States Pharmacopoeia (USP), the European Pharmacopoeia (EP), the British Pharmacopoeia, and/or the International Pharmacopoeia. [0794] Pharmaceutically acceptable excipients used in the manufacture of pharmaceutical compositions include, but are not limited to, inert diluents, dispersing and/or granulating agents, surface active agents and/or emulsifiers, disintegrating agents, binding agents, preservatives, buffering agents, lubricating agents, and/or oils. Such excipients may optionally be included in pharmaceutical formulations. Excipients such as cocoa butter and suppository waxes, coloring agents, coating agents, sweetening, flavoring, and/or perfuming agents can be present in the composition, according to the judgment of the formulator. [0795] General considerations in the formulation and/or manufacture of pharmaceutical agents may be found, for example, in Remington: The Science and Practice of Pharmacy 21st ed., Lippincott Williams & Wilkins, 2005 (incorporated herein by reference). [0796] In some embodiments, pharmaceutical compositions provided herein may be formulated with one or more pharmaceutically acceptable carriers or diluents as well as any other known adjuvants and excipients in accordance with conventional techniques such as those disclosed in Remington: The Science and Practice of Pharmacy 21st ed., Lippincott Williams & Wilkins, 2005 (incorporated herein by reference). [0797] Pharmaceutical compositions described herein can be administered by appropriate methods known in the art. As will be appreciated by a skilled artisan, the route and/or mode of administration may depend on a number of factors, including, e.g., but not limited to stability and/or pharmacokinetics and/or pharmacodynamics of pharmaceutical compositions described herein. [0798] In some embodiments, pharmaceutical compositions described herein are formulated for parenteral administration, which includes modes of administration other than enteral and topical administration, usually by injection, and includes, without limitation, intravenous, intramuscular, intraarterial, intradermal, subcutaneous, subcuticular, or intraarticular injection and infusion. In preferred embodiments, pharmaceutical compositions described herein are formulated for intravenous, intramuscular, or subcutaneous administration. In particularly preferred embodiments, pharmaceutical compositions described herein are formulated for intramuscular administration. [0799] In some embodiments, pharmaceutical compositions described herein are formulated for intravenous administration. In some embodiments, pharmaceutically acceptable excipients that may be useful for intravenous administration include sterile aqueous solutions or dispersions and sterile powders for preparation of sterile injectable solutions or dispersions. [0800] Therapeutic compositions typically must be sterile and stable under the conditions of manufacture and storage. The composition can be formulated as a solution, microemulsion, lipid nanoparticles, or other ordered structure suitable to high drug concentration. The carrier can be a solvent or dispersion medium containing, for example, water, ethanol, polyol (for example, glycerol, propylene glycol, and liquid polyethylene glycol, and the like), and suitable mixtures thereof. Proper fluidity can be maintained, for example, by the use of surfactants. In many cases, it will be preferable to include isotonic agents, for example, sugars, polyalcohols such as mannitol, sorbitol, or sodium chloride in the composition. In some embodiments, prolonged absorption of the injectable compositions can be brought about by including in the composition an agent that delays absorption, for example, monostearate salts and gelatin. [0801] Sterile injectable solutions can be prepared by incorporating the active compound in the required amount in an appropriate solvent with one or a combination of ingredients enumerated above, as required, followed by sterilization and/or microfiltration. In some embodiments, pharmaceutical compositions can be prepared as described herein and/or methods known in the art. In some embodiments, a pharmaceutical composition includes ALC-0315; ALC-0159; DSPC; Cholesterol; Sucrose; NaCl; KCl; Na2HPO4; KH2PO4; Water for injection. In some embodiments, normal saline (isotonic 0.9% NaCl) is used as diluent. [0802] These compositions may also contain adjuvants such as preservatives, wetting agents, emulsifying agents and dispersing agents. Prevention of the presence of microorganisms may be ensured both by sterilization procedures, and by the inclusion of various antibacterial and antifungal agents, for example, paraben, chlorobutanol, phenol sorbic acid, and the like. It may also be desirable to include isotonic agents, such as sugars, sodium chloride, and the like into pharmaceutical compositions described herein. In addition, prolonged absorption of the injectable pharmaceutical form may be brought about by the inclusion of agents which delay absorption such as aluminum monostearate and gelatin. [0803] Formulations of pharmaceutical compositions described herein may be prepared by any method known or hereafter developed in the art of pharmacology. In general, such preparatory methods include the step of bringing active ingredient(s) into association with a diluent or another excipient and/or one or more other accessory ingredients, and then, if necessary and/or desirable, shaping and/or packaging the product into a desired single- or multi-dose unit. [0804] A pharmaceutical composition in accordance with the present disclosure may be prepared, packaged, and/or sold in bulk, as a single unit dose, and/or as a plurality of single unit doses. As used herein, a “unit dose” is discrete amount of the pharmaceutical composition comprising a predetermined amount of at least one RNA product produced using a system and/or method described herein. [0805] Relative amounts of polyribonucleotides encapsulated in lipid nanoparticles, a pharmaceutically acceptable excipient, and/or any additional ingredients in a pharmaceutical composition can vary, depending upon the subject to be treated, target cells, diseases or disorders, and may also further depend upon the route by which the composition is to be administered. [0806] In some embodiments, pharmaceutical compositions described herein are formulated into pharmaceutically acceptable dosage forms by conventional methods known to those of skill in the art. Actual dosage levels of the active ingredients (e.g., polyribonucleotides encapsulated in lipid nanoparticles) in the pharmaceutical compositions described herein may be varied so as to obtain an amount of the active ingredient which is effective to achieve the desired therapeutic response for a particular patient, composition, and mode of administration, without being toxic to the patient. The selected dosage level will depend upon a variety of pharmacokinetic factors including the activity of the particular compositions of the present disclosure employed, the route of administration, the time of administration, the rate of excretion of the particular compound being employed, the duration of the treatment, other drugs, compounds and/or materials used in combination with the particular compositions employed, the age, sex, weight, condition, general health and prior medical history of the patient being treated, and like factors well known in the medical arts. [0807] A physician having ordinary skill in the art can readily determine and prescribe the effective amount of the pharmaceutical composition required. For example, a physician could start doses of active ingredients (e.g., polyribonucleotides encapsulated in lipid nanoparticles) employed in the pharmaceutical composition at levels lower than that required in order to achieve the desired therapeutic effect and gradually increase the dosage until the desired effect is achieved. [0808] In some embodiments, a pharmaceutical composition is formulated (e.g., but not limited to, for intravenous, intramuscular, or subcutaneous administration) to deliver a dose of about 5 mg RNA/kg. [0809] In some embodiments, a pharmaceutical composition described herein may further comprise one or more additives, for example, in some embodiments that may enhance stability of such a composition under certain conditions. Examples of additives may include but are not limited to salts, buffer substances, preservatives, and carriers. For example, in some embodiments, a pharmaceutical composition may further comprise a cryoprotectant (e.g., sucrose) and/or an aqueous buffered solution, which may in some embodiments include one or more salts, including, e.g., alkali metal salts or alkaline earth metal salts such as, e.g., sodium salts, potassium salts, and/or calcium salts. [0810] In some embodiments, a pharmaceutical composition provided herein is a preservative-free, sterile RNA-lipid nanoparticle dispersion in an aqueous buffer for intravenous or intramuscular administration. [0811] Although the descriptions of pharmaceutical compositions provided herein are principally directed to pharmaceutical compositions that are suitable for administration to humans, it will be understood by the skilled artisan that such compositions are generally suitable for administration to animals of all sorts. Modification of pharmaceutical compositions suitable for administration to humans in order to render the compositions suitable for administration to various animals is well understood, and the ordinarily skilled veterinary pharmacologist can design and/or perform such modification with merely ordinary, if any, experimentation. [0812] In some embodiments, two or more polyribonucleotides as described herein may be present in a pharmaceutical composition in equal amounts. For example, if a pharmaceutical composition comprises two polyribonucleotides, the two polyribonucleotides can be present in the pharmaceutical composition at a 1:1 ratio. Additionally, if a pharmaceutical composition comprises three polyribonucleotides, the three polyribonucleotides can be present in the pharmaceutical composition at a 1:1:1 ratio. [0813] In some embodiments, two or more polyribonucleotides as described herein may be present in a pharmaceutical composition in different amounts. For example, if a pharmaceutical composition comprises three polyribonucleotides, the three polyribonucleotides can be present in the pharmaceutical composition at a 1:1:1 ratio. Additionally, if a pharmaceutical composition comprises three polyribonucleotides, the three polyribonucleotides can be present in the pharmaceutical composition at a 1:0.5:0.5 ratio. [0814] In some embodiments, a pharmaceutical composition provided herein comprises (i) a first polyribonucleotide that encodes a first polypeptide and (ii) a second polyribonucleotide that encodes a second polypeptide. [0815] In some embodiments, the first polypeptide comprises an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identity to the amino acid sequence according to SEQ ID NO: 203. In some embodiments, the second polypeptide comprises an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identity to the amino acid sequence according to SEQ ID NO: 33. In some embodiments, the first polyribonucleotide and the second polyribonucleotide are present at a ratio of 1:1. In some embodiments, the first polyribonucleotide and the second polyribonucleotide are present at a ratio of 0.5:1, respectively. [0816] In some embodiments, the first polypeptide comprises an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identity to the amino acid sequence according to SEQ ID NO: 203. In some embodiments, the second polypeptide comprises an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identity to the amino acid sequence according to SEQ ID NO: 81. In some embodiments, the first polyribonucleotide and the second polyribonucleotide are present at a ratio of 1:1. In some embodiments, the first polyribonucleotide and the second polyribonucleotide are present at a ratio of 0.5:1, respectively. [0817] In some embodiments, the first polypeptide comprises an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identity to the amino acid sequence according to SEQ ID NO: 209. In some embodiments, the second polypeptide comprises an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identity to the amino acid sequence according to SEQ ID NO: 33. In some embodiments, the first polyribonucleotide and the second polyribonucleotide are present at a ratio of 1:1. In some embodiments, the first polyribonucleotide and the second polyribonucleotide are present at a ratio of 0.5:1, respectively. [0818] In some embodiments, the first polypeptide comprises an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identity to the amino acid sequence according to SEQ ID NO: 209. In some embodiments, the second polypeptide comprises an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identity to the amino acid sequence according to SEQ ID NO: 81. In some embodiments, the first polyribonucleotide and the second polyribonucleotide are present at a ratio of 1:1. In some embodiments, the first polyribonucleotide and the second polyribonucleotide are present at a ratio of 0.5:1, respectively. [0819] In some embodiments, the first polypeptide comprises an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identity to the amino acid sequence according to SEQ ID NO: 203. In some embodiments, the second polypeptide comprises an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identity to the amino acid sequence according to SEQ ID NO: 209. In some embodiments, the first polyribonucleotide and the second polyribonucleotide are present at a ratio of 1:1. [0820] In some embodiments, a pharmaceutical composition provided herein comprises (i) a first polyribonucleotide that encodes a first polypeptide, (ii) a second polyribonucleotide that encodes a second polypeptide, and (iii) a third polyribonucleotide that encodes a third polypeptide. [0821] In some embodiments, the first polypeptide comprises an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identity to the amino acid sequence according to SEQ ID NO: 203. In some embodiments, the second polypeptide comprises an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identity to the amino acid sequence according to SEQ ID NO: 33. In some embodiments, the third polypeptide comprises an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identity to the amino acid sequence according to SEQ ID NO: 209. In some embodiments, the first polyribonucleotide, the second polyribonucleotide, and the third polyribonucleotide are present at a ratio of 1:1:1, respectively. In some embodiments, the first polyribonucleotide, the second polyribonucleotide, and the third polyribonucleotide are present at a ratio of 0.5:1:0.5, respectively. [0822] In some embodiments, the first polypeptide comprises an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identity to the amino acid sequence according to SEQ ID NO: 203. In some embodiments, the second polypeptide comprises an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identity to the amino acid sequence according to SEQ ID NO: 81. In some embodiments, the third polypeptide comprises an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identity to the amino acid sequence according to SEQ ID NO: 209. In some embodiments, the first polyribonucleotide, the second polyribonucleotide, and the third polyribonucleotide are present at a ratio of 1:1:1, respectively. In some embodiments, the first polyribonucleotide, the second polyribonucleotide, and the third polyribonucleotide are present at a ratio of 0.5:1:0.5, respectively. [0823] In some embodiments, the present disclosure provides a method comprising preparing a pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine). In some embodiments, a pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) comprising a combination disclosed herein. In some embodiments, a method of preparing a combination pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) comprises obtaining a first amount of a first pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) in a first container (e.g., syringe). In some embodiments, a method of preparing a combination pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) comprises obtaining a second amount of a second pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) in a second container (e.g., syringe). In some embodiments, a method of preparing a combination pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) comprises obtaining a third amount of a third pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) in a third container (e.g., syringe). In some embodiments, a method of preparing a combination pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) comprises connecting the first container (e.g., syringe), the second container (e.g., syringe), and/or the third container (e.g., syringe) using an adapter. In some embodiments, a method of preparing a combination pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) comprises transferring a first pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) to a second syringe (e.g., syringe) and optionally discarding the first syringe. In some embodiments, a method of preparing a combination pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) comprises transferring a first pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) and a second pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) to a third syringe (e.g., syringe) and optionally discarding the first syringe and the second syringe. [0824] In some embodiments, a method of preparing a combination pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) comprises: (i) obtaining a first amount of a first pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) in a first container (e.g., syringe); (ii) obtaining a second amount of a second pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) in a second container (e.g., syringe); (iii) obtaining a third amount of a third pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) in a third container (e.g., syringe) (iii) connecting the first container (e.g., syringe) and the second container (e.g., syringe) using an adapter; (iv) transferring a first pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) to a second container (e.g., syringe); (v) transferring a first pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) and second pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) to a third container (e.g., syringe); and (v) discarding the first syringe and second syringe. [0825] In some embodiments, a first pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine), second pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine), and third pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) are not are not stable when co- formulated (e.g., wherein the immunogenicity of the first pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) and/or the second pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) decreases after mixing and storing at 4°C or room temperature for 1 week or longer, 1 day or longer, or 1 hour or longer as compared to the first pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) and/or the second pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) stored under similar (e.g., the same) conditions). [0826] In some embodiments, a first pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) comprises a first delivery modality, wherein the first delivery modality comprises a lipid nanoparticle (LNP), a lipoplex (LPX), a liposome, and/or an oligosaccharide. In some embodiments, a second pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) comprises a second delivery modality, wherein the second delivery modality comprises a lipid nanoparticle (LNP), a lipoplex (LPX), a liposome, and/or an oligosaccharide. In some embodiments, a third pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) comprises a third delivery modality, wherein the third delivery modality comprises a lipid nanoparticle (LNP), a lipoplex (LPX), a liposome, and/or an oligosaccharide. [0827] In some embodiments, a first pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) comprises a recombinant polypeptide comprising a lipophilic region that interacts with the second and/or third delivery modality. In some embodiments, a second pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) comprises a recombinant polypeptide comprising a lipophilic region that interacts with the first and/or third delivery modality. In some embodiments, a third pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) comprises a recombinant polypeptide comprising a lipophilic region that interacts with the first and/or second delivery modality. [0828] In some embodiments, a first pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) comprises a recombinant polypeptide and a lipid. In some embodiments, a second pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) comprises a recombinant polypeptide and a lipid. In some embodiments, a third pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) comprises a recombinant polypeptide and a lipid. [0829] In some embodiments, a first pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) and a second pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) are mixed prior to transferring a first pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) to a second syringe, by a method comprising repeatedly transferring liquid from a first syringe to a second syringe (e.g., until the first pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) and the second pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) form a substantially homogenous mixture). In some embodiments, a first pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) is transferred to a second syringe by a method comprising compressing the plunger of a first syringe only a single time, so that a first pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) and a second pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) form a substantially heterogenous mixture. In some embodiments, a first pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) / second pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) mixture and a third pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) are mixed prior to transferring the first pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) / second pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) mixture to a third syringe, by a method comprising repeatedly transferring liquid from a second syringe to a third syringe (e.g., until the first pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) / second pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) mixture and the third pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) form a substantially homogenous mixture). In some embodiments, a first pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) / second pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) mixture is transferred to a third syringe by a method comprising compressing the plunger of a second syringe only a single time, so that a first pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) / second pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) mixture and a third pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) form a substantially heterogenous mixture. [0830] In some embodiments, a first pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine), second pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine), and third pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) are combined using a method disclosed herein in an alternate order (e.g., sequentially combined or simultaneously combined). In some embodiments, a first pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) and a second pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) are combined as disclosed herein prior to combination with a third pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine). In some embodiments, a second pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) and a third pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) are combined as disclosed herein prior to combination with a first pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine). In some embodiments, a first pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) and a third pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) are combined as disclosed herein prior to combination with a second pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine). In some embodiments, a first pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine), a second pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine), and a third pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) are combined simultaneously. [0831] In some embodiments, a first pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine), second pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine), and/or third pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) are a nucleic acid pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine). In some embodiments, a nucleic acid pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) is an RNA pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) (e.g., an LNP-formulated polyribonucleotide). [0832] In some embodiments, a needle is attached to each of the first syringe, second syringe, and/or third syringe when obtaining a first pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine), a second pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) and a third pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine), and each of the needles is removed prior to attaching an adapter. [0833] In some embodiments, a first pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine), second pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine), and/or third pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) are combined under conditions such that there is no substantial volume loss of the first pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine), second pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine), or third pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) (e.g., wherein the sum of the first amount of the first pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine), the second amount of the second pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine), and the third amount of the third pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) is approximately the same as the mixture administered to the subject, e.g., wherein the sum of the first amount of the first pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine), the second amount of the second pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine), and the third amount of the third pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) is within at least about 5%, at least about 4%, at least about 3%, at least about 2% or at least about 1% of the amount administered to the subject). [0834] In some embodiments, a first pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine), second pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine), and/or third pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) are combined in a pharmacy. In some embodiments, a first pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine), second pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine), and/or third pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) are combined in a hospital. [0835] In some embodiments, a mixture of a first pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine), second pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine), and third pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) is administered to a subject shortly after producing the mixture (e.g., within about 1 hour, within about 30 min, within about 15 min, within about 10 min, or within about 5 min, or within about 1 min of producing the mixture). [0836] In some embodiments, a first pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine), second pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine), and third pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) are obtained from a multidose vial. [0837] In some embodiments, a first amount of a first pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine), a second amount of a second pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine), and a third amount of a third pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) each correspond to an amount that has been shown to provide a clinical benefit and/or prophylaxis in subjects when administered alone (e.g., shown in clinical trials to provide a clinical benefit or prophylaxis), and/or (ii) a first amount of a first pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine), second amount of a second pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine), and third amount of a third pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) each correspond to a dose that has been approved for sale by a government regulatory authority (e.g., the US FDA or the EMA). [0838] In some embodiments, a first pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) is a Plasmodium pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine). In some embodiments, a second pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) is a Plasmodium pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine). In some embodiments, a third pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) is a Plasmodium pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine). In some embodiments, a first pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) and second pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) are Plasmodium pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine). In some embodiments, a first pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) and third pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) are Plasmodium pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine)s. In some embodiments, a second pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) and third pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) are Plasmodium pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine)s. In some embodiments, a first pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine), second pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine), and third pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) are Plasmodium pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine). [0839] In some embodiments, a Plasmodium pharmaceutical composition is a pharmaceutical composition that comprises one or more polyribonucleotides encoding a Plasmodium construct described herein. In some embodiments, a first Plasmodium pharmaceutical composition comprises a polyribonucleotide encoding a Plasmodium T-cell string polypeptide construct described herein. In some embodiments, a second Plasmodium pharmaceutical composition comprises a polyribonucleotide encoding a Plasmodium CSP polypeptide construct described herein. [0840] In some embodiments, a third Plasmodium pharmaceutical composition comprises a polyribonucleotide encoding a Plasmodium T-cell string polypeptide construct described herein. [0841] In some embodiments, a first Plasmodium pharmaceutical composition comprises a polyribonucleotide encoding a Plasmodium T-cell string polypeptide construct having an amino acid sequence that is at least 85% identical to the amino acid sequence according to SEQ ID NO: 203. In some embodiments, a first Plasmodium pharmaceutical composition comprises a polyribonucleotide encoding a Plasmodium T-cell string polypeptide construct having an amino acid sequence that is at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% identical to the amino acid sequence according to SEQ ID NO: 203. In some embodiments, a second Plasmodium pharmaceutical composition comprises a polyribonucleotide encoding a Plasmodium CSP polypeptide construct having an amino acid sequence that is at least 85% identical to the amino acid sequence according to SEQ ID NO: 33. In some embodiments, a second Plasmodium pharmaceutical composition comprises a polyribonucleotide encoding a Plasmodium CSP polypeptide construct having an amino acid sequence that is at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% identical to the amino acid sequence according to SEQ ID NO: 33. In some embodiments, a third Plasmodium pharmaceutical composition comprises a polyribonucleotide encoding a Plasmodium T-cell string polypeptide construct having an amino acid sequence that is at least 85% identical to the amino acid sequence according to SEQ ID NO: 209. In some embodiments, a third Plasmodium pharmaceutical composition comprises a polyribonucleotide encoding a Plasmodium T-cell string polypeptide construct having an amino acid sequence that is at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% identical to the amino acid sequence according to SEQ ID NO: 209. [0842] In some embodiments, at least one (e.g., all) of a first syringe, a second syringe, and a third syringe, is not a uni-directional syringe (e.g., at least one of the syringes is a bidirectional syringe and/or at least one of the syringes does not have a stopper that prevents motion of the plunger in one direction). [0843] In some embodiments, an adapter is a sterile single-packaged adapter. In some embodiments, an adapter is a Luer-Luer adapter (e.g., a Luer dual female adapter). [0844] In some embodiments, the present disclosure provides a system comprising: (i) a first syringe; (ii) an adapter comprising a first end and a second end, the first end of the adapter coupled to a distal end of the first syringe; (iii) a second syringe coupled at a distal end to the second end of the adapter; and (iv) multiple pharmaceutical compositions (e.g., immunogenic compositions, e.g., vaccines) disposed within the first syringe and/or the second syringe, a first pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) of the multiple pharmaceutical compositions (e.g., immunogenic compositions, e.g., vaccines) being disposed within the first syringe and a second pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) of the multiple pharmaceutical compositions (e.g., immunogenic compositions, e.g., vaccines) being disposed within the second syringe. In some embodiments, a system further comprises a third syringe and an adapter comprising a first end and a second end, the first end of the adapter coupled to a distal end of the second syringe and the second end of the adapter coupled to a distal end of the third syringe, wherein multiple pharmaceutical compositions (e.g., immunogenic compositions, e.g., vaccines) are disposed within the first syringe, second syringe, and/or third syringe, with a first pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) of the multiple pharmaceutical compositions (e.g., immunogenic compositions, e.g., vaccines) being disposed within the first syringe, a second pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) of the multiple pharmaceutical compositions (e.g., immunogenic compositions, e.g., vaccines) being disposed within the second syringe, and a third pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) of the multiple pharmaceutical compositions (e.g., immunogenic compositions, e.g., vaccines) being disposed within the third syringe. [0845] In some embodiments, multiple commingled pharmaceutical compositions (e.g., immunogenic compositions, e.g., vaccines) are disposed within a first syringe, second syringe, and/or third syringe. In some embodiments, commingled pharmaceutical compositions (e.g., immunogenic compositions, e.g., vaccines) comprise a homogenous mixture. [0846] In some embodiments, a first syringe, second syringe, and/or third syringe comprise a needle. In some embodiments, a first syringe, second syringe, and/or third syringe do not comprise a needle. [0847] In some embodiments, the present disclosure provides a method of preparing and/or administering commingled pharmaceutical compositions (e.g., immunogenic compositions, e.g., vaccines), the method comprising: (i) providing a first vial containing a first pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) and a second vial containing a second pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine); (ii) providing an empty syringe comprising a detachable needle assembly; (iii) withdrawing a dosage amount of the first pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) from the first vial using the syringe; (iv) aseptically removing the needle assembly from the syringe; (v) providing an unused needle assembly; (vi) aseptically attaching the unused needle assembly to the syringe; and (vii) slowly withdrawing a dosage amount of the second pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) from the second vial using the syringe, thereby creating a syringe with commingled pharmaceutical compositions (e.g., immunogenic compositions, e.g., vaccines). [0848] In some embodiments, a method of preparing and/or administering commingled pharmaceutical compositions (e.g., immunogenic compositions, e.g., vaccines) further comprises a third vial containing a third pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine). In some embodiments, a method of preparing and/or administering commingled pharmaceutical compositions (e.g., immunogenic compositions, e.g., vaccines) comprises: (i) providing a first vial containing a first pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine), a second vial containing a second pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine), and a third vial containing a third pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine); (ii) providing an empty syringe comprising a detachable needle assembly; (iii) withdrawing a dosage amount of the first pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) from the first vial using the syringe; (iv) aseptically removing the needle assembly from the syringe; (v) providing an unused needle assembly; (vi) aseptically attaching the unused needle assembly to the syringe; (vii) slowly withdrawing a dosage amount of the second pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) from the second vial using the syringe; (viii) aseptically removing the needle assembly from the syringe; (ix) providing an unused needle assembly; and (x) slowly withdrawing a dosage amount of the third pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) from the third vial using the syringe, thereby creating a syringe with commingled pharmaceutical compositions (e.g., immunogenic compositions, e.g., vaccines). [0849] In some embodiments, slowly withdrawing a dosage amount of a second pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) from a second vial comprises slowly withdrawing a dosage amount of the second pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) from the second vial over the course of at least 5 seconds. In some embodiments, slowly withdrawing a dosage amount of a third pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) from a third vial comprises slowly withdrawing a dosage amount of the third pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) from the third vial over the course of at least 5 seconds. [0850] In some embodiments, commingled pharmaceutical compositions (e.g., immunogenic compositions, e.g., vaccines) are administered to a subject. [0851] In some embodiments, a first pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) comprises a polyribonucleotide disclosed herein. In some embodiments, a second pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) comprises a polyribonucleotide disclosed herein. In some embodiments, a third pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) comprises a polyribonucleotide disclosed herein. In some embodiments, a polyribonucleotide encodes a polypeptide that comprises one or more Plasmodium T-cell antigens. In some embodiments, a polyribonucleotide encodes a polypeptide that comprises one or more Plasmodium polypeptides or antigenic portions thereof. In some embodiments, a polyribonucleotide comprises or consists of SEQ ID NO: 204. In some embodiments, a polyribonucleotide comprises or consists of a sequence that is at least 85% identical to SEQ ID NO: 204. In some embodiments, a polyribonucleotide comprises or consists of a sequence that is at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% identical to SEQ ID NO: 204. In some embodiments, a polyribonucleotide comprises or consists of SEQ ID NO: 209. In some embodiments, a polyribonucleotide comprises or consists of a sequence that is at least 85% identical to SEQ ID NO: 209. In some embodiments, a polyribonucleotide comprises or consists of a sequence that is at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% identical to SEQ ID NO: 209. In some embodiments, a polyribonucleotide comprises or consists of SEQ ID NO: 33. In some embodiments, a polyribonucleotide comprises or consists of a sequence that is at least 85% identical to SEQ ID NO: 33. In some embodiments, a polyribonucleotide comprises or consists of a sequence that is at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% identical to SEQ ID NO: 33. [0852] In some embodiments, a first pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) comprises a polyribonucleotide encodes a polypeptide that comprises one or more Plasmodium T-cell antigens. In some embodiments, a first pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) comprises a polyribonucleotide encodes a polypeptide that comprises one or more Plasmodium polypeptides or antigenic portions thereof. In some embodiments, a first pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) comprises a polyribonucleotide that comprises or consists of SEQ ID NO: 204. In some embodiments, a first pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) comprises a polyribonucleotide that comprises or consists of a sequence that is at least 85% identical to SEQ ID NO: 204. In some embodiments, a first pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) comprises a polyribonucleotide that comprises or consists of a sequence that is at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% identical to SEQ ID NO: 204. In some embodiments, a first pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) comprises a polyribonucleotide that encodes a polypeptide that comprises or consists of SEQ ID NO: 203. In some embodiments, a first pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) comprises a polyribonucleotide that comprises or consists of a sequence that is at least 85% identical to SEQ ID NO: 203. In some embodiments, a first pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) comprises a polyribonucleotide that comprises or consists of a sequence that is at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% identical to SEQ ID NO: 203. In some embodiments, a first pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) comprises a polyribonucleotide that comprises or consists of SEQ ID NO: 210. In some embodiments, a first pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) comprises a polyribonucleotide that comprises or consists of a sequence that is at least 85% identical to SEQ ID NO: 210. In some embodiments, a first pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) comprises a polyribonucleotide that comprises or consists of a sequence that is at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% identical to SEQ ID NO: 210. In some embodiments, a first pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) comprises a polyribonucleotide that encodes a polypeptide that comprises or consists of SEQ ID NO: 209. In some embodiments, a first pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) comprises a polyribonucleotide that comprises or consists of a sequence that is at least 85% identical to SEQ ID NO: 209. In some embodiments, a first pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) comprises a polyribonucleotide that comprises or consists of a sequence that is at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% identical to SEQ ID NO: 209. In some embodiments, a first pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) comprises a polyribonucleotide that comprises or consists of SEQ ID NO: 147. In some embodiments, a first pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) comprises a polyribonucleotide that comprises or consists of a sequence that is at least 85% identical to SEQ ID NO: 147. In some embodiments, a first pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) comprises a polyribonucleotide that comprises or consists of a sequence that is at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% identical to SEQ ID NO: 147. In some embodiments, a first pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) comprises a polyribonucleotide that encodes a polypeptide that comprises or consists of SEQ ID NO: 33. In some embodiments, a first pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) comprises a polyribonucleotide that comprises or consists of a sequence that is at least 85% identical to SEQ ID NO: 33. In some embodiments, a first pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) comprises a polyribonucleotide that comprises or consists of a sequence that is at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% identical to SEQ ID NO: 33. [0853] In some embodiments, a second pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) comprises a polyribonucleotide encodes a polypeptide that comprises one or more Plasmodium T-cell antigens. In some embodiments, a second pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) comprises a polyribonucleotide encodes a polypeptide that comprises one or more Plasmodium polypeptides or antigenic portions thereof. In some embodiments, a second pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) comprises a polyribonucleotide that comprises or consists of SEQ ID NO: 204. In some embodiments, a second pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) comprises a polyribonucleotide that comprises or consists of a sequence that is at least 85% identical to SEQ ID NO: 204. In some embodiments, a second pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) comprises a polyribonucleotide that comprises or consists of a sequence that is at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% identical to SEQ ID NO: 204. In some embodiments, a second pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) comprises a polyribonucleotide that encodes a polypeptide that comprises or consists of SEQ ID NO: 203. In some embodiments, a second pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) comprises a polyribonucleotide that comprises or consists of a sequence that is at least 85% identical to SEQ ID NO: 203. In some embodiments, a second pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) comprises a polyribonucleotide that comprises or consists of a sequence that is at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% identical to SEQ ID NO: 203. In some embodiments, a second pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) comprises a polyribonucleotide that comprises or consists of SEQ ID NO: 210. In some embodiments, a second pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) comprises a polyribonucleotide that comprises or consists of a sequence that is at least 85% identical to SEQ ID NO: 210. In some embodiments, a second pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) comprises a polyribonucleotide that comprises or consists of a sequence that is at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% identical to SEQ ID NO: 210. In some embodiments, a second pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) comprises a polyribonucleotide that encodes a polypeptide that comprises or consists of SEQ ID NO: 209. In some embodiments, a second pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) comprises a polyribonucleotide that comprises or consists of a sequence that is at least 85% identical to SEQ ID NO: 209. In some embodiments, a second pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) comprises a polyribonucleotide that comprises or consists of a sequence that is at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% identical to SEQ ID NO: 209. In some embodiments, a second pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) comprises a polyribonucleotide that comprises or consists of SEQ ID NO: 147. In some embodiments, a second pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) comprises a polyribonucleotide that comprises or consists of a sequence that is at least 85% identical to SEQ ID NO: 147. In some embodiments, a second pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) comprises a polyribonucleotide that comprises or consists of a sequence that is at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% identical to SEQ ID NO: 147. In some embodiments, a second pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) comprises a polyribonucleotide that encodes a polypeptide that comprises or consists of SEQ ID NO: 33. In some embodiments, a second pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) comprises a polyribonucleotide that comprises or consists of a sequence that is at least 85% identical to SEQ ID NO: 33. In some embodiments, a second pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) comprises a polyribonucleotide that comprises or consists of a sequence that is at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% identical to SEQ ID NO: 33. [0854] In some embodiments, a third pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) comprises a polyribonucleotide encodes a polypeptide that comprises one or more Plasmodium T-cell antigens. In some embodiments, a third pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) comprises a polyribonucleotide encodes a polypeptide that comprises one or more Plasmodium polypeptides or antigenic portions thereof. In some embodiments, a third pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) comprises a polyribonucleotide that comprises or consists of SEQ ID NO: 204. In some embodiments, a third pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) comprises a polyribonucleotide that comprises or consists of a sequence that is at least 85% identical to SEQ ID NO: 204. In some embodiments, a third pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) comprises a polyribonucleotide that comprises or consists of a sequence that is at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% identical to SEQ ID NO: 204. In some embodiments, a third pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) comprises a polyribonucleotide that encodes a polypeptide that comprises or consists of SEQ ID NO: 203. In some embodiments, a third pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) comprises a polyribonucleotide that comprises or consists of a sequence that is at least 85% identical to SEQ ID NO: 203. In some embodiments, a third pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) comprises a polyribonucleotide that comprises or consists of a sequence that is at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% identical to SEQ ID NO: 203. In some embodiments, a third pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) comprises a polyribonucleotide that comprises or consists of SEQ ID NO: 210. In some embodiments, a third pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) comprises a polyribonucleotide that comprises or consists of a sequence that is at least 85% identical to SEQ ID NO: 210. In some embodiments, a third pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) comprises a polyribonucleotide that comprises or consists of a sequence that is at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% identical to SEQ ID NO: 210. In some embodiments, a third pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) comprises a polyribonucleotide that encodes a polypeptide that comprises or consists of SEQ ID NO: 209. In some embodiments, a third pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) comprises a polyribonucleotide that comprises or consists of a sequence that is at least 85% identical to SEQ ID NO: 209. In some embodiments, a third pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) comprises a polyribonucleotide that comprises or consists of a sequence that is at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% identical to SEQ ID NO: 209. In some embodiments, a third pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) comprises a polyribonucleotide that comprises or consists of SEQ ID NO: 147. In some embodiments, a third pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) comprises a polyribonucleotide that comprises or consists of a sequence that is at least 85% identical to SEQ ID NO: 147. In some embodiments, a third pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) comprises a polyribonucleotide that comprises or consists of a sequence that is at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% identical to SEQ ID NO: 147. In some embodiments, a third pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) comprises a polyribonucleotide that encodes a polypeptide that comprises or consists of SEQ ID NO: 33. In some embodiments, a third pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) comprises a polyribonucleotide that comprises or consists of a sequence that is at least 85% identical to SEQ ID NO: 33. In some embodiments, a third pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) comprises a polyribonucleotide that comprises or consists of a sequence that is at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% identical to SEQ ID NO: 33. V. Patient Populations [0855] In some aspects, technologies of the present disclosure are used for therapeutic and/or prophylactic purposes. In some embodiments, technologies of the present disclosure are used in the treatment and/or prophylactic of an infection with a malaria parasite. Prophylactic purposes of the present disclosure comprise pre- exposure prophylaxis and/or post-exposure prophylaxis. In some such embodiments, a malaria parasite is, for example, Plasmodium falciparum, Plasmodium knowlesi, Plasmodium ovale, Plasmodium simiovale, Plasmodium vivax, Plasmodium malariae, Plasmodium ovale curtisi, Plasmodium ovale wallikeri, and/or Plasmodium berghei. [0856] In some embodiments, technologies of the present disclosure are used in the treatment and/or prophylaxis of a disorder related to such an infection. A disordered related to such an infection comprises, for example, a typical symptom and/or a complication of a malaria infection. [0857] In some embodiments, provided compositions (e.g., that are or comprise Plasmodium antigens) may be useful to detect and/or characterize one or more features of an anti-malaria immune response (e.g., by detecting binding to a provided antigen by serum from an infected subject). [0858] In some embodiments, provided compositions (e.g., that are or comprise Plasmodium antigens) are useful to raise antibodies to one or more epitopes included therein; such antibodies may themselves be useful, for example for detection or treatment of malarial parasite(s) or infection thereby. [0859] The present disclosure provides use of encoding nucleic acids (e.g., DNA or RNA) to produce encoded antigens and/or use of DNA constructs to produce RNA. [0860] In some embodiments, technologies of the present disclosure are utilized in a non-limited subject population; in some embodiments, technologies of the present disclosure are utilized in particular subject populations. [0861] In some embodiments, a subject population comprises an adult population. In some embodiments, an adult population comprises subjects between the ages of about 18 years and about 60 years of age (e.g., about 20, 25, 30, 35, 40, 45, 50, 55, or 60 years of age). In some embodiments, an adult population comprises subjects between the ages of about 19 years and about 60 years of age (e.g., about 20, 25, 30, 35, 40, 45, 50, 55, or 60 years of age). In some embodiments, an adult population comprises subjects between the ages of about 18 years and about 55 years of age (e.g., about 20, 25, 30, 35, 40, 45, 50, 55, or 60 years of age). [0862] In some embodiments, a subject population comprises an elderly population. In some embodiments, an elderly population comprises subjects of about 60 years of age, about 70 years of age, or older (e.g., about 65, 70, 75, 80, 85, 90, 95, or 100 years of age). [0863] In some embodiments, a subject population comprises a pediatric population. In some embodiments, a pediatric population comprises subjects approximately 18 years old or younger. In some such embodiments, a pediatric population comprises subjects between the ages of about 1 year and about 18 years (e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, or 18 years of age). [0864] In some embodiments, a subject population comprises a newborn population. In some embodiments, a newborn population comprises subjects about 12 months or younger (e.g., 12, 11, 10, 9, 8, 7, 6, 5, 4, 3, 2, 1 months or younger). In some embodiments, subject populations to be treated with technologies described herein include infants (e.g., about 12 months or younger) whose mothers did not receive such technologies described herein during pregnancy. In some embodiments, subject populations to be treated with technologies described herein may include pregnant women; in some embodiments, infants whose mothers were treated with disclosed technologies during pregnancy (e.g., who received at least one dose, or alternatively only who received both doses), are not vaccinated during the first weeks, months, or even years (e.g., 1, 2, 3, 4, 5, 6, 7, 8 weeks or more, or 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24 months or more, or 1, 2, 3, 4, 5 years or more) post-birth. Alternatively or additionally, in some embodiments, infants whose mothers were treated with disclosed technologies during pregnancy (e.g., who received at least one dose, or alternatively only who received both doses), receive reduced treated with disclosed technologies (e.g., lower doses and/or smaller numbers of administrations – e.g., boosters – and/or lower total exposure over a given period of time) after birth, for example during the first weeks, months, or even years (e.g., 1, 2, 3, 4, 5, 6, 7, 8 weeks or more, or 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24 months or more, or 1, 2, 3, 4, 5 years or more) post-birth or may need reduced vaccination (e.g., lower doses and/or smaller numbers of administrations – e.g., boosters – over a given period of time), In some embodiments, compositions as provided herein are administered to subject populations that do not include pregnant women. [0865] In some embodiments, a subject population is or comprises children aged 6 weeks to up to 17 months of age. [0866] In some embodiments, a subject has a body mass index over 15 kg/m² and under 40 kg/m². In some embodiments, a subject has a body mass index over 18.5 kg/m² and under 35 kg/m. In some embodiments, a subject’s body mass index is determined at an initial visit with a health professional. In some embodiments, a subject’s body mass index is determined when a first dose of a pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) as described herein is administered. [0867] In some embodiments, a subject weighs at least 40 kg. In some embodiments, a subject weighs at least 45 kg. In some embodiments, a subject’s weight is determined at an initial visit with a health professional. In some embodiments, a subject’s weight is determined when a first dose of a pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) as described herein is administered. [0868] In some embodiments, a subject has a body mass index over 15 kg/m² and under 40 kg/m² and weighs at least 40kg. In some embodiments, a subject has a body mass index over 18.5 kg/m² and under 35 kg/m² and weighs at least 45kg. In some embodiments, a subject’s body mass index and weight are determined at an initial visit with a health professional. In some embodiments, a subject’s body mass index and weight are determined when a first dose of a pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) as described herein is administered. [0869] In some embodiments, a subject population comprises a population with a high risk of infection (e.g., Malaria). In some such embodiments, a population may be deemed to have a high risk of infection due to a local epidemic or a global pandemic. In some such embodiments, a population may be deemed to have a high risk of infection due to a subject population’s geographic area. In some embodiments, a subject population comprises subjects that have been exposed to infection (e.g., Malaria). In some embodiments, a subject is malaria naïve, e.g., has not experienced a prior malarial infection. In some embodiments, a subject previously has been exposed to malaria (e.g., Plasmodium falciparum). Previous exposure to malaria does not encompass a prior vaccination with a malarial parasite or a component thereof. In some embodiments, a subject previously has been infected with malaria (e.g., Plasmodium falciparum). [0870] In some embodiments, a subject is malaria naïve, e.g., has not experienced a prior malarial infection. In some embodiments, a subject previously has been exposed to malaria (e.g., Plasmodium falciparum). Previous exposure to malaria does not encompass a prior vaccination with a malarial parasite or a component thereof. In some embodiments, a subject previously has been infected with malaria (e.g., Plasmodium falciparum). [0871] In some embodiments, a subject has not traveled to a malaria-endemic region within the 3 months, 4 months, 5 months, 6 months or 1 year prior to receiving a first dose of a polyribonucleotide, RNA construct, or composition (e.g., pharmaceutical composition) described herein. In some embodiments, a subject has traveled to a malaria-endemic region within the 3 months, 4 months, 5 months, 6 months or 1 year prior to receiving a first dose. In some embodiments, a subject intends to travel to a malaria-endemic region within 3 months, 4 months, 5 months, 6 months or 1 year after receiving a first dose. In some embodiments, a subject resides in a malaria-endemic region. A malaria-endemic region is defined by the Center for Disease Control and Prevention. In some embodiments, a malaria-endemic region is defined by the Center for Disease Control and Prevention at www.cdc.gov/malaria/travelers/country_table/a.html, as of July 24, 2023. In some embodiments, a malaria-endemic region includes all or a portion of Afghanistan, Angola, Bangaladesh, Bhutan, Bolivia, Botswana, Brazil, Burma, Cameroon, Cambodia, Central African Republic, Chad, Colombia, Comoros, Congo, Costa Rica, Cote d’Ivoire, Democratic Republic of the Congo, Djibouti, Dominican Republic, Ecuador, Equatorial Guinea, Eritrea, Eswatini, Ethopia, French Guiana, Gabon, Gambia, Ghana, Guatemala, Guinea, Guinea-Bissau, Guyana, Haiti, Honduras, India, Indonesia, Kenya, Laos, Liberia, Madagascar, Malawi, Mali, Mauritania, Mexico, Mozambique, Namibia, Nepal, Nicaragua, Niger, Nigeria, North Korea, Pakistan, Panama, Papua New Guinea, Peru, Philippines, Rwanda, São Tomé and Príncipe, Saudia Arabia, Senegal, Sierra Leone, Solomon Islands, Somalia, South Africa, South Korea, South Sudan, Sudan, Suriname, Tanzania, Thailand, Togo, Uganda, Vanuatu, Venezuela, Vietnam, Yemen, Zambia, and Zimbabwe. [0872] In some embodiments, where a subject population is or includes pregnant women, provided technologies offer a particular advantage of interrupting malaria’s transmission cycle, including, for example, in some embodiments, by reducing or eliminating transmission from pregnant mothers to their fetuses. [0873] In some embodiments, a subject population is or comprises immunocompromised individuals. In some embodiments, a subject population does not include immunocompromised individuals. [0874] In some embodiments, a provided pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) may be administered in combination with (i.e., so that subject(s) are simultaneously exposed to both) another pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) or therapeutic intervention, e.g., to treat or prevent malaria or another disease, disorder, or condition. [0875] In some embodiments, a provided pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) may be administered with a protein vaccine, a DNA vaccine, an RNA vaccine, a cellular vaccine, a conjugate vaccine, etc. In some embodiments, one or more doses of a provided pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) may be administered together with (e.g., in a single visit) another vaccine or other therapy. [0876] In some embodiments, a provided pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) may be administered to subjects who have been exposed, or expect they have been exposed, to malaria. In some embodiments, a provided pharmaceutical composition (e.g., immunogenic composition, e.g., vaccine) may be administered to subjects who do not have symptoms of malarial infection. VI. Treatment Methods [0877] In some embodiments, technologies of the present disclosure may be administered to subjects according to a particular dosing regimen. In some embodiments, a dosing regimen may involve a single administration; in some embodiments, a dosing regimen may comprise one or more “booster” administrations after the initial administration. In some embodiments, initial and boost doses are the same amount; in some embodiments they differ. In some embodiments, two or more booster doses are administered. In some embodiments, a plurality of doses are administered at regular intervals. In some embodiments, periods of time between doses become longer. In some embodiments, one or more subsequent doses is administered if a particular clinical (e.g., reduction in neutralizing antibody levels) or situational (e.g., local development of a new strain) even arises or is detected. [0878] In some embodiments, administered pharmaceutical compositions (e.g., immunogenic compositions, e.g., vaccines) comprising RNA constructs that encode Plasmodium polypeptide constructs are administered in RNA doses of from about 0.1 μg to about 300 μg, about 0.5 μg to about 200 μg, or about 1 μg to about 100 μg, such as about 1 μg, about 3 μg, about 10 μg, about 30 μg, about 50 μg, about 70 μg, or about 100 μg. In some embodiments, administered pharmaceutical compositions (e.g., immunogenic compositions, e.g., vaccines) comprising RNA constructs that encode Plasmodium polypeptide constructs are administered in RNA doses of 10 μg or less, 30 μg or less, 50 μg or less, 70 μg or less, or 100 μg or less. In some embodiments, an saRNA construct is administered at a lower dose (e.g., 2, 4, 5, 10-fold or more lower) than a modRNA or uRNA construct. [0879] In some embodiments, a first booster dose is administered within a about six months of the initial dose, and preferably within about 5, 4, 3, 2, or 1 months. In some embodiments, a first booster dose is administered in a time period that begins about 1, 2, 3, or 4 weeks after the first dose, and ends about 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12 weeks of the first dose (e.g., between about 1 and about 12 weeks after the first dose, or between about 2 or 3 weeks and about 5 and 6 weeks after the first dose, or about 3 weeks or about 4 weeks after the first dose). [0880] In some embodiments, a plurality of booster doses (e.g., 2, 3, or 4) doses are administered within 6 months of the first dose, or within 12 months of the first dose. [0881] In some embodiments, a first dose and a second dose are administered about 6, about 7, about 8, about 9, or about 10 weeks apart. In other words, in some embodiments, a second dose is administered about 6, about 7, about 8, about 9, or about 10 weeks after a first dose. [0882] In some embodiments, a third dose is administered about 15, about 16, about 17, about 18, about 19, or about 20 weeks after a second dose. [0883] In some embodiments, a second dose is administered about 8 weeks after a first dose, and a third dose is administered about 18 weeks after the second dose. [0884] In some embodiments, 3 doses or fewer are required to achieve effective vaccination (e.g., greater than 60%, and in some embodiments greater than about 70%, about 75%, about 80%, about 85%, about 90% or more) reduction in risk of infection, or of serious disease. In some embodiments, not more than two doses are required. In some embodiments, a single dose is sufficient. In some embodiments, an RNA dose is about 60 μg or lower, 50 μg or lower, 40 μg or lower, 30 μg or lower, 20 μg or lower, 10 μg or lower, 5 μg or lower, 2.5 μg or lower, or 1 μg or lower. In some embodiments, an RNA dose is about 0.25 μg, at least 0.5 μg, at least 1 μg, at least 2 μg, at least 3 μg, at least 4 μg, at least 5 μg, at least 10 μg, at least 20 μg, at least 30 μg, or at least 40 μg. In some embodiments, an RNA dose is about 0.25 μg to 60 μg, 0.5 μg to 55 μg, 1 μg to 50 μg, 5 μg to 40 μg, or 10 μg to 30 μg may be administered per dose. In some embodiments, an RNA dose is about 30 μg. In some embodiments, at least two such doses are administered. For example, a second dose may be administered about 21 days following administration of the first dose. In some embodiments, a first booster dose is administered about one month after an initial dose. In some such embodiments, at least one further booster is administered at one-month interval(s). In some embodiments, after 2 or 3 boosters, a longer interval is introduced and no further booster is administered for at least 6, 9, 12, 18, 24, or more months. In some embodiments, a single further booster is administered after about 18 months. In some embodiments, no further booster is required unless, for example, a material change in clinical or environmental situation is observed. [0885] In some embodiments, one or more outcomes may be assessed following administration of one or more doses of a pharmaceutical composition provided herein. Exemplary outcomes include, but are not limited to: local reaction at the injection site (e.g., pain, erythema/redness, induration/swelling, etc.), frequency of solicited local reactions at the injection site (e.g., pain, erythema/redness, induration/swelling, etc.), systemic reactions (e.g., vomiting, diarrhea, headache, fatigue, muscle/joint pain, fever, etc.), frequency of solicited systemic reactions (e.g., vomiting, diarrhea, headache, fatigue, muscle/joint pain, fever, etc.), adverse events, medically attended adverse events, severe adverse events, frequency of subjects with at least one adverse event, frequency of subjects with at least one medically attended adverse events, frequency of subjects with at least one severe adverse events, number of subjects protected from blood stage parasitemia, proportion of subjects protected from blood stage parasitemia, and combinations thereof. [0886] In some embodiments, blood stage parasitemia can be assessed by PCR, e.g., qPCR. [0887] In some embodiments, statistics on antibody levels at assessed time points can be obtained following administration of one or more doses of a pharmaceutical composition provided herein. Time points can include at the time of a first dose, the time of a second dose, the time of a third dose, following a known or suspected malaria exposure, or following a known or suspected malaria infection. VII. Methods of Manufacture [0888] Individual polyribonucleotides can be produced by methods known in the art. For example, in some embodiments, polyribonucleotides can be produced by in vitro transcription, for example, using a DNA template. A plasmid DNA used as a template for in vitro transcription to generate a polyribonucleotide described herein is also within the scope of the present disclosure. [0889] A DNA template is used for in vitro RNA synthesis in the presence of an appropriate RNA polymerase (e.g., a recombinant RNA-polymerase such as a T7 RNA-polymerase) with ribonucleotide triphosphates (e.g., ATP, CTP, GTP, UTP). In some embodiments, polyribonucleotides (e.g., ones described herein) can be synthesized in the presence of modified ribonucleotide triphosphates. By way of example only, in some embodiments, pseudouridine (ψ), N1-methyl-pseudouridine (m1ψ), or 5-methyl-uridine (m5U) can be used to replace uridine triphosphate (UTP). In some embodiments, pseudouridine (ψ) can be used to replace uridine triphosphate (UTP). In some embodiments, N1-methyl-pseudouridine (m1ψ) can be used to replace uridine triphosphate (UTP). In some embodiments, 5-methyl- uridine (m5U) can be used to replace uridine triphosphate (UTP). [0890] As will be clear to those skilled in the art, during in vitro transcription, an RNA polymerase (e.g., as described and/or utilized herein) typically traverses at least a portion of a single-stranded DNA template in the 3'→ 5' direction to produce a single-stranded complementary RNA in the 5'→ 3' direction. [0891] In some embodiments where a polyribonucleotide comprises a polyA tail, one of those skill in the art will appreciate that such a polyA tail may be encoded in a DNA template, e.g., by using an appropriately tailed PCR primer, or it can be added to a polyribonucleotide after in vitro transcription, e.g., by enzymatic treatment (e.g., using a poly(A) polymerase such as an E. coli Poly(A) polymerase). Suitable poly(A) tails are described herein above. For example, in some embodiments, a poly(A) tail comprises a nucleotide sequence of A AAAAAAAAAAAAAAAAAAAAAAAA (SEQ ID NO: 568). In some embodiments, a poly(A) tail comprises a plurality of A residues interrupted by a linker. In some embodiments, a linker comprises the nucleotide sequence GCATATGAC (SEQ ID NO: 413). [0892] In some embodiments, those skilled in the art will appreciate that addition of a 5' cap to an RNA (e.g., mRNA) can facilitate recognition and attachment of the RNA to a ribosome to initiate translation and enhances translation efficiency. Those skilled in the art will also appreciate that a 5' cap can also protect an RNA product from 5' exonuclease mediated degradation and thus increases half-life. Methods for capping are known in the art; one of ordinary skill in the art will appreciate that in some embodiments, capping may be performed after in vitro transcription in the presence of a capping system (e.g., an enzyme-based capping system such as, e.g., capping enzymes of vaccinia virus). In some embodiments, a cap may be introduced during in vitro transcription, along with a plurality of ribonucleotide triphosphates such that a cap is incorporated into a polyribonucleotide during transcription (also known as co-transcriptional capping). In some embodiments, a GTP fed-batch procedure with multiple additions in the course of the reaction may be used to maintain a low concentration of GTP in order to effectively cap the RNA. Suitable 5' cap are described herein above. For example, in some embodiments, a 5' cap comprises m7(3'OMeG)(5')ppp(5')(2'OMeA)pG. [0893] Following RNA transcription, a DNA template is digested. In some embodiments, digestion can be achieved with the use of DNase I under appropriate conditions. [0894] In some embodiments, in-vitro transcribed polyribonucleotides may be provided in a buffered solution, for example, in a buffer such as HEPES, a phosphate buffer solution, a citrate buffer solution, an acetate buffer solution; in some embodiments, such solution may be buffered to a pH within a range of, for example, about 6.5 to about 7.5; in some embodiments approximately 7.0. In some embodiments, production of polyribonucleotides may further include one or more of the following steps: purification, mixing, filtration, and/or filling. [0895] In some embodiments, polyribonucleotides can be purified (e.g., in some embodiments after in vitro transcription reaction), for example, to remove components utilized or formed in the course of the production, like, e.g., proteins, DNA fragments, and/or or nucleotides. Various nucleic acid purifications that are known in the art can be used in accordance with the present disclosure. Certain purification steps may be or include, for example, one or more of precipitation, column chromatography (including, e.g., but not limited to anionic, cationic, hydrophobic interaction chromatography (HIC)), solid substrate-based purification (e.g., magnetic bead-based purification). In some embodiments, polyribonucleotides may be purified using magnetic bead-based purification, which in some embodiments may be or comprise magnetic bead-based chromatography. In some embodiments, polyribonucleotides may be purified using hydrophobic interaction chromatography (HIC) and/or diafiltration. In some embodiments, polyribonucleotides may be purified using HIC followed by diafiltration. [0896] In some embodiments, dsRNA may be obtained as side product during in vitro transcription. In some such embodiments, a second purification step may be performed to remove dsRNA contamination. For example, in some embodiments, cellulose materials (e.g., microcrystalline cellulose) may be used to remove dsRNA contamination, for examples in some embodiments in a chromatographic format. In some embodiments, cellulose materials (e.g., microcrystalline cellulose) can be pretreated to inactivate potential RNase contamination, for example in some embodiments by autoclaving followed by incubation with aqueous basic solution, e.g., NaOH. In some embodiments, cellulose materials may be used to purify polyribonucleotides according to methods described in WO 2017/182524, the entire content of which is incorporated herein by reference. [0897] In some embodiments, a batch of polyribonucleotides may be further processed by one or more steps of filtration and/or concentration. For example, in some embodiments, polyribonucleotide(s), for example, after removal of dsRNA contamination, may be further subject to diafiltration (e.g., in some embodiments by tangential flow filtration), for example, to adjust the concentration of polyribonucleotides to a desirable RNA concentration and/or to exchange buffer to a drug substance buffer. [0898] In some embodiments, polyribonucleotides may be processed through 0.2 μm filtration before they are filled into appropriate containers. [0899] In some embodiments, polyribonucleotides and compositions thereof may be manufactured in accordance with a process as described herein, or as otherwise known in the art. [0900] In some embodiments, polyribonucleotides and compositions thereof may be manufactured at a large scale. For example, in some embodiments, a batch of polyribonucleotides can be manufactured at a scale of greater than 1 g, greater than 2 g, greater than 3 g, greater than 4 g, greater than 5 g, greater than 6 g, greater than 7 g, greater than 8 g, greater than 9 g, greater than 10 g, greater than 15 g, greater than 20 g, or higher. [0901] In some embodiments, RNA quality control may be performed and/or monitored at any time during production process of polyribonucleotides and/or compositions comprising the same. For example, in some embodiments, RNA quality control parameters, including one or more of RNA identity (e.g., sequence, length, and/or RNA natures), RNA integrity, RNA concentration, residual DNA template, and residual dsRNA, may be assessed and/or monitored after each or certain steps of a polyribonucleotide manufacturing process, e.g., after in vitro transcription, and/or each purification step. [0902] In some embodiments, the stability of polyribonucleotides (e.g., produced by in vitro transcription) and/or compositions comprising polyribonucleotides can be assessed under various test storage conditions, for example, at room temperatures vs. fridge or sub-zero temperatures over a period of time (e.g., at least 3 months, at least 6 months, at least 9 months, at least 12 months, or longer). In some embodiments, polyribonucleotides (e.g., ones described herein) and/or compositions thereof may be stored stable at a fridge temperature (e.g., about 4 C to about 10 C) for at least 1 month or longer including, at least 2 months, at least 3 months, at least 4 months, at least 5 months, at least 6 months, at least 7 months, at least 8 months, at least 9 months, at least 10 months, at least 11 months, or at least 12 months or longer. In some embodiments, polyribonucleotides (e.g., ones described herein) and/or compositions thereof may be stored stable at a sub-zero temperature (e.g., -20 C or below) for at least 1 month or longer including, at least 2 months, at least 3 months, at least 4 months, at least 5 months, at least 6 months, at least 7 months, at least 8 months, at least 9 months, at least 10 months, at least 11 months, or at least 12 months or longer. In some embodiments, polyribonucleotides (e.g., ones described herein) and/or compositions thereof may be stored stable at room temperature (e.g., at about 25°C) for at least 1 month or longer. [0903] In some embodiments, one or more assessments may be utilized during manufacture, or other preparation or use of polyribonucleotides (e.g., as a release test). [0904] In some embodiments, one or more quality control parameters may be assessed to determine whether polyribonucleotides described herein meet or exceed acceptance criteria (e.g., for subsequent formulation and/or release for distribution). In some embodiments, such quality control parameters may include, but are not limited to RNA integrity, RNA concentration, residual DNA template and/or residual dsRNA. Certain methods for assessing RNA quality are known in the art; for example, one of skill in the art will recognize that in some embodiments, one or more analytical tests can be used for RNA quality assessment. Examples of such certain analytical tests may include but are not limited to gel electrophoresis, UV absorption, and/or PCR assay. [0905] In some embodiments, a batch of polyribonucleotides may be assessed for one or more features as described herein to determine next action step(s). For example, a batch of polyribonucleotides can be designated for one or more further steps of manufacturing and/or formulation and/or distribution if RNA quality assessment indicates that such a batch of polyribonucleotides meet or exceed the relevant acceptance criteria. Otherwise, an alternative action can be taken (e.g., discarding the batch) if such a batch of polyribonucleotides does not meet or exceed the acceptance criteria. [0906] In some embodiments, a batch of polyribonucleotides that satisfy assessment results can be utilized for one or more further steps of manufacturing and/or formulation and/or distribution. VIII. DNA Constructs [0907] Among other things, the present disclosure provides DNA constructs, for example that may encode one or more antibody agents as described herein, or components thereof. In some embodiments, DNA constructs provided by and/or utilized in accordance with the present disclosure are comprised in a vector. [0908] Non-limiting examples of a vector include plasmid vectors, cosmid vectors, phage vectors such as lambda phage, viral vectors such as retroviral, adenoviral or baculoviral vectors, or artificial chromosome vectors such as bacterial artificial chromosomes (BAC), yeast artificial chromosomes (YAC), or P1 artificial chromosomes (PAC). In some embodiments, a vector is an expression vector. In some embodiments, a vector is a cloning vector. In general, a vector is a nucleic acid construct that can receive or otherwise become linked to a nucleic acid element of interest (e.g., a construct that is or encodes a payload, or that imparts a particular functionality, etc.). [0909] Expression vectors, which may be plasmid or viral or other vectors, typically include an expressible sequence of interest (e.g., a coding sequence) that is functionally linked with one or more control elements (e.g., promoters, enhancers, transcription terminators, etc.). Typically, such control elements are selected for expression in a system of interest. In some embodiments, a system is ex vivo (e.g., an in vitro transcription system); in some embodiments, a system is in vivo (e.g., a bacterial, yeast, plant, insect, fish, vertebrate, mammalian cell or tissue, etc.). [0910] Cloning vectors are generally used to modify, engineer, and/or duplicate (e.g., by replication in vivo, for example in a simple system such as bacteria or yeast, or in vitro, such as by amplification such as polymerase chain reaction or other amplification process). In some embodiments, a cloning vector may lack expression signals. [0911] In many embodiments, a vector may include replication elements such as primer binding site(s) and/or origin(s) of replication. In many embodiments, a vector may include insertion or modification sites such as restriction endonuclease recognition sites and/or guide RNA binding sites, etc. [0912] In some embodiments, a vector is a viral vector (e.g., an AAV vector). In some embodiments, a vector is a non-viral vector. In some embodiments, a vector is a plasmid. [0913] Those skilled in the art are aware of a variety of technologies useful for the production of recombinant polynucleotides (e.g., DNA or RNA) as described herein. For example, restriction digestion, reverse transcription, amplification (e.g., by polymerase chain reaction), Gibson assembly, etc., are well established and useful tools and technologies. Alternatively or additionally, certain nucleic acids may be prepared or assembled by chemical and/or enzymatic synthesis. In some embodiments, a combination of known methods is utilized to prepare a recombinant polynucleotide. [0914] In some embodiments, polynucleotide(s) of the present disclosure are included in a DNA construct (e.g., a vector) amenable to transcription and/or translation. [0915] In some embodiments, an expression vector comprises a polynucleotide that encodes proteins and/or polypeptide of the present disclosure operatively linked to a sequence or sequences that control expression (e.g., promoters, start signals, stop signals, polyadenylation signals, activators, repressors, etc.). In some embodiments, a sequence or sequences that control expression are selected to achieve a desired level of expression. In some embodiments, more than one sequence that controls expression (e.g., promoters) are utilized. In some embodiments, more than one sequence that controls expression (e.g., promoters) are utilized to achieve a desired level of expression of a plurality of polynucleotides that encode a plurality of proteins and/or polypeptides. In some embodiments, a plurality of recombinant proteins and/or polypeptide are expressed from the same vector (e.g., a bi- cistronic vector, a tri-cistronic vector, multi-cistronic). In some embodiments, a plurality of polypeptides are expressed, each of which is expressed from a separate vector. [0916] In some embodiments, an expression vector comprising a polynucleotide of the present disclosure is used to produce an RNA and/or protein and/or polypeptide in a host cell. In some embodiments, a host cell may be in vitro (e.g., a cell line) – for example a cell or cell line (e.g., Human Embryonic Kidney (HEK cells), Chinese Hamster Ovary cells, etc.) suitable for producing polynucleotides of the present disclosure and proteins and/or polypeptide encoded by said polynucleotides. [0917] In some embodiments, an expression vector is an RNA expression vector. In some embodiments, an RNA expression vector comprises a polynucleotide template used to produce an RNA in cell-free enzymatic mix. In some embodiments, an RNA expression vector comprising a polynucleotide template is enzymatically linearized prior to in vitro transcription. In some embodiments, a polynucleotide template is generated through PCR as a linear polynucleotide template. In some embodiments, a linearized polynucleotide is mixed with enzymes suitable for RNA synthesis, RNA capping and/or purification. In some embodiments, the resulting RNA is suitable for producing proteins encoded by the RNA. [0918] A variety of methods are known in the art to introduce an expression vector into host cells. In some embodiments, a vector may be introduced into host cells using transfection. In some embodiments, transfection is completed, for example, using calcium phosphate transfection, lipofection, or polyethylenimine-mediated transfection. In some embodiments, a vector may be introduced into a host cell using transduction. [0919] In some embodiments, transformed host cells are cultured following introduction of a vector into a host cell to allow for expression of said recombinant polynucleotides. In some embodiments, a transformed host cells are cultured for at least 12 hours, 16 hours, 20 hours, 24 hours, 28 hours, 32 hours, 36 hours 40 hours, 44 hours, 48 hours, 52 hours, 56 hours, 60 hours, 64 hours, 68 hours, 72 hours or longer. Transformed host cells are cultured in growth conditions (e.g., temperature, carbon-dioxide levels, growth medium) in accordance with the requirements of a host cell selected. A skilled artisan would recognize culture conditions for host cells selected are well known in the art. EXEMPLARY NUMBERED EMBODIMENTS [0920] Embodiment 1: A combination comprising: (i) a first pharmaceutical composition comprising a first polyribonucleotide, wherein the first polyribonucleotide encodes a first polypeptide, and the first polypeptide comprises one or more Plasmodium T-cell antigens; and (ii) a second pharmaceutical composition comprising a second polyribonucleotide, wherein the second polyribonucleotide encodes a second polypeptide, and the second polypeptide comprises one or more Plasmodium polypeptide or antigenic portions thereof. [0921] The combination of embodiment 1, wherein the first polypeptide comprises at least 10 amino acid s and at most 1100 amino acids. [0922] Embodiment 3: The combination of embodiment 1 or 2, wherein the first polypeptide comprises at least 10 amino acids and at most 500 amino acids. [0923] Embodiment 4: The combination of any one of embodiments 1-3, wherein the one or more Plasmodium T-cell antigens comprised in the first polypeptide comprise at least 2 and at most 10 Plasmodium T-cell antigens. [0924] Embodiment 5: The combination of any one of embodiments 1-4, wherein the one or more Plasmodium T cell antigens comprised in the first polypeptide comprise two or more of: (i) an antigenic Plasmodium CSP polypeptide fragment; (ii) an antigenic Plasmodium LSA-1 polypeptide fragment; (iii) an antigenic Plasmodium TRAP polypeptide fragment; (iv) an antigenic Plasmodium LSAP2 polypeptide fragment; (v) an antigenic Plasmodium UIS3 polypeptide fragment; (vi) an antigenic Plasmodium ETRAMP10.3 polypeptide fragment; (vii) an antigenic Plasmodium LISP-1 polypeptide fragment; (viii) an antigenic Plasmodium LISP-2 polypeptide fragment; and (ix) an antigenic Plasmodium LSA-3 polypeptide fragment. [0925] Embodiment 6: The combination of any one of embodiments 1-5, wherein the one or more Plasmodium T cell antigens comprised in the first polypeptide comprise: (i) an antigenic Plasmodium CSP polypeptide fragment; (ii) an antigenic Plasmodium TRAP polypeptide fragment; (iii) an antigenic Plasmodium UIS3 polypeptide fragment; (iv) an antigenic Plasmodium ETRAMP10.3 polypeptide fragment; and (v) an antigenic Plasmodium LSAP2 polypeptide fragment. [0926] Embodiment 7: The combination of embodiment 6, wherein the first polypeptide comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 179. [0927] Embodiment 8: The combination of any one of embodiments 1-6, wherein the one or more Plasmodium T cell antigens comprised in the first polypeptide comprise: (i) an antigenic Plasmodium CSP polypeptide fragment; (ii) an antigenic Plasmodium TRAP polypeptide fragment; (iii) an antigenic Plasmodium UIS3 polypeptide fragment; (iv) an antigenic Plasmodium ETRAMP10.3 polypeptide fragment; (v) an antigenic Plasmodium LSAP2 polypeptide fragment; (vi) an antigenic Plasmodium LSA-3 polypeptide fragment; (vii) an antigenic Plasmodium LSA-1(a) polypeptide fragment; and (viii) an antigenic Plasmodium LSA-1(b) polypeptide fragment. [0928] Embodiment 9: The combination of embodiment 8, wherein the first polypeptide comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 182. [0929] Embodiment 10: The combination of any one of embodiments 1-6, wherein the one or more Plasmodium T cell antigens comprised in the first polypeptide comprise: (i) an antigenic Plasmodium CSP polypeptide fragment; (ii) an antigenic Plasmodium TRAP polypeptide fragment; (iii) an antigenic Plasmodium UIS3 polypeptide fragment; (iv) an antigenic Plasmodium ETRAMP10.3 polypeptide fragment; (v) an antigenic Plasmodium LSAP2 polypeptide fragment; (vi) an antigenic Plasmodium LSA-1(a) polypeptide fragment; (vii) an antigenic Plasmodium LSA-1(b) polypeptide fragment; (viii) an antigenic Plasmodium LISP-2 polypeptide fragment; and (ix) an antigenic Plasmodium LISP-1 polypeptide fragment. [0930] Embodiment 11: The combination of embodiment 10, wherein the first polypeptide comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 188. [0931] Embodiment 12: The combination of any one of embodiments 1-6, wherein the one or more Plasmodium T cell antigens comprised in the first polypeptide comprise: (i) an antigenic Plasmodium CSP polypeptide fragment; (ii) an antigenic Plasmodium TRAP polypeptide fragment; (iii) an antigenic Plasmodium UIS3 polypeptide fragment; (iv) an antigenic Plasmodium ETRAMP10.3 polypeptide fragment; (v) an antigenic Plasmodium LSAP2 polypeptide fragment; (vi) an antigenic Plasmodium LSA-1(a) polypeptide fragment; (vii) an antigenic Plasmodium LSA-1(b) polypeptide fragment; and (viii) an antigenic Plasmodium LISP-1 polypeptide fragment. [0932] Embodiment 13: The combination of embodiment 12, wherein the first polypeptide comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 191. [0933] Embodiment 14: The combination of any one of embodiments 1-6, wherein the one or more Plasmodium T cell antigens comprised in the first polypeptide comprise: (i) an antigenic Plasmodium CSP polypeptide fragment; (ii) an antigenic Plasmodium TRAP polypeptide fragment; (iii) an antigenic Plasmodium UIS3 polypeptide fragment; (iv) an antigenic Plasmodium ETRAMP10.3 polypeptide fragment; (v) an antigenic Plasmodium LSAP2 polypeptide fragment; (vi) an antigenic Plasmodium LISP-2 polypeptide fragment; and (vii) an antigenic Plasmodium LISP-1 polypeptide fragment. [0934] Embodiment 15: The combination of embodiment 14, wherein the first polypeptide comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 194. [0935] Embodiment 16: The combination of any one of embodiments 1-6, wherein the one or more Plasmodium T cell antigens comprised in the first polypeptide comprise: (i) an antigenic Plasmodium CSP polypeptide fragment; (ii) an antigenic Plasmodium TRAP polypeptide fragment; (iii) an antigenic Plasmodium UIS3 polypeptide fragment; (iv) an antigenic Plasmodium ETRAMP10.3 polypeptide fragment; (v) an antigenic Plasmodium LSAP2 polypeptide fragment; (vi) an antigenic Plasmodium LSA-1(b) polypeptide fragment; and (vii) an antigenic Plasmodium LISP-1 polypeptide fragment. [0936] Embodiment 17: The combination of embodiment 16, wherein the first polypeptide comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 197. [0937] Embodiment 18: The combination of any one of embodiments 1-6, wherein the one or more Plasmodium T cell antigens comprised in the first polypeptide comprise: (i) an antigenic Plasmodium CSP polypeptide fragment; (ii) an antigenic Plasmodium TRAP polypeptide fragment; (iii) an antigenic Plasmodium UIS3 polypeptide fragment; (iv) an antigenic Plasmodium ETRAMP10.3 polypeptide fragment; (v) an antigenic Plasmodium LSAP2 polypeptide fragment; (vi) an antigenic Plasmodium LSA-1(a) polypeptide fragment; (vii) an antigenic Plasmodium LSA-1(b) polypeptide fragment; (viii) an antigenic Plasmodium LISP-2 polypeptide fragment; (ix) an antigenic Plasmodium LISP-1 polypeptide fragment; and (x) an antigenic Plasmodium LSA-3 polypeptide fragment. [0938] Embodiment 19: The combination of embodiment 18, wherein the first polypeptide comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 200. [0939] Embodiment 20: The combination of any one of embodiments 1-5, wherein the one or more Plasmodium T cell antigens comprised in the first polypeptide comprise: (i) an antigenic Plasmodium LSA-1(a) polypeptide fragment; (ii) an antigenic Plasmodium LSA-1(b) polypeptide fragment; (iii) an antigenic Plasmodium LISP-2 polypeptide fragment; (iv) an antigenic Plasmodium LISP-1 polypeptide fragment; and (v) an antigenic Plasmodium LSA-3 polypeptide fragment. [0940] Embodiment 21: The combination of embodiment 20, wherein the first polypeptide comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 212. [0941] Embodiment 22: The combination of any one of embodiments 1-5, wherein the one or more Plasmodium T cell antigens comprised in the first polypeptide comprise: (i) an antigenic Plasmodium LSA-1(a) polypeptide fragment; (ii) an antigenic Plasmodium LSA-1(b) polypeptide fragment; (iii) an antigenic Plasmodium LISP-2 polypeptide fragment; and (iv) an antigenic Plasmodium LISP-1 polypeptide fragment. [0942] Embodiment 23: The combination of embodiment 22, wherein the first polypeptide comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 209. [0943] Embodiment 24: The combination of any one of embodiments 1-6, 8, 10, 12, 14, 16, and 18, wherein the one or more Plasmodium T cell antigens comprised in the first polypeptide comprise an antigenic Plasmodium CSP polypeptide fragment, and wherein the antigenic Plasmodium CSP polypeptide fragment comprises a Plasmodium CSP N-terminal region. [0944] Embodiment 25: The combination of embodiment 24, wherein the antigenic Plasmodium CSP polypeptide fragment further comprises a Plasmodium CSP N-terminal end region. [0945] Embodiment 26: The combination of embodiment 24 or 25, wherein the antigenic Plasmodium CSP polypeptide fragment further comprises a Plasmodium CSP junction region. [0946] Embodiment 27: The combination of any one of embodiments 24-26, wherein the antigenic Plasmodium CSP polypeptide fragment comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 437. [0947] Embodiment 28: The combination of any one of embodiments 1-27, wherein the one or more Plasmodium T cell antigens comprised in the first polypeptide do not comprise an antigenic Plasmodium berghei CSP polypeptide fragment. [0948] Embodiment 29: The combination of any one of embodiments 1-5, 8, 10, 12, 18, 20, 22, and 24-26, wherein the one or more Plasmodium T cell antigens comprised in the first polypeptide comprise an antigenic Plasmodium LSA-1(a) polypeptide fragment, and wherein the antigenic Plasmodium LSA-1(a) polypeptide fragment comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 447. [0949] The combination of any one of embodiments 1-5, 8, 10, 12, 16, 18, 20, 22, and 24- 26, wherein t he one or more Plasmodium T cell antigens comprised in the first polypeptide comprise an antigenic Plasmodium LSA-1(b) polypeptide fragment, and wherein the antigenic Plasmodium LSA-1(b) polypeptide fragment comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 457. [0950] Embodiment 31: The combination of any one of embodiments 1-6, 8, 10, 12, 14, 16, 18, and 24-26, wherein the one or more Plasmodium T cell antigens comprised in the first polypeptide comprise an antigenic Plasmodium TRAP polypeptide fragment, and wherein the antigenic Plasmodium TRAP polypeptide fragment comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 472. [0951] Embodiment 32: The combination of any one of embodiments 1-6, 8, 10, 12, 14, 16, 18, and 24-26, wherein the one or more Plasmodium T cell antigens comprised in the first polypeptide comprise an antigenic Plasmodium LSAP2 polypeptide fragment, and wherein the antigenic Plasmodium LSAP2 polypeptide fragment comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 497. [0952] Embodiment 33: The combination of any one of embodiments 1-6, 8, 10, 12, 14, 16, 18, and 24-26, wherein the one or more Plasmodium T cell antigens comprised in the first polypeptide comprise an antigenic Plasmodium UIS3 polypeptide fragment, and wherein the antigenic Plasmodium UIS3 polypeptide fragment comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 510. [0953] Embodiment 34: The combination of any one of embodiments 1-6, 8, 10, 12, 14, 16, 18, and 24-26, wherein the one or more Plasmodium T cell antigens comprised in the first polypeptide comprise an antigenic Plasmodium ETRAMP10.3 polypeptide fragment, and wherein the antigenic Plasmodium ETRAMP10.3 polypeptide fragment comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 516. [0954] Embodiment 35: The combination of any one of embodiments 1-5, 10, 12, 14, 16, 18, 20, 22, and 24-26, wherein the one or more Plasmodium T cell antigens comprised in the first polypeptide comprise an antigenic Plasmodium LISP-1 polypeptide fragment, and wherein the antigenic Plasmodium LISP-1 polypeptide fragment comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 252. [0955] Embodiment 36: The combination of any one of embodiments 1-5, 10, 14, 18, 20, 22, and 24-26, wherein the one or more Plasmodium T cell antigens comprised in the first polypeptide comprise an antigenic Plasmodium LISP-2 polypeptide fragment, and wherein the antigenic Plasmodium LISP-2 polypeptide fragment comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 533. [0956] Embodiment 37: The combination of any one of embodiments 1-5, 8, 18, 20, and 24-26, wherein the one or more Plasmodium T cell antigens comprised in the first polypeptide comprise an antigenic Plasmodium LSA-3 polypeptide fragment, and wherein the antigenic Plasmodium LSA-3 polypeptide fragment comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 543. [0957] Embodiment 38: The combination of any one of embodiments 1-37, wherein the one or more Plasmodium T cell antigens comprised in the first polypeptide each comprise one or more T cell epitopes. [0958] Embodiment 39: The combination of any one of embodiments 1-38, wherein the first polypeptide further comprises an MHC class I trafficking signal (MITD). [0959] Embodiment 40: The combination of embodiment 39, wherein the MITD is located at the C-terminal end comprised in the first polypeptide. [0960] Embodiment 41: The combination of embodiment 39 or 40, wherein the MITD comprises or consists of an amino acid sequence according to SEQ ID NO: 561. [0961] Embodiment 42: The combination of any one of embodiments 1-41, wherein the first polypeptide comprises a secretory signal. [0962] Embodiment 43: The combination of embodiment 42, wherein the secretory signal comprises or consists of a Plasmodium secretory signal. [0963] Embodiment 44: The combination of embodiment 43, wherein the Plasmodium secretory signal comprises or consists of a Plasmodium CSP secretory signal. [0964] Embodiment 45: The combination of embodiment 44, wherein the Plasmodium CSP secretory signal comprises or consists of an amino acid sequence according to SEQ ID NO: 332. [0965] Embodiment 46: The combination of embodiment 42, wherein the secretory signal comprises or consists of a heterologous secretory signal. [0966] Embodiment 47: The combination of embodiment 46, wherein the heterologous secretory signal comprises or consists of a non-human secretory signal. [0967] Embodiment 48: The combination of embodiment 46 or 47, wherein the heterologous secretory signal comprises or consists of a viral secretory signal. [0968] Embodiment 49: The combination of embodiment 48, wherein the viral secretory signal comprises or consists of an HSV secretory signal. [0969] Embodiment 50: The combination of embodiment 49, wherein the HSV secretory signal comprises or consists of an HSV-1 or HSV-2 secretory signal. [0970] Embodiment 51: The combination of embodiment 49 or 50, wherein the HSV secretory signal comprises or consists of an HSV glycoprotein D (gD) secretory signal. [0971] Embodiment 52: The combination of embodiment 51, wherein the HSV gD secretory signal comprises or consists of an amino acid sequence according to SEQ ID NO: 314. [0972] Embodiment 53: The combination of embodiment 51, wherein the HSV gD secretory signal comprises or consists of an amino acid sequence according to SEQ ID NO: 320. [0973] Embodiment 54: The combination of embodiment 48, wherein the viral secretory signal comprises or consists of an Ebola virus secretory signal. [0974] Embodiment 55: The combination of embodiment 54, wherein the Ebola virus secretory signal comprises or consists of an Ebola virus spike glycoprotein (SGP) secretory signal. [0975] Embodiment 56: The combination of embodiment 55, wherein the Ebola virus SGP secretory signal comprises or consists of an amino acid sequence according to SEQ ID NO: 335. [0976] Embodiment 57: The combination of any one of embodiments 42-56, wherein the secretory signal is located at the N-terminus of the polypeptide. [0977] Embodiment 58: The combination of any one of embodiments 1-41, wherein the first polypeptide does not comprise a secretory signal. [0978] Embodiment 59: The combination of any one of embodiments 1-58, wherein the polypeptide comprises one or more linkers. [0979] Embodiment 60: The combination of embodiment 59, wherein the one or more linkers comprise one or more glycine-serine linkers. [0980] Embodiment 61: The combination of embodiment 59, wherein the one or more linkers comprise at least one linker comprising an amino acid sequence according to SEQ ID NO: 404. [0981] Embodiment 62: The combination of embodiment 59, wherein the one or more linkers comprise at least one linker comprising an amino acid sequence according to SEQ ID NO: 411. [0982] Embodiment 63: The combination of embodiment 59, wherein the one or more linkers comprise at least one linker comprising an amino acid sequence according to SEQ ID NO: 408. [0983] Embodiment 64: The combination of embodiment 59, wherein the one or more linkers comprise at least one linker comprising an amino acid sequence according to SEQ ID NO: 412. [0984] Embodiment 65: The combination of any one of embodiments 1-64, wherein the polypeptide comprises a linker between two Plasmodium T-cell antigens. [0985] Embodiment 66: The combination of any one of embodiments 1-65, wherein the polypeptide comprises a transmembrane region. [0986] Embodiment 67: The combination of embodiment 66, wherein the transmembrane region comprises or consists of a Plasmodium transmembrane region. [0987] Embodiment 68: The combination of embodiment 67, wherein the Plasmodium transmembrane region comprises or consists of a Plasmodium CSP glycosylphosphatidylinositol (GPI) anchor region. [0988] Embodiment 69: The combination of embodiment 68, wherein the Plasmodium CSP GPI anchor region comprises or consists of an amino acid sequence according to SEQ ID NO: 385. [0989] Embodiment 70: The combination of embodiment 66, wherein the transmembrane region comprises or consists of a heterologous transmembrane region. [0990] Embodiment 71: The combination of embodiment 70, wherein the heterologous transmembrane region does not comprise a hemagglutinin transmembrane region. [0991] Embodiment 72: The combination of embodiment 70 or 71, wherein the heterologous transmembrane region comprises or consists of a non-human transmembrane region. [0992] Embodiment 73: The combination of any one of embodiments 70-72, wherein the heterologous transmembrane region comprises or consists of a viral transmembrane region. [0993] Embodiment 74: The combination of any one of embodiments 70-73, wherein the heterologous transmembrane region comprises or consists of an HSV transmembrane region. [0994] Embodiment 75: The combination of embodiment 74, wherein the HSV transmembrane region comprises or consists of an HSV-1 or HSV-2 transmembrane region. [0995] Embodiment 76: The combination of embodiment 74 or 75, wherein the HSV transmembrane region comprises or consists of an HSV gD transmembrane region. [0996] Embodiment 77: The combination of embodiment 76, wherein the HSV gD transmembrane region comprises or consists of an amino acid sequence according to SEQ ID NO: 379. [0997] Embodiment 78: The combination of embodiment 66 or 70, wherein the transmembrane region comprises or consists of a human transmembrane region. [0998] Embodiment 79: The combination of embodiment 78, wherein the human transmembrane region comprises or consists of a human decay accelerating factor glycosylphosphatidylinositol (hDAF-GPI) anchor region. [0999] Embodiment 80: The combination of embodiment 79, wherein the hDAF-GPI anchor region comprises or consists of an amino acid sequence according to SEQ ID NO: 382. [1000] Embodiment 81: The combination of any one of embodiments 1-65, wherein the polypeptide does not comprise a transmembrane region. [1001] Embodiment 82: The combination of any one of embodiments 1-81, wherein the polypeptide does not comprise an antigenic fragment of a bacterial polypeptide. [1002] Embodiment 83: The combination of any one of embodiments 1-82, wherein the polypeptide does not comprise an antigenic bacillus Calmette-Guérin (BCG) polypeptide fragment, optionally wherein the antigenic BCG polypeptide fragment comprises an amino acid sequence according to SEQ ID NO: 416. [1003] Embodiment 84: The combination of any one of embodiments 1-83, wherein the polypeptide does not comprise an antigenic tetanus toxin (TT) polypeptide fragment, optionally wherein the antigenic TT polypeptide fragment comprises an amino acid sequence according to SEQ ID NO: 417. [1004] Embodiment 85: The combination of any one of embodiments 1-84, wherein the one or more Plasmodium T cell antigens comprised in the first polypeptide do not comprise an antigenic Plasmodium sporozoite threonine–asparagine-rich protein (STARP) polypeptide fragment, and optionally wherein the antigenic Plasmodium STARP polypeptide fragment comprises an amino acid sequence according to SEQ ID NO: 418. [1005] Embodiment 86: The combination of any one of embodiments 1-85, wherein the one or more Plasmodium polypeptide or antigenic portions thereof comprised in the second polypeptide are one or more Plasmodium CSP polypeptide regions or antigenic portions thereof. [1006] Embodiment 87: The combination of embodiment 86, wherein each of the one or more Plasmodium CSP polypeptide regions or portions thereof comprised in the second polypeptide comprise 10 or more contiguous amino acids of the amino acid sequence according to SEQ ID NO: 1. [1007] Embodiment 88: The combination of embodiment 86 or 87, wherein the one or more Plasmodium CSP polypeptide regions or portions thereof comprised in the second polypeptide comprise one or more repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223). [1008] Embodiment 89: The combination of any one of embodiments 86-88, wherein the one or more Plasmodium CSP polypeptide regions or portions thereof comprised in the second polypeptide comprise one or more repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223), and wherein the second polypeptide does not comprise the amino acid sequence of NPNA (SEQ ID NO: 228). [1009] Embodiment 90: The combination of any one of embodiments 86-89, wherein the one or more Plasmodium CSP polypeptide regions or portions thereof comprised in the second polypeptide comprise two or more repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223). [1010] Embodiment 91: The combination of any one of embodiments 86-90, wherein the one or more Plasmodium CSP polypeptide regions or portions thereof comprised in the second polypeptide comprise five or more repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223). [1011] Embodiment 92: The combination of any one of embodiments 86-91, wherein the one or more Plasmodium CSP polypeptide regions or portions thereof comprised in the second polypeptide comprise between two and twelve repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223). [1012] Embodiment 93: The combination of any one of embodiments 86-90, wherein the one or more Plasmodium CSP polypeptide regions or portions thereof comprised in the second polypeptide comprise exactly three repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223). [1013] Embodiment 94: The combination of any one of embodiments 86-92, wherein the one or more Plasmodium CSP polypeptide regions or portions thereof comprised in the second polypeptide comprise between four and twelve repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223). [1014] Embodiment 95: The combination of any one of embodiments 86-92 and 94, wherein the one or more Plasmodium CSP polypeptide regions or portions thereof comprised in the second polypeptide comprise: (i) exactly eight repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223); or (ii) exactly nine repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223). [1015] Embodiment 96: The combination of any one of embodiments 86-95, wherein the repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223) are all contiguous with each other. [1016] Embodiment 97: The combination of any one of embodiments 86-95, wherein the repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223) are not all contiguous with each other. [1017] Embodiment 98: The combination of any one of embodiments 86-94, wherein the one or more Plasmodium CSP polypeptide regions or portions thereof comprised in the second polypeptide comprise three portions of a Plasmodium CSP polypeptide, wherein each portion comprises three contiguous repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223), and wherein each of the portions are not contiguous with each other. [1018] Embodiment 99: The combination of any one of embodiments 86-90, wherein the one or more Plasmodium CSP polypeptide regions or portions thereof comprised in the second polypeptide comprise four portions of a Plasmodium CSP polypeptide, and wherein each portion comprises two contiguous repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223). [1019] The combination of embodiment 99, wherein the one or more Plasmodium CSP polypeptide r egions or antigenic portions thereof comprise: (i) at least two repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223), (ii) two to eighteen repeats of the amino acid sequence of NANP, and (iii) a Plasmodium CSP C-terminal region, a Plasmodium CSP C-terminal region variant, or an antigenic portion thereof. [1020] Embodiment 101: The combination of embodiment 100, one or more Plasmodium CSP polypeptide regions or antigenic portions thereof comprise, in N-terminal to C-terminal order: (i) the at least two repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223), (ii) the two to eighteen repeats of the amino acid sequence of NANP, and (iii) the Plasmodium CSP C-terminal region, a Plasmodium CSP C-terminal region variant, or an antigenic portion thereof. [1021] Embodiment 102: The combination of any one of embodiments 86-101, wherein the one or more Plasmodium CSP polypeptide regions or portions thereof comprised in the second polypeptide comprise one or more Plasmodium CSP C-terminal regions, Plasmodium CSP C-terminal region variants, or antigenic portions thereof. [1022] Embodiment 103: The combination of embodiment 102, wherein the one or more Plasmodium CSP polypeptide regions or portions thereof comprised in the second polypeptide comprise exactly one Plasmodium CSP C-terminal region, and wherein the Plasmodium CSP C-terminal region comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 235. [1023] Embodiment 104: The combination of any one of embodiments 86-101, wherein the one or more Plasmodium CSP polypeptide regions or antigenic portions thereof comprise an antigenic portion of a Plasmodium CSP C-terminal region or a Plasmodium CSP C-terminal region variant. [1024] Embodiment 105: The combination of any one of embodiments 86-101, wherein the one or more Plasmodium CSP polypeptide regions or portions thereof comprised in the second polypeptide comprise two or more antigenic portions of a Plasmodium CSP C-terminal region. [1025] Embodiment 106: The combination of embodiment 104 or 105, wherein the antigenic portion of a Plasmodium CSP C-terminal region comprises an amino acid sequence according SEQ ID NO: 261, wherein X₃ is N or K, X₄ is K, I, or R, and X₅ is N or Y. [1026] Embodiment 107: The combination of any one of embodiments 104-106, wherein the antigenic portion of a Plasmodium CSP C-terminal region comprises an amino acid sequence according SEQ ID NO: 262, wherein X₃ is N or K, X₄ is K, I, or R, and X₅ is N or Y. [1027] Embodiment 108: The combination of any one of embodiments 104-107, wherein the antigenic portion of a Plasmodium CSP C-terminal region comprises an amino acid sequence according SEQ ID NO: 262, wherein X₃ is N or K, X₄ is K, I, or R, and X₅ is N or Y. [1028] Embodiment 109: The combination of any one of embodiments 104-108, wherein the antigenic portion of a Plasmodium CSP C-terminal region comprises an amino acid sequence according SEQ ID NO: 263, wherein X₃ is N or K, X₄ is K, I, or R, and X₅ is N or Y. [1029] E 110: The combination of any one of embodiments 104-109, wherein the antigenic portion of a Pl asmodium CSP C-terminal region comprises an amino acid sequence according SEQ ID NO: 264, wherein X₁X₂ is EK or KE, X₃ is N or K, X₄ is K, I, or R, and X₅ is N or Y. [1030] Embodiment 111: The combination of any one of embodiments 104-110, wherein the antigenic portion of a Plasmodium CSP C-terminal region comprises an amino acid sequence according SEQ ID NO: 265, wherein X₁X₂ is EK or KE, X₃ is N or K, X₄ is K, I, or R, and X₅ is N or Y. [1031] Embodiment 112: The combination of any one of embodiments 104-111, wherein the antigenic portion of a Plasmodium CSP C-terminal region comprises an amino acid sequence according SEQ ID NO: 266, wherein X₁X₂ is EK or KE, X₃ is N or K, X₄ is K, I, or R, and X₅ is N or Y. [1032] Embodiment 113: The combination of any one of embodiments 104-112, wherein the antigenic portion of a Plasmodium CSP C-terminal region comprises an amino acid sequence according SEQ ID NO: 267. [1033] Embodiment 114: The combination of any one of embodiments 104-113, wherein the antigenic portion of a Plasmodium CSP C-terminal region or a Plasmodium CSP C-terminal region variant comprises an amino acid sequence according SEQ ID NO: 992. [1034] Embodiment 115: The combination of any one of embodiments 104-114, wherein the antigenic portion of a Plasmodium CSP C-terminal region or a Plasmodium CSP C-terminal region variant comprises an amino acid sequence according SEQ ID NO: 993. [1035] Embodiment 116. The combination of any one of embodiments 86-101, wherein the one or more Plasmodium CSP polypeptide regions or antigenic portions thereof comprise a Plasmodium CSP C-terminal region variant or antigenic portion thereof. [1036] Embodiment 117. The combination of any one of embodiments 86-115, wherein the Plasmodium CSP C-terminal region variant or antigenic portion thereof comprises one or more amino acid substitutions, insertions, or deletions. [1037] Embodiment 118. The combination of any one of embodiments 86-117, wherein the Plasmodium CSP C-terminal region variant or antigenic portion thereof comprises one or more amino acid substitutions, wherein the one or more amino acid substitutions comprise S301N, K317E, E318Q, N321K, E357Q, A361E, or any combination thereof, wherein the amino acid numbering is relative to SEQ ID NO: 1. [1038] Embodiment 119. The combination of any one of embodiments 86-117, wherein the Plasmodium CSP C-terminal region variant or antigenic portion thereof comprises one or more amino acid substitutions, wherein the one or more amino acid substitutions comprise S301N, K317E, E318Q, N321K, E357Q, and A361E, wherein the amino acid numbering is relative to SEQ ID NO: 1. [1039] Embodiment 120. The combination of any one of embodiments 86-117, wherein the Plasmodium CSP C-terminal region variant comprises or consists of an amino acid sequence that is at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identical to the amino acid sequence of SEQ ID NO: 994. [1040] Embodiment 121: The combination of any one of embodiments 104-120, wherein the second polypeptide comprises one or more portions of the Plasmodium CSP C-terminal region, wherein each of the one or more portions comprise or consist of: (i) an amino acid sequence according to SEQ ID NO: 244, (ii) an amino acid sequence according to SEQ ID NO: 248, (iii) an amino acid sequence according to SEQ ID NO: 262, (iv) an amino acid sequence according to SEQ ID NO: 256, or (v) a combination thereof. [1041] Embodiment 122: The combination of any one of embodiments 104-121, wherein the second polypeptide comprises one portion of the Plasmodium CSP C-terminal region, wherein the portion comprises or consists of: (i) an amino acid sequence according to SEQ ID NO: 244, (ii) an amino acid sequence according to SEQ ID NO: 248, (iii) an amino acid sequence according to SEQ ID NO: 262, (iv) an amino acid sequence according to SEQ ID NO: 256, or (v) a combination thereof. [1042] Embodiment 123: The combination of any one of embodiments 104-122, wherein the second polypeptide comprises one or more portions of the Plasmodium CSP C-terminal region, wherein the one or more portions collectively comprise or consist of: (i) an amino acid sequence according to SEQ ID NO: 244, (ii) an amino acid sequence according to SEQ ID NO: 248, (iii) an amino acid sequence according to SEQ ID NO: 262, and (iv) an amino acid sequence according to SEQ ID NO: 256. [1043] Embodiment 124: The combination of any one of embodiments 104-123, wherein the antigenic portion of a Plasmodium CSP C-terminal region comprises or consists of an amino acid sequence that is at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identical to the amino acid sequence of SEQ ID NO: 259. [1044] Embodiment 125: The combination of any one of embodiments 104-124, wherein the second polypeptide comprises a serine immediately following the Plasmodium CSP C-terminal region. [1045] Embodiment 126: The combination of any one of embodiments 104-125, wherein the second polypeptide comprises a serine-valine sequence immediately following the Plasmodium CSP C-terminal region. [1046] Embodiment 127: The combination of any one of embodiments 86-126, wherein the one or more Plasmodium CSP polypeptide regions or portions thereof comprised in the second polypeptide comprise one or more Plasmodium CSP junction regions, portions thereof, or variants thereof. [1047] Embodiment 128: The combination of embodiment 86-127, wherein the one or more Plasmodium CSP polypeptide regions or portions thereof comprised in the second polypeptide comprise two or more Plasmodium CSP junction regions or portions thereof. [1048] Embodiment 129: The combination of embodiment 86-127, wherein the one or more Plasmodium CSP polypeptide regions or portions thereof comprised in the second polypeptide comprise exactly one Plasmodium CSP junction region. [1049] Embodiment 130: The combination of embodiment 129, wherein the one Plasmodium CSP junction region consists of an amino acid sequence according to SEQ ID NO: 272. [1050] Embodiment 131: The combination of embodiment 127 or 128, wherein the one or more Plasmodium CSP polypeptide regions or portions thereof comprised in the second polypeptide comprise one or more portions of a Plasmodium CSP junction region. [1051] Embodiment 132: The combination of embodiment 131, wherein the one or more portions of a Plasmodium CSP junction region comprise a deletion of K93, L94, K95, Q96, P97, or a combination thereof, and wherein the amino acid numbering is relative to SEQ ID NO: 1. [1052] The combination of embodiment 131 or 132, wherein the one or more portions of a Plasmodium CSP junction region comprise a deletion of K93, L94, K95, and Q96, and wherein the amino acid numbering is relative to SEQ ID NO: 1. [1053] The combination of any one of embodiments 131-133, wherein the one or more portions of a Plasmodium CSP junction region comprise a deletion of K93, L94, K95, Q96 and P97, and wherein the amino acid numbering is relative to SEQ ID NO: 1. [1054] Embodiment 135: The combination of any one of embodiments 131-134, wherein each portion of a Plasmodium CSP junction region comprises or consists of an amino acid sequence according to SEQ ID NO: 275. [1055] Embodiment 136: The combination of any one of embodiments 131-134, wherein each portion of a Plasmodium CSP junction region comprises or consists of an amino acid sequence according to SEQ ID NO: 277. [1056] Embodiment 137: The combination of embodiment 128, wherein the two or more Plasmodium CSP junction regions consist of an amino acid sequence according to SEQ ID NO: 272. [1057] Embodiment 138: The combination of embodiment 128, wherein the one or more Plasmodium CSP polypeptide regions or portions thereof comprised in the second polypeptide comprise two or more portions of a Plasmodium CSP junction region. [1058] Embodiment 139: The combination of embodiment 138, wherein the two or more portions of a Plasmodium CSP junction region comprise a deletion of K93, L94, K95, Q96, P97, or a combination thereof, and wherein the amino acid numbering is relative to SEQ ID NO: 1. [1059] E The combination of embodiment 138 or 139, wherein the two or more portions of a Plasmodium CSP junction region comprise a deletion of K93, L94, K95, and Q96, and wherein the amino acid numbering is relative to SEQ ID NO: 1. [1060] Embodiment 141: The combination of any one of embodiments 138-140, wherein the two or more portions of a Plasmodium CSP junction region comprise a deletion of K93, L94, K95, Q96 and P97, and wherein the amino acid numbering is relative to SEQ ID NO: 1. [1061] Embodiment 142: The combination of any one of embodiments 138-141, wherein each portion of a Plasmodium CSP junction region comprises or consists of an amino acid sequence according to SEQ ID NO: 275. [1062] Embodiment 143: The combination of any one of embodiments 138-141, wherein each portion of a Plasmodium CSP junction region comprises or consists of an amino acid sequence according to SEQ ID NO: 277. [1063] Embodiment 144: The combination of embodiment 127, wherein the one or more Plasmodium CSP polypeptide regions or portions thereof comprised in the second polypeptide comprise one or more Plasmodium CSP junction region variants. [1064] Embodiment 145: The combination of embodiment 144, wherein the Plasmodium CSP junction region variant comprises one or more substitution mutations. [1065] Embodiment 146: The combination of embodiment 145, wherein the one or more substitution mutations comprise a K93A mutation, an L94A mutation, or both, wherein the amino acid numbering is relative to SEQ ID NO: 1. [1066] Embodiment 147: The combination of embodiment 144 or 145, wherein each Plasmodium CSP junction region variant comprises the amino acid sequence of AAKQ. [1067] Embodiment 148: The combination of any one of embodiments 86-147, wherein the one or more Plasmodium CSP polypeptide regions or portions thereof comprised in the second polypeptide comprise one or more Plasmodium CSP N-terminal end regions or portions thereof. [1068] Embodiment 149: The combination of embodiment 148, wherein the one or more Plasmodium CSP polypeptide regions or portions thereof comprised in the second polypeptide comprise two or more Plasmodium CSP N-terminal end regions or portions thereof. [1069] Embodiment 150: The combination of embodiment 148 or 149, wherein each Plasmodium CSP N- terminal end region consists of an amino acid sequence according to SEQ ID NO: 285. [1070] Embodiment 151: The combination of any one of embodiments 86-147, wherein the second polypeptide does not comprise a Plasmodium CSP N-terminal end region or any portion thereof. [1071] Embodiment 152: The combination of any one of embodiments 86-151, wherein the one or more Plasmodium CSP polypeptide regions or portions thereof comprised in the second polypeptide comprise one or more Plasmodium CSP N-terminal regions or portions thereof. [1072] Embodiment 153: The combination of embodiment 152, wherein the one or more Plasmodium CSP polypeptide regions or portions thereof comprised in the second polypeptide comprise two or more Plasmodium CSP N-terminal regions or portions thereof. [1073] Embodiment 154: The combination of embodiment 152 or 153, wherein each Plasmodium CSP N- terminal region comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 288. [1074] Embodiment 155: The combination of embodiment 152, wherein the one or more Plasmodium CSP polypeptide regions or portions thereof comprised in the second polypeptide comprise an antigenic portion of a Plasmodium CSP N-terminal region. [1075] Embodiment 156: The combination of embodiment 155, wherein the antigenic portion of a Plasmodium CSP N-terminal region is a Plasmodium CSP N-terminal start region. [1076] Embodiment 157: The combination of embodiment 156, wherein the Plasmodium CSP N-terminal start region comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 1010. [1077] Embodiment 158: The combination of any one of embodiments 86-151, wherein the second polypeptide does not comprise a Plasmodium CSP N-terminal region or any portion thereof. [1078] Embodiment 159: The combination of any one of embodiments 86-158, wherein the one or more Plasmodium CSP polypeptide regions or portions thereof comprised in the second polypeptide comprise one or more Plasmodium CSP major repeat regions or portions thereof. [1079] Embodiment 160: The combination of embodiment 159, wherein the one or more Plasmodium CSP major repeat regions or portions thereof comprise the amino acid sequence NANPNA or NPNANP. [1080] Embodiment 161: The combination of embodiment 159 or 160, wherein the one or more Plasmodium CSP polypeptide regions or portions thereof comprised in the second polypeptide comprise at least two Plasmodium CSP major repeat region portions, wherein each CSP major repeat region portion comprises at least 4 and at most 7 repeats of the sequence NANP. [1081] Embodiment 162: The combination of any one of embodiments 159-161, wherein the one or more Plasmodium CSP polypeptide regions or portions thereof comprised in the second polypeptide comprise two or three Plasmodium CSP major repeat region portions, wherein each CSP major repeat region portion comprises 6 repeats of the sequence NANP (SEQ ID NO: 230). [1082] The combination of embodiment 159 or 160, wherein the one or more Plasmodium C SP polypeptide regions or portions thereof comprised in the second polypeptide comprise exactly one Plasmodium CSP major repeat region or portion thereof, and the Plasmodium CSP major repeat region or portion thereof comprises a total of at least 2 and at most 35 repeats of the amino acid sequence NANP. [1083] Embodiment 164: The combination of any one of embodiments 159, 160, 162, and 163, wherein the Plasmodium CSP major repeat region or portion thereof comprises two contiguous stretches of repeats of the amino acid sequence NANP (SEQ ID NO: 230), and wherein the two contiguous stretches of repeats of the amino acid sequence NANP (SEQ ID NO: 230) flank an amino acid sequence of NVDP (SEQ ID NO:229). [1084] Embodiment 165: The combination of embodiment 164, wherein the Plasmodium CSP major repeat region comprises, in N-terminus to C-terminus order, 17 repeats of the amino acid sequence NANP (SEQ ID NO: 230), an amino acid sequence of NVDP (SEQ ID NO:229), and 18 repeats of the amino acid sequence NANP (SEQ ID NO: 230). [1085] Embodiment 166: The combination of any one of embodiments 159-164, wherein a portion of the Plasmodium CSP major repeat region consists of at most 18 contiguous repeats of the amino acid sequence NANP. [1086] E The combination of any one of embodiments 159-164, wherein a portion of the Plasmodium CSP major repeat region consists of 2 contiguous repeats of the amino acid sequence NANP. [1087] Embodiment 168: The combination of embodiment 167, wherein the Plasmodium CSP major repeat region comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 305. [1088] Embodiment 169: The combination of any one of embodiments 159-164, 166 and 167, wherein the one or more Plasmodium CSP polypeptide regions or antigenic portions thereof comprises an antigenic portion of a Plasmodium CSP major repeat region. [1089] Embodiment 170: The combination of embodiment 169, wherein the antigenic portion of a Plasmodium CSP major repeat region comprises at least six repeats of the amino acid sequence of NANP. [1090] Embodiment 171: The combination of embodiment 170, wherein the antigenic portion of a Plasmodium CSP major repeat region further comprises an asparagine-alanine positioned immediately following of the six repeats of the amino acid sequence of NANP (SEQ ID NO: 230). [1091] Embodiment 172: The combination of embodiment 171, wherein the antigenic portion of a Plasmodium CSP major repeat region comprises or consists of an amino acid sequence that is at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identical to the amino acid sequence of SEQ ID NO: 303. [1092] Embodiment 173: The combination of embodiment 169, wherein the antigenic portion of a Plasmodium CSP major repeat region comprises eighteen repeats of the amino acid sequence of NANP (SEQ ID NO: 230). [1093] Embodiment 174: The combination of embodiment 173, wherein the antigenic portion of a Plasmodium CSP major repeat region comprises or consists of an amino acid sequence that is at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identical to the amino acid sequence of SEQ ID NO: 308. [1094] Embodiment 175: The combination of any one of embodiments 86-174, wherein the second polypeptide does not comprise (i) a Plasmodium CSP N-terminal region or any portion thereof and/or (ii) a Plasmodium CSP C-terminal region or any portion thereof. [1095] Embodiment 176: The combination of any one of embodiments 86-158, wherein the second polypeptide does not comprise a Plasmodium CSP major repeat region or a portion of a Plasmodium CSP major repeat region comprising the amino acid sequence NPNA (SEQ ID NO: 228). [1096] Embodiment 177: The combination of any one of embodiments 86-176, wherein the one or more Plasmodium CSP polypeptide regions or portions thereof, if present in the second polypeptide, are in the following N- terminus to C-terminus order: (i) one or more Plasmodium CSP N-terminal regions or portions thereof, (ii) one or more Plasmodium CSP N-terminal end regions or portions thereof, (iii) one or more Plasmodium CSP junction regions, portions thereof, or variants thereof, (iv) one or more repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223), (v) one or more Plasmodium CSP major repeat regions or portions thereof, and (vi) one or more Plasmodium CSP C-terminal regions or portions thereof. [1097] Embodiment 178: The combination of any one of embodiments 86-177, wherein the one or more Plasmodium CSP polypeptide regions or portions thereof, if present in the second polypeptide, are in the following N- terminus to C-terminus order: (i) one Plasmodium CSP N-terminal region or portion thereof, (ii) one Plasmodium CSP N-terminal end region or portion thereof, (iii) one Plasmodium CSP junction region, portion thereof, or variant thereof, (iv) one or more repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223), (v) one Plasmodium CSP major repeat region or portion thereof, and (vi) one Plasmodium CSP C-terminal region or portion thereof. [1098] Embodiment 179: The combination of any one of embodiments 1-178, wherein the second polypeptide comprises one or more helper antigens. [1099] Embodiment 180: The combination of embodiment 179, wherein the one or more helper antigens comprise a Plasmodium antigen. [1100] Embodiment 181: The combination of embodiment 179 or 180, wherein the one or more helper antigens are Plasmodium 2-phospho-D-glycerate hydro-lyase antigen, Plasmodium liver stage antigen 1(a), (LSA- 1(a)), Plasmodium liver stage antigen 1(b) (LSA-1(b)), Plasmodium thrombospondin-related anonymous protein (TRAP), Plasmodium liver stage associated protein 1 (LSAP1), Plasmodium liver stage associated protein 2 (LSAP2), Plasmodium UIS3, Plasmodium ETRAMP10.3, Plasmodium liver specific protein 1 (LISP-1), Plasmodium liver specific protein 2 (LISP-2), Plasmodium liver stage antigen 3 (LSA-3), Plasmodium EXP1, Plasmodium E140, Plasmodium reticulocyte-binding protein homolog 5 (Rh5), Plasmodium glutamic acid-rich protein (GARP), Plasmodium parasite- infected erythrocyte surface protein 2 (PIESP2), Plasmodium Cysteine-Rich Protective Antigen (CyRPA), Plasmodium Ripr, Plasmodium P113, or a combination thereof. [1101] Embodiment 182: The combination of any one of embodiments 179-181, wherein the one or more helper antigens comprise or consist of a P. falciparum 2-phospho-D-glycerate hydro-lyase antigen. [1102] The combination of 182, wherein the P. falciparum 2-phospho-D-glycerate hydro- lyase antigen comprises or consists of an amino acid sequence according to SEQ ID NO: 388. [1103] Embodiment 184: The combination of any one of embodiments 179-183, wherein the one or more helper antigens comprise or consist of a P. falciparum liver-stage antigen 3. [1104] Embodiment 185: The combination of 184, wherein the P. falciparum liver-stage antigen 3 comprises or consists of an amino acid sequence according to SEQ ID NO: 391. [1105] Embodiment 186: The combination of any one of embodiments 179-185, wherein the one or more helper antigens comprise an Anopheles antigen. [1106] Embodiment 187: The combination of any one of embodiments 179-186, wherein the helper antigen comprises or consists of an Anopheles gambiae TRIO. [1107] Embodiment 188: The combination of 187, wherein the Anopheles gambiae TRIO comprises or consists of an amino acid sequence according to SEQ ID NO: 393. [1108] Embodiment 189: The combination of any one of embodiments 179-188, wherein the second polypeptide comprises a secretory signal and the helper antigen immediately follows the secretory signal. [1109] Embodiment 190: The combination of any one of embodiments 179-189, wherein the second polypeptide comprises a helper antigen at the C-terminus of the second polypeptide. [1110] Embodiment 191: The combination of any one of embodiments 1-190, wherein the second polypeptide comprises a multimerization region. [1111] Embodiment 192: The combination of embodiment 191, wherein the multimerization region comprises or consists of a trimerization region. [1112] Embodiment 193: The combination of embodiment 192, wherein the trimerization region comprises or consists of a fibritin region. [1113] Embodiment 194: The combination of embodiment 193, wherein the fibritin region comprises or consists of an amino acid sequence according to SEQ ID NO: 399. [1114] Embodiment 195: The combination of any one of embodiments 191-194, wherein the second polypeptide comprises a multimerization region at the N-terminus of the second polypeptide. [1115] Embodiment 196: The combination of any one of embodiments 1-195, wherein the second polypeptide comprises a self-aggregation region. [1116] Embodiment 197: The combination of embodiment 196, wherein the self-aggregation region comprises or consists of a ferritin region. [1117] Embodiment 198: The combination of embodiment 197, wherein the ferritin region comprises or consists of an amino acid sequence according to SEQ ID NO: 402. [1118] Embodiment 199: The combination of any one of embodiments 196-198, wherein the polypeptide comprises a self-aggregation region at the N-terminus of the polypeptide. [1119] Embodiment 200: The combination of any one of embodiments 1-199, wherein the second polypeptide comprises a secretory signal. [1120] Embodiment 201: The combination of embodiment 200, wherein the secretory signal comprises or consists of a Plasmodium secretory signal. [1121] Embodiment 202: The combination of embodiment 201, wherein the Plasmodium secretory signal comprises or consists of a Plasmodium CSP secretory signal. [1122] Embodiment 203: The combination of embodiment 202, wherein the Plasmodium CSP secretory signal comprises or consists of an amino acid sequence according to SEQ ID NO: 332. [1123] Embodiment 204: The combination of embodiment 200, wherein the secretory signal comprises or consists of a heterologous secretory signal. [1124] Embodiment 205: The combination of 204, wherein the heterologous secretory signal comprises or consists of a non-human secretory signal. [1125] Embodiment 206: The combination of embodiment 204 or 205, wherein the heterologous secretory signal comprises or consists of a viral secretory signal. [1126] Embodiment 207: The combination of embodiment 206, wherein the viral secretory signal comprises or consists of an HSV secretory signal. [1127] Embodiment 208: The combination of embodiment 207, wherein the HSV secretory signal comprises or consists of an HSV-1 or HSV-2 secretory signal. [1128] Embodiment 209: The combination of embodiment 207 or 208, wherein the HSV secretory signal comprises or consists of an HSV glycoprotein D (gD) secretory signal. [1129] Embodiment 210: The combination of embodiment 209, wherein the HSV gD secretory signal comprises or consists of an amino acid sequence according to SEQ ID NO: 314. [1130] Embodiment 211: The combination of embodiment 209, wherein the HSV gD secretory signal comprises or consists of an amino acid sequence according to SEQ ID NO: 320. [1131] Embodiment 212: The combination of embodiment 206, wherein the viral secretory signal comprises or consists of an Ebola virus secretory signal. [1132] Embodiment 213: The combination of embodiment 212, wherein the Ebola virus secretory signal comprises or consists of an Ebola virus spike glycoprotein (SGP) secretory signal. [1133] Embodiment 214: The combination of embodiment 213, wherein the Ebola virus SGP secretory signal comprises or consists of an amino acid sequence according to SEQ ID NO: 335. [1134] Embodiment 215: The combination of any one of embodiments 200-214, wherein the secretory signal is located at the N-terminus of the second polypeptide. [1135] Embodiment 216: The combination of any one of embodiments 1-199, wherein the second polypeptide does not comprise a secretory signal. [1136] Embodiment 217: The combination of any one of embodiments 1-216, wherein the second polypeptide comprises a transmembrane region. [1137] Embodiment 218: The combination of embodiment 217, wherein the transmembrane region comprises or consists of a Plasmodium transmembrane region. [1138] Embodiment 219: The combination of embodiment 218, wherein the Plasmodium transmembrane region comprises or consists of a Plasmodium CSP glycosylphosphatidylinositol (GPI) anchor region. [1139] E 220: The combination of embodiment 219, wherein the Plasmodium CSP GPI anchor region compris es or consists of an amino acid sequence according to SEQ ID NO: 385. [1140] Embodiment 221: The combination of embodiment 217, wherein the transmembrane region comprises or consists of a heterologous transmembrane region. [1141] Embodiment 222: The combination of embodiment 221, wherein the heterologous transmembrane region does not comprise a hemagglutinin transmembrane region. [1142] The combination of embodiment 221 or 222, wherein the heterologous transmembra ne region comprises or consists of a non-human transmembrane region. [1143] Embodiment 224: The combination of any one of embodiments 221-223 wherein the heterologous transmembrane region comprises or consists of a viral transmembrane region. [1144] Embodiment 225: The combination of embodiment 224, wherein the viral transmembrane region comprises or consists of an HSV transmembrane region. [1145] Embodiment 226: The combination of embodiment 225, wherein the HSV transmembrane region comprises or consists of an HSV-1 or HSV-2 transmembrane region. [1146] Embodiment 227: The combination of embodiment 224 or 225, wherein the HSV transmembrane region comprises or consists of an HSV gD transmembrane region. [1147] Embodiment 228: The combination of embodiment 227, wherein the HSV gD transmembrane region comprises or consists of an amino acid sequence according to SEQ ID NO: 379. [1148] Embodiment 229: The combination of any one of embodiments 221-223, wherein the heterologous transmembrane region comprises or consists of a human transmembrane region. [1149] Embodiment 230: The combination of embodiment 229, wherein the human transmembrane region comprises or consists of a human decay accelerating factor glycosylphosphatidylinositol (hDAF-GPI) anchor region. [1150] Embodiment 231: The combination of embodiment 230, wherein the hDAF-GPI anchor region comprises or consists of an amino acid sequence according to SEQ ID NO: 382. [1151] Embodiment 232: The combination of any one of embodiments 1-216, wherein the second polypeptide does not comprise a transmembrane region. [1152] Embodiment 233: The combination of any one of embodiments 1-232, wherein the second polypeptide comprises one or more linkers. [1153] Embodiment 234: The combination of embodiment 233, wherein the one or more linkers comprise one or more glycine-serine linkers. [1154] Embodiment 235: The combination of embodiment 233, wherein the one or more linkers comprise or consist of an amino acid sequence according to SEQ ID NO: 404. [1155] Embodiment 236: The combination of embodiment 233, wherein the one or more linkers comprise or consist of an amino acid sequence according to SEQ ID NO: 411. [1156] Embodiment 237: The combination of embodiment 233, wherein the one or more linkers comprise or consist of an amino acid sequence according to SEQ ID NO: 408. [1157] Embodiment 238: The combination of embodiment 226, wherein the one or more linkers comprise or consist of an amino acid sequence according to SEQ ID NO: 412. [1158] Embodiment 239: The combination of any one of embodiments 233-238, wherein the second polypeptide comprises a linker between the C-terminal region or portion thereof and the transmembrane region. [1159] Embodiment 240: The combination of any one of embodiments 233-238, wherein the second polypeptide comprises a linker after an amino acid sequence of NANPNVDP (SEQ ID NO: 223). [1160] Embodiment 241: The combination of any one of embodiments 1-86, wherein the second polypeptide comprises: (i) a secretory signal, (ii) one or more Plasmodium CSP junction regions, portions thereof, or variants thereof, (iii) one or more repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223), (iv) one or more Plasmodium CSP C-terminal regions or portions thereof, and (v) a transmembrane region, and wherein the second polypeptide does not comprise: (a) an amino acid sequence of NPNA (SEQ ID NO: 228), and (b) a Plasmodium CSP N-terminal region or portion thereof. [1161] Embodiment 242: The combination of embodiment 241, wherein the second polypeptide does not comprise a Plasmodium CSP N-terminal end region. [1162] Embodiment 243: The combination of embodiment 241 and 242, wherein the second polypeptide comprises one or more Plasmodium CSP N-terminal end regions or portions thereof. [1163] Embodiment 244: The combination of any one of embodiments 1-86, wherein the second polypeptide comprises: (i) a secretory signal, (ii) one or more Plasmodium CSP junction regions, portions thereof, or variants thereof, (iii) one or more repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223), and (iv) one or more Plasmodium CSP C-terminal regions or portions thereof. [1164] Embodiment 245: The combination of any one of embodiments 1-86, wherein the second polypeptide comprises: (i) a secretory signal, (ii) three or more Plasmodium CSP junction regions, portions thereof, or variants thereof, (iii) three or more repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223), and (iv) two or more Plasmodium CSP major repeat region portions, and wherein the polypeptide does not comprise: (a) a Plasmodium CSP N-terminal region or portion thereof, and (b) a Plasmodium CSP C-terminal region or portion thereof. [1165] Embodiment 246: The combination of embodiment 244 or 245, wherein the second polypeptide comprises an amino acid sequence that has at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identity to a sequence of SEQ ID NO: 108. [1166] Embodiment 247: The combination of any one of embodiments 1-86, wherein the second polypeptide comprises: (i) a secretory signal, (ii) one or more Plasmodium CSP junction regions, portions thereof, or variants thereof, (iii) one or more repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223), (iv) one or more Plasmodium CSP C-terminal regions or portions thereof, and (v) a transmembrane region. [1167] Embodiment 248: The combination of any one of embodiments 1-86, wherein the second polypeptide comprises: (i) a secretory signal, (ii) three or more Plasmodium CSP junction regions, portions thereof, or variants thereof, (iii) three or more repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223), (iv) two or more Plasmodium CSP major repeat region portions, and (v) a transmembrane region, and wherein the polypeptide does not comprise (a) a Plasmodium CSP N-terminal region or portion thereof, and (b) a Plasmodium CSP C-terminal region or portion thereof. [1168] Embodiment 249: The combination of embodiment 247 or 248, wherein the second polypeptide comprises an amino acid sequence that has at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identity to a sequence of SEQ ID NO: 107 or 109. [1169] E i 250: The combination of any one of embodiments 1-86, wherein the second polypeptide co mprises: (i) a secretory signal, (ii) three or more Plasmodium CSP junction regions, portions thereof, or variants thereof, (iii) three or more repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223), and (iv) two or more Plasmodium CSP major repeat region portions, and wherein the polypeptide does not comprise: (a) a Plasmodium CSP N-terminal region or portion thereof, and (b) a Plasmodium CSP C-terminal region or portion thereof. [1170] Embodiment 251: The combination of embodiment 250, wherein the second polypeptide comprises an amino acid sequence that has at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to a sequence of SEQ ID NO: 110 or 111. [1171] Embodiment 252: The combination of any one of embodiments 241-251, wherein the second polypeptide comprises one or more helper antigens. [1172] Embodiment 253: The combination of any one of embodiments 1-86, wherein the second polypeptide comprises: (i) a secretory signal, (ii) a Plasmodium CSP N-terminal end region, (iii) a Plasmodium CSP junction region, (iv) nine repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223), (v) a Plasmodium CSP C-terminal region, and (vi) five antigenic repeat regions, wherein each antigenic repeat region comprises: (A) a linker, and (B) a helper antigen, and wherein the second polypeptide does not comprise any of: (a) an amino acid sequence of NPNA (SEQ ID NO: 228), (b) a Plasmodium CSP N-terminal region or portion thereof, and (c) a transmembrane region. [1173] Embodiment 254: The combination of embodiment 253, wherein the second polypeptide comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 36. [1174] Embodiment 255: The combination of any one of embodiments 1-86, wherein the second polypeptide comprises: (i) a secretory signal, (ii) a helper antigen, (iii) a linker, (iv) a Plasmodium CSP N-terminal end region, (v) a Plasmodium CSP junction region, (vi) nine repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223) (vii) a Plasmodium CSP C-terminal region, (viii) a serine-valine sequence immediately following the Plasmodium CSP C-terminal region, (ix) a linker, and (x) a transmembrane region, and wherein the second polypeptide does not comprise any of: (a) an amino acid sequence of NPNA (SEQ ID NO: 228), and (b) a Plasmodium CSP N-terminal region or portion thereof. [1175] Embodiment 256: The combination of embodiment 255, wherein the second polypeptide comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 39. [1176] Embodiment 257: The combination of any one of embodiments 1-86, wherein the second polypeptide comprises: (i) a secretory signal, (ii) a portion of a Plasmodium CSP junction region, (iii) three repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223), (iv) a Plasmodium CSP C-terminal region, (v) a serine-valine sequence immediately following the Plasmodium CSP C-terminal region, (vi) a linker, and (vii) a transmembrane region, and wherein the second polypeptide does not comprise any of: (a) a Plasmodium CSP N-terminal region or portion thereof, (b) a Plasmodium CSP N-terminal end region or portion thereof, and (c) an amino acid sequence of NPNA (SEQ ID NO: 228). [1177] Embodiment 258: The combination of embodiment 257, wherein the second polypeptide comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 57. [1178] Embodiment 259: The combination of any one of embodiments 1-86, wherein the second polypeptide comprises: (i) a secretory signal, (ii) a portion of a Plasmodium CSP junction region, (iii) nine repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223), (iv) a Plasmodium CSP C-terminal region, (v) a serine-valine sequence immediately following the Plasmodium CSP C-terminal region, (vi) a linker, and (vii) a transmembrane region, and wherein the second polypeptide does not comprise any of: (a) a Plasmodium CSP N-terminal region or portion thereof, (b) a Plasmodium CSP N-terminal end region or portion thereof, and (c) an amino acid sequence of NPNA (SEQ ID NO: 228). [1179] Embodiment 260: The combination of embodiment 259, wherein the second polypeptide comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 60. [1180] Embodiment 261: The combination of any one of embodiments 1-86, wherein the second polypeptide comprises: (i) a secretory signal, (ii) a Plasmodium CSP junction region, (iii) three repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223), (iv) a Plasmodium CSP C-terminal region, (v) a serine-valine sequence immediately following the Plasmodium CSP C-terminal region, (vi) a linker, and (vii) a transmembrane region, and wherein the second polypeptide does not comprise any of: (a) a Plasmodium CSP N-terminal region or portion thereof, (b) a Plasmodium CSP N-terminal end region or portion thereof, and (c) an amino acid sequence of NPNA (SEQ ID NO: 228). [1181] Embodiment 262: The combination of embodiment 261, wherein the second polypeptide comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 63. [1182] Embodiment 263: The combination of any one of embodiments 1-86, wherein the second polypeptide comprises: (i) a secretory signal, (ii) a Plasmodium CSP junction region, (iii) nine repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223), (iv) a Plasmodium CSP C-terminal region, (v) a serine-valine sequence immediately following the Plasmodium CSP C-terminal region, (vi) a linker, and (vii) a transmembrane region, and wherein the second polypeptide does not comprise any of: (a) a Plasmodium CSP N-terminal region or portion thereof, (b) a Plasmodium CSP N-terminal end region or portion thereof, and (c) an amino acid sequence of NPNA (SEQ ID NO: 228). [1183] Embodiment 264: The combination of embodiment 263, wherein the second polypeptide comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 66. [1184] E i 265: The combination of any one of embodiments 1-86, wherein the second polypeptide co mprises: (i) a secretory signal, (ii) a Plasmodium CSP junction region variant, (iii) three repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223), (iv) a Plasmodium CSP C-terminal region, (v) a serine-valine sequence immediately following the Plasmodium CSP C-terminal region, (vi) a linker, and (vii) a transmembrane region, and wherein the second polypeptide does not comprise any of: (a) a Plasmodium CSP N-terminal region or portion thereof, (b) a Plasmodium CSP N-terminal end region or portion thereof, and (c) an amino acid sequence of NPNA (SEQ ID NO: 228). [1185] Embodiment 266: The combination of embodiment 265, wherein the second polypeptide comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 69. [1186] Embodiment 267: The combination of any one of embodiments 1-86, wherein the second polypeptide comprises: (i) a secretory signal, (ii) a Plasmodium CSP junction region variant, (iii) nine repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223), (iv) a Plasmodium CSP C-terminal region, (v) a serine-valine sequence immediately following the Plasmodium CSP C-terminal region, (vi) a linker, and (vii) a transmembrane region, and wherein the second polypeptide does not comprise any of: (a) a Plasmodium CSP N-terminal region or portion thereof, (b) a Plasmodium CSP N-terminal end region or portion thereof, and (c) an amino acid sequence of NPNA (SEQ ID NO: 228). [1187] Embodiment 268: The combination of embodiment 267, wherein the second polypeptide comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 72. [1188] Embodiment 269: The combination of any one of embodiments 1-86, wherein the second polypeptide comprises: (i) a secretory signal, (ii) a portion of a Plasmodium CSP junction region, (iii) three repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223), (iv) a Plasmodium CSP C-terminal region, (v) a serine-valine sequence immediately following the Plasmodium CSP C-terminal region, (vi) a linker, and (vii) a transmembrane region, and wherein the second polypeptide does not comprise any of: (a) a Plasmodium CSP N-terminal region or portion thereof, (b) a Plasmodium CSP N-terminal end region or portion thereof, and (c) an amino acid sequence of NPNA (SEQ ID NO: 228). [1189] Embodiment 270: The combination of embodiment 269, wherein the second polypeptide comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 75. [1190] Embodiment 271: The combination of any one of embodiments 1-86, wherein the second polypeptide comprises: (i) a secretory signal, (ii) a portion of a Plasmodium CSP junction region, (iii) nine repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223), (iv) a Plasmodium CSP C-terminal region, (v) a serine-valine sequence immediately following the Plasmodium CSP C-terminal region, (vi) a linker, and (vii) a transmembrane region, and wherein the second polypeptide does not comprise any of: (a) a Plasmodium CSP N-terminal region or portion thereof, (b) a Plasmodium CSP N-terminal end region or portion thereof, and (c) an amino acid sequence of NPNA (SEQ ID NO: 228). [1191] Embodiment 272: The combination of embodiment 271, wherein the second polypeptide comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 78. [1192] Embodiment 273: The combination of any one of embodiments 1-86, wherein the second polypeptide comprises: (i) a secretory signal, (ii) a Plasmodium CSP N-terminal end region, (iii) a Plasmodium CSP junction region, (iv) nine repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223), (v) a Plasmodium CSP C-terminal region, (vi) a serine-valine sequence immediately following the Plasmodium CSP C-terminal region, (vii) a linker, and (viii) a transmembrane region, and wherein the second polypeptide does not comprise any of: (a) a Plasmodium CSP N-terminal region or portion thereof, and (b) an amino acid sequence of NPNA (SEQ ID NO: 228). [1193] Embodiment 274: The combination of embodiment 273, wherein the second polypeptide comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 81. [1194] Embodiment 275: The combination of any one of embodiments 1-86, wherein the second polypeptide comprises: (i) a secretory signal, (ii) a Plasmodium CSP N-terminal end region, (iii) a Plasmodium CSP junction region variant, (iv) nine repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223), (v) a Plasmodium CSP C-terminal region, (vi) a serine-valine sequence immediately following the Plasmodium CSP C-terminal region, (vii) a linker, and (viii) a transmembrane region, and wherein the second polypeptide does not comprise any of: (a) a Plasmodium CSP N-terminal region or portion thereof, and (b) an amino acid sequence of NPNA (SEQ ID NO: 228). [1195] Embodiment 276: The combination of embodiment 275, wherein the second polypeptide comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 84. [1196] Embodiment 277: The combination of any one of embodiments 1-86, wherein the second polypeptide comprises: (i) a secretory signal, (ii) a Plasmodium CSP N-terminal end region, (iii) a Plasmodium CSP junction region, (iv) nine repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223), (v) a Plasmodium CSP C-terminal region, (vi) a transmembrane region, and wherein the second polypeptide does not comprise any of: (a) a Plasmodium CSP N-terminal region or portion thereof, and (b) an amino acid sequence of NPNA (SEQ ID NO: 228). [1197] Embodiment 278: The combination of embodiment 277, wherein the second polypeptide comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 102. [1198] Embodiment 279: The combination of any one of embodiments 1-86, wherein the second polypeptide comprises: (i) a secretory signal, (ii) a Plasmodium CSP N-terminal end region, (iii) a Plasmodium CSP junction region, (iv) nine repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223), (v) a Plasmodium CSP C-terminal region, and (vi) a transmembrane region, and wherein the second polypeptide does not comprise any of: (a) a Plasmodium CSP N-terminal region or portion thereof, and (b) an amino acid sequence of NPNA (SEQ ID NO: 228). [1199] Embodiment 280: The combination of embodiment 279, wherein the second polypeptide comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 105. [1200] Embodiment 281: The combination of any one of embodiments 1-86, wherein the second polypeptide comprises: (i) a secretory signal, (ii) two or more Plasmodium CSP neutralizing region repeats, wherein each Plasmodium CSP neutralizing region repeat comprises or consists of: (a) a Plasmodium CSP N-terminal end region, (b) a Plasmodium CSP junction region, (c) two repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223), and (d) a linker, (iii) a portion of a Plasmodium CSP major repeat region, (iv) a Plasmodium CSP C-terminal region, (v) a serine-valine sequence immediately following the Plasmodium CSP C-terminal region, (vi) a linker, and (vii) a transmembrane region, and wherein the second polypeptide does not comprise a Plasmodium CSP N-terminal region or portion thereof. [1201] Embodiment 282: The combination of embodiment 281, wherein the second polypeptide comprises exactly four Plasmodium CSP neutralizing region repeats. [1202] Embodiment 283: The combination of embodiment 281 or 282, wherein the second polypeptide comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 87. [1203] Embodiment 284: The combination of any one of embodiments 1-86, wherein the second polypeptide comprises: (i) a secretory signal, (ii) one Plasmodium CSP junction region, (iii) three repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223), (iv) a Plasmodium CSP major repeat region, (v) one Plasmodium CSP C-terminal region, (vi) a serine-valine sequence immediately following the Plasmodium CSP C-terminal region, (vii) a linker, and (viii) a transmembrane region, and wherein the second polypeptide does not comprise any of: (a) a Plasmodium CSP N-terminal region or portion thereof, and (b) a Plasmodium CSP N-terminal end region or portion thereof. [1204] Embodiment 285: The combination of embodiment 284, wherein the second polypeptide comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 30. [1205] Embodiment 286: The combination of any one of embodiments 1-86, wherein the second polypeptide comprises: (i) a secretory signal, (ii) a Plasmodium CSP N-terminal region, (iii) a Plasmodium CSP N-terminal end region, (iv) a portion of a Plasmodium CSP junction region, (v) three repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223), (vi) a Plasmodium CSP major repeat region, (vii) a Plasmodium CSP C-terminal region, and (viii) a serine immediately following the Plasmodium CSP C-terminal region, and wherein the second polypeptide does not comprise a transmembrane region. [1206] Embodiment 287: The combination of embodiment 286, wherein the second polypeptide comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 27. [1207] Embodiment 288: The combination of any one of embodiments 1-86, wherein the second polypeptide comprises: (i) a secretory signal, (ii) a Plasmodium CSP N-terminal region, (iii) a Plasmodium CSP N-terminal end region, (iv) a Plasmodium CSP junction region, (v) three repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223), (vi) a Plasmodium CSP major repeat region, (vii) a Plasmodium CSP C-terminal region, and (viii) a serine immediately following the Plasmodium CSP C-terminal region, and wherein the second polypeptide does not comprise a transmembrane region. [1208] Embodiment 289: The combination of embodiment 288, wherein the second polypeptide comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 8. [1209] Embodiment 290: The combination of any one of embodiments 1-86, wherein the second polypeptide comprises: (i) a secretory signal, (ii) a Plasmodium CSP N-terminal region, (iii) a Plasmodium CSP N-terminal end region, (iv) a Plasmodium CSP junction region, (v) three repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223), (vi) a Plasmodium CSP major repeat region, (vii) a Plasmodium CSP C-terminal region, and (viii) a serine immediately following the Plasmodium CSP C-terminal region, and wherein the second polypeptide does not comprise a transmembrane region. [1210] Embodiment 291: The combination of embodiment 290, wherein the second polypeptide comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 24. [1211] Embodiment 292: The combination of any one of embodiments 1-86, wherein the second polypeptide comprises: (i) a secretory signal, (ii) a Plasmodium CSP N-terminal region, (iii) a Plasmodium CSP N-terminal end region, (iv) a Plasmodium CSP junction region, (v) three repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223), (vi) a Plasmodium CSP major repeat region, (vii) a Plasmodium CSP C-terminal region, and (viii) a serine-valine sequence immediately following the Plasmodium CSP C-terminal region, and wherein the second polypeptide does not comprise a transmembrane region. [1212] Embodiment 293: The combination of embodiment 292, wherein the second polypeptide comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 99. [1213] Embodiment 294: The combination of any one of embodiments 1-86, wherein the second polypeptide comprises: (i) a secretory signal, (ii) a Plasmodium CSP N-terminal region, (iii) a Plasmodium CSP N-terminal end region, (iv) a Plasmodium CSP junction region, (v) three repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223), (vi) a Plasmodium CSP major repeat region, (vii) a Plasmodium CSP C-terminal region, and (viii) a transmembrane region. [1214] Embodiment 295: The combination of embodiment 294, wherein the second polypeptide comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 33. [1215] Embodiment 296: The combination of any one of embodiments 1-86, wherein the second polypeptide comprises: (i) a secretory signal, (ii) a Plasmodium CSP N-terminal region, (iii) a Plasmodium CSP N-terminal end region, (iv) a Plasmodium CSP junction region, (v) three repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223), (vi) a Plasmodium CSP major repeat region, (vii) a Plasmodium CSP C-terminal region, (viii) a serine-valine sequence immediately following the Plasmodium CSP C-terminal region, (ix) a linker, and (x) a multimerization region, and wherein the second polypeptide does not comprise a transmembrane region. [1216] Embodiment 297: The combination of embodiment 296, wherein the second polypeptide comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 42. [1217] Embodiment 298: The combination of any one of embodiments 1-86, wherein the second polypeptide comprises: (i) a secretory signal, (ii) a Plasmodium CSP N-terminal region, (iii) a Plasmodium CSP N-terminal end region, (iv) a Plasmodium CSP junction region, (v) three repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223), (vi) a Plasmodium CSP major repeat region, (vii) a Plasmodium CSP C-terminal region, (viii) a serine immediately following the Plasmodium CSP C-terminal region, (ix) a linker, and (x) a transmembrane region. [1218] Embodiment 299: The combination of embodiment 298, wherein the second polypeptide comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 48. [1219] Embodiment 300: The combination of any one of embodiments 1-86, wherein the second polypeptide comprises: (i) a secretory signal, (ii) a Plasmodium CSP N-terminal region, (iii) a Plasmodium CSP N-terminal end region, (iv) a Plasmodium CSP junction region, (v) three repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223), (vi) a Plasmodium CSP major repeat region, (vii) a Plasmodium CSP C-terminal region, (viii) a serine-valine sequence immediately following the Plasmodium CSP C-terminal region, (ix) a linker, (x) a transmembrane region. [1220] Embodiment 301: The combination of embodiment 300, wherein the second polypeptide comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 90. [1221] Embodiment 302: The combination of any one of embodiments 1-86, wherein the second polypeptide comprises: (i) a secretory signal, (ii) a Plasmodium CSP N-terminal region, (iii) a Plasmodium CSP N-terminal end region, (iv) a Plasmodium CSP junction region, (v) three repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223), (vi) a Plasmodium CSP major repeat region, (vii) a Plasmodium CSP C-terminal region, (viii) a serine immediately following the Plasmodium CSP C-terminal region, and (ix) a transmembrane region. [1222] E 303: The combination of embodiment 302, wherein the second polypeptide comprises or consists of a n amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 21. [1223] The combination of any one of embodiments 1-86, wherein the second polypeptide c omprises: (i) a secretory signal, (ii) an antigenic portion of a Plasmodium CSP major repeat region, (iii) a Plasmodium CSP C-terminal region, and (iv) a serine-valine immediately following the Plasmodium CSP C-terminal region. [1224] Embodiment 305: The combination of embodiment 304, wherein the second polypeptide comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 51. [1225] E i 306: The combination of any one of embodiments 1-86, wherein the second polypeptide co mprises: (i) a secretory signal, (ii) an antigenic portion of a Plasmodium CSP major repeat region, (iii) a Plasmodium CSP C-terminal region, (iv) a serine immediately following the Plasmodium CSP C-terminal region, (v) a linker, and (vi) a transmembrane region. [1226] Embodiment 307: The combination of embodiment 306, wherein the second polypeptide comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 54. [1227] Embodiment 308: The combination of any one of embodiments 1-86, wherein the one or more Plasmodium CSP polypeptide regions or portions thereof comprised in the second polypeptide comprise in N-terminus to C-terminus order: (i) three contiguous repeats of the amino acid sequence NANPNVDP (SEQ ID NO: 223); (ii) six contiguous repeats of the amino acid sequence NANP (SEQ ID NO: 230); (iii) three contiguous repeats of the amino acid sequence NANPNVDP (SEQ ID NO: 223); (iv) six contiguous repeats of the amino acid sequence NANP (SEQ ID NO: 230); and (v) three contiguous repeats of the amino acid sequence NANPNVDP (SEQ ID NO: 223). [1228] Embodiment 309: The combination of any one of embodiments 1-86, wherein the second polypeptide further comprises: (i) one or more Plasmodium CSP N-terminal regions or portions thereof, (ii) one or more Plasmodium CSP N-terminal end regions or portions thereof, (iii) one or more Plasmodium CSP junction regions, portions thereof, or variants thereof, (iv) one or more Plasmodium CSP C-terminal regions or portions thereof, or (v) a combination thereof. [1229] Embodiment 310: The combination of any one of embodiments 1-86, wherein the one or more Plasmodium CSP polypeptide regions or portions thereof comprised in the second polypeptide comprise in N-terminus to C-terminus order: (i) a Plasmodium CSP N-terminal end region or portion thereof, (ii) a Plasmodium CSP R1 region or portion thereof, (iii) a Plasmodium CSP junction region or portion thereof, (iv) three contiguous repeats of the amino acid sequence NANPNVDP (SEQ ID NO: 223); (v) six contiguous repeats of the amino acid sequence NANP (SEQ ID NO: 230); (vi) three contiguous repeats of the amino acid sequence NANPNVDP (SEQ ID NO: 223); (vii) six contiguous repeats of the amino acid sequence NANP (SEQ ID NO: 230); (viii) three contiguous repeats of the amino acid sequence NANPNVDP (SEQ ID NO: 223); and (ix) a Plasmodium CSP C-terminal region or portion thereof. [1230] Embodiment 311: The combination of any one of embodiments 308-310 wherein the second polypeptide further comprises a Plasmodium CSP GPI domain. [1231] Embodiment 312: The combination of any one of embodiments 308-311, wherein the Plasmodium CSP C-terminal region or portion thereof comprised in the second polypeptide comprises a substitution at a fucosylation site. [1232] Embodiment 313: The combination of any one of embodiments 1-86, wherein the one or more Plasmodium CSP polypeptide regions or portions thereof comprised in the second polypeptide comprise in N-terminus to C-terminus order three repeating domains, wherein each repeating domain comprises: (i) one or more Plasmodium CSP junction regions, portions thereof, or variants thereof, (ii) three contiguous repeats of the amino acid sequence NANPNVDP (SEQ ID NO: 223), and (iii) six contiguous repeats of the amino acid sequence NANP (SEQ ID NO: 230). [1233] Embodiment 314: The combination of any one of embodiments 1-86, wherein the one or more Plasmodium CSP polypeptide regions or portions thereof comprised in the second polypeptide comprise in N-terminus to C-terminus order three repeating domains, wherein each repeating domain comprises: (i) one or more Plasmodium R1 regions or portions thereof, (ii) one or more Plasmodium CSP junction regions, portions thereof, or variants thereof, (iii) three contiguous repeats of the amino acid sequence NANPNVDP (SEQ ID NO: 223), and (iv) six contiguous repeats of the amino acid sequence NANP (SEQ ID NO: 230). [1234] Embodiment 315: The combination of any one of embodiments 308-314, further comprising one or more linker sequences. [1235] Embodiment 316: The combination of embodiment 315, wherein the linker is a glycine-serine linker. [1236] Embodiment 317: The combination of any one of embodiments 308-316, wherein the second polypeptide comprises a linker sequence following each six contiguous repeats of the amino acid sequence NANP. [1237] Embodiment 318: The combination of any one of embodiments 1-86, wherein the second polypeptide comprises: (i) a secretory signal, (ii) a Plasmodium CSP N-terminal region, (iii) a Plasmodium CSP N-terminal end region, (iv) a Plasmodium CSP junctional region, (v) a Plasmodium CSP minor repeat region, (vi) an antigenic portion of a Plasmodium CSP major repeat region, and (vii) a Plasmodium CSP C-terminal region. [1238] Embodiment 319: The combination of embodiment 318, wherein the antigenic portion of a Plasmodium CSP major repeat region comprises or consists of eighteen repeats of the amino acid sequence of NANP. [1239] Embodiment 320: The combination of embodiment 318 or 319, wherein the second polypeptide comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the amino acid sequence according to SEQ ID NO: 117. [1240] Embodiment 321: The combination of embodiment 318, wherein the antigenic portion of a Plasmodium CSP major repeat region comprises of six repeats of the amino acid sequence of NANP (SEQ ID NO: 230). [1241] Embodiment 322: The combination of embodiment 319, wherein the antigenic portion of a Plasmodium CSP major repeat region further comprises an asparagine-alanine positioned immediately following the six repeats of the amino acid sequence of NANP (SEQ ID NO: 230). [1242] Embodiment 323: The combination of any one of embodiments 318, 319, 321 and 322, wherein the second polypeptide comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the amino acid sequence according to SEQ ID NO: 122. [1243] Embodiment 324: The combination of any one of embodiments 1-86, wherein the second polypeptide comprises: (i) a secretory signal, (ii) a Plasmodium CSP N-terminal region, (iii) a Plasmodium CSP N-terminal end region, (iv) a Plasmodium CSP junctional region, (v) a Plasmodium CSP minor repeat region, (vi) an antigenic portion of a Plasmodium CSP major repeat region, (vii) a Plasmodium CSP C-terminal region, and (viii) a transmembrane region. [1244] Embodiment 325: The combination of embodiment 324, wherein the antigenic portion of a Plasmodium CSP major repeat region comprises or consists of eighteen repeats of the amino acid sequence of NANP (SEQ ID NO: 230). [1245] Embodiment 326: The combination of embodiment 324 or 325, wherein the second polypeptide comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the amino acid sequence according to SEQ ID NO: 112. [1246] Embodiment 327: The combination any one of embodiments 1-86, wherein the second polypeptide comprises: (i) a secretory signal, (ii) a Plasmodium CSP N-terminal region, (iii) a Plasmodium CSP N-terminal end region, (iv) a linker, (v) a Plasmodium CSP junctional region, (vi) a Plasmodium CSP minor repeat region, (vii) an antigenic portion of a Plasmodium CSP major repeat region, (viii) a Plasmodium CSP C-terminal region, (ix) a linker, and (x) a transmembrane region. [1247] Embodiment 328: The combination of embodiment 327, wherein the antigenic portion of a Plasmodium CSP major repeat region comprises or consists of eighteen repeats of the amino acid sequence of NANP. [1248] Embodiment 329: The combination of embodiment 327 or 328, wherein the second polypeptide comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the amino acid sequence according to SEQ ID NO: 125. [1249] Embodiment 330: The combination of any one of embodiments 1-86, wherein the second polypeptide comprises: (i) a secretory signal, (ii) a Plasmodium CSP N-terminal region, (iii) a Plasmodium CSP N-terminal end region, (iv) a Plasmodium CSP junctional region, (v) a Plasmodium CSP minor repeat region, (vi) a Plasmodium CSP major repeat region, (vii) a linker, and (viii) a transmembrane region. [1250] Embodiment 331: The combination of embodiment 330, wherein the second polypeptide comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the amino acid sequence according to SEQ ID NO: 130. [1251] Embodiment 332: The combination of any one of embodiments 1-86, wherein the second polypeptide comprises: (i) a secretory signal, (ii) a Plasmodium CSP junctional region, (iii) a Plasmodium CSP minor repeat region, (iv) an antigenic portion of a Plasmodium CSP major repeat region, (v) a linker, (vi) an antigenic portion of a Plasmodium CSP C-terminal region, (vii) a serine-valine, (viii) a linker, and (ix) a multimerization region. [1252] Embodiment 333: The combination of embodiment 332, wherein the antigenic portion of a Plasmodium CSP major repeat region comprises of six repeats of the amino acid sequence of NANP. [1253] Embodiment 334: The combination of embodiment 333, wherein the antigenic portion of a Plasmodium CSP major repeat region further comprises an asparagine-alanine positioned immediately following the six repeats of the amino acid sequence of NANP (SEQ ID NO: 230). [1254] Embodiment 335: The combination of any one of embodiments 332-334, wherein the antigenic portion of a Plasmodium CSP C-terminal region comprises or consists of an amino acid sequence that is at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%, at least 90%, at least 95%, at least 98%, or 100% identical to the amino acid sequence of SEQ ID NO: 259. [1255] Embodiment 336: The combination of any one of embodiments 332-335, wherein the second polypeptide comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the amino acid sequence according to SEQ ID NO: 135. [1256] Embodiment 337: The combination of any one of embodiments 1-86, wherein the second polypeptide comprises: (i) a secretory signal, (ii) a Plasmodium CSP junctional region, (iii) a Plasmodium CSP minor repeat region, (iv) an antigenic portion of a Plasmodium CSP major repeat region, (v) a linker, (vi) an antigenic portion of a Plasmodium CSP C-terminal region, (vii) a serine-valine, (viii) a linker, and (ix) a self-aggregation region. [1257] Embodiment 338: The combination of embodiment 337, wherein the antigenic portion of a Plasmodium CSP major repeat region comprises of six repeats of the amino acid sequence of NANP (SEQ ID NO: 230). [1258] Embodiment 339: The combination of embodiment 337 or 338, wherein the antigenic portion of a Plasmodium CSP major repeat region further comprises an asparagine-alanine positioned immediately following the six repeats of the amino acid sequence of NANP (SEQ ID NO: 230). [1259] Embodiment 340: The combination of any one of embodiments 337-339, wherein the antigenic portion of a Plasmodium CSP C-terminal region comprises or consists of an amino acid sequence that is at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%, at least 90%, at least 95%, at least 98%, or 100% identical to the amino acid sequence of SEQ ID NO: 259. [1260] E 341: The combination of any one of embodiments 337-340, wherein the second polypeptide co mprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the amino acid sequence according to SEQ ID NO: 138. [1261] The combination of any one of embodiments 1-86, wherein the second polypeptide c omprises: (i) a secretory signal, (ii) a Plasmodium CSP junctional region, (iii) a Plasmodium CSP minor repeat region, (iv) an antigenic portion of a Plasmodium CSP major repeat region, (v) a linker, (vi) an antigenic portion of a Plasmodium CSP C-terminal region, (vii) a serine-valine, (viii) a linker, and (ix) a transmembrane region. [1262] Embodiment 343: The combination of embodiment 342, wherein the antigenic portion of a Plasmodium CSP major repeat region comprises of six repeats of the amino acid sequence of NANP (SEQ ID NO: 230). [1263] Embodiment 344: The combination of embodiment 343, wherein the antigenic portion of a Plasmodium CSP major repeat region further comprises an asparagine-alanine positioned immediately following the six repeats of the amino acid sequence of NANP (SEQ ID NO: 230). [1264] Embodiment 345: The combination of embodiment 343 or 344, wherein the antigenic portion of a Plasmodium CSP C-terminal region comprises or consists of an amino acid sequence that is at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%, at least 90%, at least 95%, at least 98%, or 100% identical to the amino acid sequence of SEQ ID NO: 259. [1265] Embodiment 346: The combination of any one of embodiments 343-345, wherein the second polypeptide comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the amino acid sequence according to SEQ ID NO: 141. [1266] Embodiment 347: The combination of any one of embodiments 1-86, wherein the second polypeptide comprises: (i) a secretory signal, (ii) a Plasmodium CSP N-terminal region, (iii) a Plasmodium CSP N-terminal end region, (iv) a Plasmodium CSP junctional region, (v) a Plasmodium CSP minor repeat region, (vi) a Plasmodium CSP major repeat region, (vii) a Plasmodium CSP C-terminal region variant, and (viii) a transmembrane region. [1267] E 348: The combination of embodiment 347, wherein the secretory signal comprises or consists of a P lasmodium secretory signal. [1268] Embodiment 349: The combination of embodiment 348, wherein the Plasmodium secretory signal comprises or consists of a Plasmodium CSP secretory signal. [1269] Embodiment 350: The combination of embodiment 349, wherein the Plasmodium CSP secretory signal comprises or consists of an amino acid sequence according to SEQ ID NO: 332. [1270] Embodiment 351: The combination of any one of embodiments 347-350, wherein the transmembrane region comprises or consists of a Plasmodium transmembrane region. [1271] Embodiment 352: The combination of embodiment 351, wherein the Plasmodium transmembrane region comprises or consists of a Plasmodium CSP glycosylphosphatidylinositol (GPI) anchor region. [1272] Embodiment 353: The combination of embodiment 352, wherein the Plasmodium CSP GPI anchor region comprises or consists of an amino acid sequence according to SEQ ID NO: 385. [1273] Embodiment 354: The combination of any one of embodiments 347-353, wherein the polypeptide comprises or consists of an amino acid sequence with at least 85% sequence identity to the amino acid sequence according to SEQ ID NO: 989. [1274] Embodiment 355: The combination of any one of embodiments 347-354, wherein the polypeptide comprises or consists of an amino acid sequence according to SEQ ID NO: 989. [1275] Embodiment 356: The combination of any one of embodiments 347-355, wherein the polyribonucleotide comprises or consists of a nucleic acid sequence with at least 85% sequence identity to the nucleic acid sequence according to SEQ ID NO: 991. [1276] Embodiment 357: The combination of any one of embodiments 347-356, wherein the polyribonucleotide comprises or consists of a nucleic acid sequence according to SEQ ID NO: 991. [1277] Embodiment 358: The combination of any one of the embodiments 1-86, wherein the second polypeptide comprises: (i) a secretory signal, (ii) an antigenic portion of a Plasmodium CSP N-terminal region, (iii) a first linker, (iv) a Plasmodium CSP N-terminal end region, (v) a Plasmodium CSP junctional region, (vi) a Plasmodium CSP minor repeat region, (vii) an antigenic portion of a Plasmodium CSP major repeat region, (viii) a Plasmodium CSP C-terminal region, (ix) a serine-valine sequence, (x) a second linker, and (xi) a transmembrane region. [1278] Embodiment 359: The combination of embodiment 358, wherein the secretory signal comprises or consists of a Plasmodium secretory signal. [1279] Embodiment 360: The combination of embodiment 359, wherein the Plasmodium secretory signal comprises or consists of a Plasmodium CSP secretory signal. [1280] Embodiment 361: The combination of embodiment 360, wherein the Plasmodium CSP secretory signal comprises or consists of an amino acid sequence according to SEQ ID NO: 332. [1281] Embodiment 362: The combination of any one of embodiments 358-361, wherein the transmembrane region comprises or consists of an HSV transmembrane region. [1282] Embodiment 363: The combination of embodiment 362, wherein the HSV transmembrane region comprises or consists of an HSV-1 or HSV-2 transmembrane region. [1283] Embodiment 364: The combination of embodiment 362 or 363, wherein the HSV transmembrane region comprises or consists of an HSV gD transmembrane region. [1284] Embodiment 365: The combination of embodiment 364, wherein the HSV gD transmembrane region comprises or consists of an amino acid sequence according to SEQ ID NO: 379. [1285] Embodiment 366: The combination of any one of embodiments 358-365, wherein the antigenic portion of a Plasmodium CSP N-terminal region comprises or consists of an amino acid sequence that is at least 85%, at least 90%, at least 95%, at least 98%, or 100% identical to the amino acid sequence of according to SEQ ID NO: 1010. [1286] Embodiment 367: The combination of any one of embodiments 358-366, wherein the antigenic portion of a Plasmodium CSP major repeat region comprises or consists of eighteen repeats of the amino acid sequence of NANP. [1287] Embodiment 368: The combination of any one of embodiments 358-367, wherein the polypeptide comprises or consists of an amino acid sequence with at least 85% sequence identity to the amino acid sequence according to SEQ ID NO: 997. [1288] Embodiment 369: The combination of any one of embodiments 358-368, wherein the polypeptide comprises or consists of an amino acid sequence according to SEQ ID NO: 997. [1289] Embodiment 370: The combination of any one of embodiments 358-369, wherein the polyribonucleotide comprises or consists of a nucleic acid sequence with at least 85% sequence identity to the nucleic acid sequence according to SEQ ID NO: 999. [1290] Embodiment 371: The combination of any one of embodiments 358-370, wherein the polyribonucleotide comprises or consists of a nucleic acid sequence according to SEQ ID NO: 999. [1291] Embodiment 372: The combination of any one of the embodiments 1-86, wherein the second polypeptide comprises: (i) a secretory signal, (ii) an antigenic portion of a Plasmodium CSP N-terminal region, (iii) a first linker, (iv) a Plasmodium CSP N-terminal end region, (v) a Plasmodium CSP junctional region, (vi) a Plasmodium CSP minor repeat region, (vii) an antigenic portion of a Plasmodium CSP major repeat region, (viii) a second linker, (ix) an antigenic portion of a Plasmodium CSP C-terminal region, (x) a serine-valine sequence, (xi) a third linker, and (xii) a transmembrane region. [1292] Embodiment 373: The combination of embodiment 372, wherein the secretory signal comprises or consists of a Plasmodium secretory signal. [1293] Embodiment 374: The combination of embodiment 373, wherein the Plasmodium secretory signal comprises or consists of a Plasmodium CSP secretory signal. [1294] Embodiment 375: The combination of embodiment 374, wherein the Plasmodium CSP secretory signal comprises or consists of an amino acid sequence according to SEQ ID NO: 332. [1295] The combination of any one of embodiments 372-375, wherein the transmembra ne region comprises or consists of an HSV transmembrane region. [1296] Embodiment 377: The combination of embodiment 376, wherein the HSV transmembrane region comprises or consists of an HSV-1 or HSV-2 transmembrane region. [1297] Embodiment 378: The combination of embodiment 376 or 377, wherein the HSV transmembrane region comprises or consists of an HSV gD transmembrane region. [1298] Embodiment 379: The combination of embodiment 378, wherein the HSV gD transmembrane region comprises or consists of an amino acid sequence according to SEQ ID NO: 379. [1299] Embodiment 380: The combination of any one of embodiments 372-379, wherein the antigenic portion of a Plasmodium CSP N-terminal region comprises or consists of an amino acid sequence that is at least 85%, at least 90%, at least 95%, at least 98%, or 100% identical to the amino acid sequence of according to SEQ ID NO: 1010. [1300] Embodiment 381: The combination of any one of embodiments 372-380, wherein the antigenic portion of a Plasmodium CSP C-terminal region comprises or consists of an amino acid sequence that is at least 85%, at least 90%, at least 95%, at least 98%, or 100% identical to the amino acid sequence of SEQ ID NO: 259. [1301] The combination of any one of embodiments 372-381, wherein the antigenic portion of a Plasmodium CSP major repeat region comprises or consists of eighteen repeats of the amino acid sequence of NANP. [1302] Embodiment 383: The combination of any one of embodiments 372-382, wherein the polypeptide comprises or consists of an amino acid sequence with at least 85% sequence identity to the amino acid sequence according to SEQ ID NO: 1000. [1303] Embodiment 384: The combination of any one of embodiments 372-383, wherein the polypeptide comprises or consists of an amino acid sequence according to SEQ ID NO: 1000. [1304] Embodiment 385: The combination of any one of embodiments 372-384, wherein the polyribonucleotide comprises or consists of a nucleic acid sequence with at least 85% sequence identity to the nucleic acid sequence according to SEQ ID NO: 1002. [1305] Embodiment 386: The combination of any one of embodiments 372-384, wherein the polyribonucleotide comprises or consists of a nucleic acid sequence according to SEQ ID NO: 1002. [1306] Embodiment 387: The combination of any one of embodiments 372-381, wherein the antigenic portion of a Plasmodium CSP major repeat region comprises six repeats of the amino acid sequence of NANP. [1307] Embodiment 388: The combination of embodiment 387, wherein the antigenic portion of a Plasmodium CSP major repeat region further comprises an asparagine-alanine positioned immediately following the six repeats of the amino acid sequence of NANP. [1308] Embodiment 389: The combination of any one of embodiments 372-381, 387, and 388, wherein the polypeptide comprises or consists of an amino acid sequence with at least 85% sequence identity to the amino acid sequence according to SEQ ID NO: 1003. [1309] Embodiment 390: The combination of any one of embodiments 372-381 and 387-389, wherein the polypeptide comprises or consists of an amino acid sequence according to SEQ ID NO: 1003. [1310] Embodiment 391: The combination of any one of embodiments 372-381 and 387-390, wherein the polyribonucleotide comprises or consists of a nucleic acid sequence with at least 85% sequence identity to the nucleic acid sequence according to SEQ ID NO: 1005. [1311] Embodiment 392: The combination of any one of embodiments 372-381 and 387-391, wherein the polyribonucleotide comprises or consists of a nucleic acid sequence according to SEQ ID NO: 1005. [1312] Embodiment 393: The combination of embodiments 241-392, wherein, when present, the features are in the second polypeptide in numerical order from the C-terminus to the N-terminus. [1313] Embodiment 394: The combination of embodiment 1, wherein: (a) the first polypeptide comprises: (i) an antigenic Plasmodium CSP polypeptide fragment, (ii) an antigenic Plasmodium TRAP polypeptide fragment, (iii) an antigenic Plasmodium UIS3 polypeptide fragment, (iv) an antigenic Plasmodium ETRAMP10.3 polypeptide fragment, and (v) an antigenic Plasmodium LSAP2 polypeptide fragment; and (b) the second polypeptide comprises: (i) a secretory signal, (ii) a Plasmodium CSP N-terminal region, (iii) a Plasmodium CSP N-terminal end region, (iv) a Plasmodium CSP junction region, (v) three repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223), (vi) a Plasmodium CSP major repeat region, (vii) a Plasmodium CSP C-terminal region, and (viii) a transmembrane region. [1314] Embodiment 395: The combination of embodiment 394, wherein the first polypeptide comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 203. [1315] Embodiment 396: The combination of embodiment 394 or 395, wherein the second polypeptide comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 33. [1316] Embodiment 397: The combination of any one of embodiments 394-396, wherein the combination further comprises a third pharmaceutical composition comprising a third polyribonucleotide, wherein the third polyribonucleotide encodes a third polypeptide, and the third polypeptide comprises: (i) an antigenic Plasmodium LSA-1(a) polypeptide fragment, (ii) an antigenic Plasmodium LSA-1(b) polypeptide fragment, (iii) an antigenic Plasmodium LISP-2 polypeptide fragment, and (iv) an antigenic Plasmodium LISP-1 polypeptide fragment. [1317] Embodiment 398: The combination of embodiment 397, wherein the third polypeptide comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 209. [1318] Embodiment 399: The combination of embodiment 1, wherein: (a) the first polypeptide comprises: (i) an antigenic Plasmodium CSP polypeptide fragment, (ii) an antigenic Plasmodium TRAP polypeptide fragment, (iii) an antigenic Plasmodium UIS3 polypeptide fragment, (iv) an antigenic Plasmodium ETRAMP10.3 polypeptide fragment, and (v) an antigenic Plasmodium LSAP2 polypeptide fragment; and (b) the second polyribonucleotide comprises: (i) a secretory signal, (ii) a Plasmodium CSP N-terminal end region, (iii) a Plasmodium CSP junction region, (iv) nine repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223), (v) a Plasmodium CSP C-terminal region, (vi) a serine-valine sequence immediately following the Plasmodium CSP C-terminal region, (vii) a linker, and (viii) a transmembrane region, and wherein the second polypeptide does not comprise any of: (a) a Plasmodium CSP N-terminal region or portion thereof, and (b) an amino acid sequence of NPNA (SEQ ID NO: 228). [1319] Embodiment 400: The combination of embodiment 399, wherein the first polypeptide comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 203. [1320] Embodiment 401: The combination of embodiment 399 or 400, wherein the second polypeptide comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 81. [1321] Embodiment 402: The combination of embodiment 1, wherein: (a) the first polypeptide comprises: (i) an antigenic Plasmodium LSA-1(a) polypeptide fragment, (ii) an antigenic Plasmodium LSA-1(b) polypeptide fragment, (iii) an antigenic Plasmodium LISP-2 polypeptide fragment, and (iv) an antigenic Plasmodium LISP-1 polypeptide fragment; and (b) the second polyribonucleotide comprises: (i) a secretory signal, (ii) a Plasmodium CSP N-terminal region, (iii) a Plasmodium CSP N-terminal end region, (iv) a Plasmodium CSP junction region, (v) three repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223), (vi) a Plasmodium CSP major repeat region, (vii) a Plasmodium CSP C-terminal region, and (viii) a transmembrane region. [1322] Embodiment 403: The combination of embodiment 402, wherein the first polypeptide comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 209. [1323] E i 404: The combination of embodiment 402 or 403, wherein the second polypeptide comprises or c onsists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 33. [1324] Embodiment 405: The combination of embodiment 1, wherein: (a) the first polypeptide comprises: (i) an antigenic Plasmodium LSA-1(a) polypeptide fragment, (ii) an antigenic Plasmodium LSA-1(b) polypeptide fragment, (iii) an antigenic Plasmodium LISP-2 polypeptide fragment, and (iv) an antigenic Plasmodium LISP-1 polypeptide fragment; and (b) the second polyribonucleotide comprises: (i) a secretory signal, (ii) a Plasmodium CSP N-terminal end region, (iii) a Plasmodium CSP junction region, (iv) nine repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223), (v) a Plasmodium CSP C-terminal region, (vi) a serine-valine sequence immediately following the Plasmodium CSP C-terminal region, (vii) a linker, and (viii) a transmembrane region, and wherein the second polypeptide does not comprise any of: (a) a Plasmodium CSP N-terminal region or portion thereof, and (b) an amino acid sequence of NPNA (SEQ ID NO: 228). [1325] Embodiment 406: The combination of embodiment 405, wherein the first polypeptide comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 209. [1326] Embodiment 407: The combination of embodiment 405 or 406, wherein the second polypeptide comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 81. [1327] Embodiment 408: The combination of any one of embodiments 1-407, wherein Plasmodium is Plasmodium falciparum. [1328] Embodiment 409: The combination of any one of embodiments 1-408, wherein the one or more Plasmodium CSP polypeptide regions or portions thereof are one or more P. falciparum CSP polypeptide regions or portions thereof. [1329] Embodiment 410: The combination of any one of embodiments 1-409, wherein the one or more Plasmodium T-cell antigens are one or more P. falciparum T-cell antigens. [1330] Embodiment 411: The combination of embodiment 408 or 410, wherein Plasmodium falciparum is Plasmodium falciparum isolate 3D7. [1331] Embodiment 412: The combination of any one of embodiments 1-411, wherein the first polyribonucleotide and/or second polyribonucleotide is an isolated polyribonucleotide. [1332] Embodiment 413: The combination of embodiment 397 or 398, wherein the third polyribonucleotide is an isolated polyribonucleotide. [1333] Embodiment 414: The combination of any one of embodiments 1-413, wherein the first polyribonucleotide and/or second polyribonucleotide is an engineered polyribonucleotide. [1334] Embodiment 415: The combination of embodiment 397 or 398, wherein the third polyribonucleotide is an engineered polyribonucleotide. [1335] Embodiment 416: The combination of any one of embodiments 1-415, wherein the first polyribonucleotide and/or second polyribonucleotide is a codon-optimized polyribonucleotide. [1336] Embodiment 417: The combination of embodiment 397 or 398, wherein the third polyribonucleotide is a codon-optimized polyribonucleotide. [1337] Embodiment 418: The combination of any one of embodiments 1-417, wherein the first polyribonucleotide is comprised in a first RNA construct, wherein the first RNA construct comprises in 5' to 3' order: (i) a 5' UTR; (ii) the first polyribonucleotide; (iii) a 3' UTR; and (iv) a polyA tail sequence. [1338] Embodiment 419: The combination of any one of embodiments 1-418, wherein the second polyribonucleotide is comprised in a second RNA construct, wherein the second RNA construct comprises in 5' to 3' order: (i) a 5' UTR; (ii) the second polyribonucleotide; (iii) a 3' UTR; and (iv) a polyA tail sequence. [1339] Embodiment 420: The combination of embodiment 418 or 419, wherein (i) the 5' UTR of the first and/or second RNA construct comprises or consists of a modified human alpha-globin 5'-UTR; and (ii) the 3' UTR of the first and/or second RNA construct comprises or consists of a first sequence from the amino terminal enhancer of split (AES) messenger RNA and a second sequence from the mitochondrial encoded 12S ribosomal RNA. [1340] Embodiment 421: The combination of any one of embodiments 418-420, wherein the 5' UTR of the first and/or second RNA construct consists of a ribonucleic acid sequence according to SEQ ID NO: 565. [1341] Embodiment 422: The combination of any one of embodiments 418-421, wherein the 3' UTR of the first and/or second RNA construct consists of a ribonucleic acid sequence according to SEQ ID NO: 567. [1342] Embodiment 423: The combination of any one of embodiments 418-422, wherein the polyA tail sequence of the first and/or second RNA construct is a split polyA tail sequence. [1343] Embodiment 424: The combination of embodiment 423, wherein the split polyA tail sequence consists of a ribonucleic acid sequence according to SEQ ID NO: 569. [1344] Embodiment 425: The combination of any one of embodiments 418-424, wherein the first and/or second RNA construct further comprise a 5' cap. [1345] Embodiment 426: The combination of any one of embodiments 418-425, wherein the first and/or second RNA construct comprise a cap proximal sequence comprising positions +1, +2, +3, +4, and +5 of the polyribonucleotide. [1346] Embodiment 427: The combination of embodiment 425 or 426, wherein the 5' cap comprises or consists of m7(3’OMeG)(5')ppp(5')(2'OMeA₁)pG₂, wherein A₁ is position +1 of the polyribonucleotide, and G₂ is position +2 of the polyribonucleotide. [1347] Embodiment 428: The combination of embodiment 426 or 427, wherein the cap proximal sequence comprises A₁ and G₂ of the Cap1 structure, and a sequence comprising: A₃A₄U₅ (SEQ ID NO: 571) at positions +3, +4 and +5 respectively of the polyribonucleotide. [1348] Embodiment 429: The combination of any one of embodiments 1-428, wherein the first and/or second RNA construct includes modified uridines in place of all uridines. [1349] Embodiment 430: The combination of embodiment 429, wherein modified uridines are each N1- methyl-pseudouridine. [1350] Embodiment 431: The combination of any one of embodiments 1-430, wherein the first and/or second pharmaceutical composition further comprises lipid nanoparticles, polyplexes (PLX), lipidated polyplexes (LPLX), or liposomes. [1351] Embodiment 432: The combination of embodiment 431, wherein the first and/or second polyribonucleotide is fully or partially encapsulated within the lipid nanoparticles, polyplexes (PLX), lipidated polyplexes (LPLX), or liposomes. [1352] Embodiment 433: The combination of any one of embodiments 1-432, wherein the first and/or second pharmaceutical composition further comprises lipid nanoparticles. [1353] Embodiment 434: The combination of any one of embodiments 431-433, wherein the first polyribonucleotide is encapsulated within the lipid nanoparticles. [1354] Embodiment 435: The combination of any one of embodiments 431-434, wherein the second polyribonucleotide is encapsulated within the lipid nanoparticles. [1355] Embodiment 436: The combination of any one of embodiments 1-435, wherein the first and/or second pharmaceutical composition comprises at least one pharmaceutically acceptable excipient. [1356] Embodiment 437: The combination of any one of embodiments 1-436 for use in the treatment of a malaria infection. [1357] Embodiment 438: The combination of any one of embodiments 1-436 for use in the prevention of a malaria infection. [1358] Embodiment 439: A method comprising administering a combination of any one of embodiments 1- 436 to a subject. [1359] Embodiment 440: The method of embodiment 439, wherein the method is a method of treating a malaria infection. [1360] Embodiment 441: The method of embodiment 439 or 440, wherein the method is a method of preventing a malaria infection. [1361] Embodiment 442: The method of any one of embodiments 439-441, wherein the subject has or is at risk of developing a malaria infection. [1362] Embodiment 443: The method of any one of embodiments 439-442, wherein the subject is a human. [1363] Embodiment 444: The method of any one of embodiments 439-443, wherein administration induces an anti-malaria immune response in the subject. [1364] Embodiment 445: Use of the combination of any one of embodiments 1-436 in the treatment of a malaria infection. [1365] Embodiment 446: Use of the combination of any one of embodiments 1-436 in the prevention of a malaria infection. EXEMPLIFICATION Example 1: Exemplary Polyribonucleotides encoding Plasmodium Polypeptide Constructs [1366] In the present example, each of the following malaria proteins were identified as of particular interest: CSP, TRAP, LSAP1, LSAP2 UIS3, ETRAMP10.3, LISP1, LISP2, LSA-3, LSA-1, EXP1 and combinations thereof. Polyribonucleotides encoding various Plasmodium CSP polypeptide constructs depicted in Table 4 were generated, and the polyribonucleotides (“RNA constructs”) were numbered according to the corresponding encoded construct number shown in Table 4. As indicated with Table 4 above, as used herein, an “ERMA” construct is an “RNA construct,” and for example, “ERMA 1” corresponds to “RNA Construct 1,” “ERMA 2” corresponds to “RNA Construct 2,” etc. Exemplary polyribonucleotides are shown in Table 11. Polyribonucleotides encoding various Plasmodium T- cell string polypeptide constructs depicted in Table 3 were generated, and the polyribonucleotides (“RNA constructs”) were numbered according to the corresponding encoded construct number shown in Table 3. As indicated in Table 3, as used herein, an “ERMA” construct is an “RNA construct,” and for example, “ERMA 14” corresponds to “RNA Construct 14,” “ERMA 15” corresponds to “RNA Construct 15,” etc. In addition, some constructs have also additional “Mas” identifiers as indicated in Table 3 and in FIG.3. Exemplary polyribonucleotides are shown in Table 9 and 10. FIG.3 provides an overview of exemplary polyribonucleotides encoding various Plasmodium T-cell string polypeptide as described herein. [1367] ERMA 48 and ERMA 55 (Mas3a) encode identical Plasmodium T-cell antigens and differ only in their secretory signals; ERMA 49 and ERMA 56 (Mas3b) encode identical Plasmodium T-cell antigens and differ only in their secretory signals. [1368] ERMA 23 and ERMA23-7 differ in their sequence optimization, i.e., have different DNA and RNA sequences, but otherwise encode an identical CSP polypeptide construct, i.e., have the same amino acid sequence. In vitro studies (data not shown) have confirmed that both ERMA 23 and ERMA 23-7 have identical or very closely comparable results for transfection rates, total expression, cell viability, endpoint titers of antibodies elicited on day 21 (pre-boost) and on day 35 (after boost) against PfCSP after immunization of mice as described here, epitope specificity of antibodies elicited upon immunization of mice as determined using a multiplex assay as described herein, and pro-inflammatory response of IFNɣ, IFNɣ in combination with IL-2, IFNɣ in combination with IL-2 and TNFα from T cells after immunization of mice as described herein. Example 2: In vitro expression of Exemplary Polyribonucleotides Encoding Plasmodium T-Cell String Polypeptide Constructs [1369] In vitro expression studies using a MS-readout indicate that Mas3a and Mas 4f are expressed upon transfection into a human cell line. [1370] Briefly, HEK293T cells were co-transfected with 2.5 μg of each Mas3a and Mas 4f constructs and harvested 24 h later. Cells were lysed in 8M urea, total protein content was normalized across samples, and disulfide bonds were reduced and alkylated. Proteins in the lysate were digested with LysC and Trypsin prior to C18 cleanup and parallel reaction monitoring analysis by MS. Heavy-isotopically labeled tryptic peptides were added to the sample prior to analysis to aid in the identification of Mas3a and Mas 4f-derived tryptic peptides. [1371] Both Mas3a and Mas 4f are detected upon transfection of the combination into HEK293T cells (FIG.4). [1372] In conclusion, in vitro expression (FIG.3) and immunopeptidomics (FIG.2) studies have confirmed that Mas3a and Mas4f are expressed and generate epitopes presented on HLA complexes when transfected into human cell lines. Example 3: Immunogenicity Studies of Exemplary Polyribonucleotides Encoding Plasmodium T-Cell String Polypeptide Constructs ERMA 48 and MAS4f [1373] The present Example documents the ability of certain polyribonucleotides encoding Plasmodium T-Cell string polypeptide constructs, provided by the present disclosure, to induce a T cell response, as assessed in mice. [1374] Provided polyribonucleotides encoding T-cell string polypeptide constructs can be assessed for their ability to induce a T-cell mediated immune response. In some embodiments, a T-cell string polypeptide construct is determined to induce a useful immune response if splenocytes from a subject (e.g., a mouse) immunized with such construct, following incubation with peptide(s) as described herein, exhibit secretion of a pro-inflammatory cytokines (e.g., IFN-γ) in an Enzyme-linked immunospot (ELISpot), as described herein. [1375] HLA-A2.1 mice were divided into multiple groups receiving treatment and were immunized intramuscularly (IM) with 2.5 μg or 5 μg of a T-cell string polypeptide construct or a combination of two T cell string polypeptide constructs (each 2.5 μg) or injected with vehicle. At the end of the experiment (day 7), splenocytes were harvested and cryopreserved. Splenocytes were incubated overnight with construct specific antigen peptide pools (See Table 16 and Table 17), using the Mouse IFN-γ ELISpot Kit (R&D Systems, EL485) following the manufacturer’s instructions, and assessed for IFN-γ responses. Specifically, splenocytes were incubated with individual antigen peptide pools (0.3 μM of each peptides within antigen pool) in 200 μl serum-free media (X- VIVO/1% Pen-Strep/1% Glutamax), for 20 hrs at 37 C in blocked pre-coated ELISpot plates in triplicate wells. Negative control included incubation with serum-free media and DMSO (matched volume to peptide pool) and positive control included incubation with 0.3 μM Concanavalin A (ConA). Post incubation, plates were washed with PBS/Tween and detection antibody (biotinylated anti- IFN-γ) was added to wells for overnight incubation at 4 C. Following incubation with the detection antibody, plates were washed with PBS/Tween and incubated with Streptavidin-AP for 2 hours at room temperature. Plates were then washed with PBS/Tween and 100 μl of BCIP/NBT Chromogen substrate was added to each well and incubated for 45 minutes at room temperature, protected from light. Chromagen solution was decanted from plates, wells were rinsed with distilled water and plates were air dried. Cell counts were recorded per well using a CTL Immunospot reader. Table 16: Peptides used for splenocyte stimulation in the ELISpot Assay

Table 17: Peptide pools tested for each T-cell string polypeptide constructs [1376] Results are in FIG.5. As shown in FIG.5A and FIG.5B, upon stimulation with construct specific antigen peptide pools, IFN- γ producing cells were detected in splenocytes from mice immunized with T-cell string polypeptide construct MAS4f. Splenocytes from mice immunized with either 2.5μg or 5 μg T-cell string polypeptide construct MAS4f had an average of at least about 1000 spots per million after stimulation with a LISP1 peptide pool. Splenocytes from mice immunized with either 2.5μg or 5 μg T-cell string polypeptide construct MAS4f had an average of at least about 250 spots per million after stimulation with a LISP2 peptide pool. Splenocytes from mice immunized with 5 μg T-cell string polypeptide construct MAS4f had an average of at least about 500 spots per million after stimulation with a LISP2 peptide pool, while splenocytes from mice immunized with 2.5 μg T-cell string polypeptide construct MAS4f had an average of at least about 500 spots per million after stimulation with a LSA1a peptide pool. Splenocytes from mice immunized with either 2.5μg or 5 μg T-cell string polypeptide construct MAS4f had an average of at least about 250 spots per million after stimulation with a LSA1b peptide pool. In contrast, upon stimulation with construct specific antigen peptide pools detection of IFN- γ producing cells, there was almost no detection of IFN- γ producing cells in splenocytes from mice treated with vehicle. As shown in FIG.5E, there was a near linear relationship between IFN- γ producing cells detected in splenocytes from mice immunized with ether 2.5μg or 5 μg T- cell string polypeptide construct MAS4f after stimulation with construct specific antigen peptide pools. These experiments indicate that IFN-γ response could be induced at a lower dose (i.e., 2.5μg) of T-cell string polypeptide string construct MAS4f. [1377] As shown in FIG.5C, upon stimulation with construct specific antigen peptide pools, IFN- γ producing cells were detected in splenocytes from mice immunized with T-cell string polypeptide construct ERMA 48. Splenocytes from mice immunized with 5 μg T-cell string polypeptide construct ERMA 48 had an average of at least about 100 spots per million after stimulation with a LISP1 peptide pool. Splenocytes from mice immunized with 5 μg T-cell string polypeptide construct ERMA 48 had an average of at least about 400 spots per million after stimulation with a LSAP2 peptide pool. Splenocytes from mice immunized with 5 μg T-cell string polypeptide construct ERMA 48 had an average of at least about 600 spots per million after stimulation with a TRAP peptide pool. Splenocytes from mice immunized with 5 μg T-cell string polypeptide construct ERMA 48 had an average of at least about 400 spots per million after stimulation with a UIS3 peptide pool. Splenocytes from mice immunized with 5 μg T-cell string polypeptide construct ERMA 48 had an average of at least about 100 spots per million after stimulation with a ETRAMP10.3 peptide pool. In contrast, upon stimulation with construct specific antigen peptide pools, there was almost no detection of IFN- γ producing cells in splenocytes from mice treated with vehicle. [1378] As shown in FIG.5D, upon stimulation with construct specific antigen peptide pools, IFN- γ producing cells were detected in splenocytes from mice immunized with a combination of T-cell string polypeptide constructs ERMA 48 and MAS4f. Splenocytes from mice immunized with 5 μg T-cell string polypeptide construct ERMA 48 and 5 μg T-cell string polypeptide construct MAS4f had an average of at least about 100 spots per million after stimulation with a CSP peptide pool. Splenocytes from mice immunized with 5 μg T-cell string polypeptide construct ERMA 48 and 5 μg T-cell string polypeptide construct MAS4f had an average of at least about 1500 spots per million after stimulation with a LISP1 peptide pool. Splenocytes from mice immunized with 5 μg T-cell string polypeptide construct ERMA 48 and 5 μg T-cell string polypeptide construct MAS4f had an average of at least about 500 spots per million after stimulation with a LISP2 peptide pool. Splenocytes from mice immunized with 5 μg T-cell string polypeptide construct ERMA 48 and 5 μg T-cell string polypeptide construct MAS4f had an average of at least about 100 spots per million after stimulation with a LSA1a peptide pool. Splenocytes from mice immunized with 5 μg T-cell string polypeptide construct ERMA 48 and 5 μg T-cell string polypeptide construct MAS4f had an average of at least about 1000 spots per million after stimulation with a LSA1b peptide pool. Splenocytes from mice immunized with 5 μg T-cell string polypeptide construct ERMA 48 and 5 μg T-cell string polypeptide construct MAS4f had an average of at least about 1000 spots per million after stimulation with a LSAP2 peptide pool. Splenocytes from mice immunized with 5 μg T-cell string polypeptide construct ERMA 48 and 5 μg T-cell string polypeptide construct MAS4f had an average of at least about 500 spots per million after stimulation with a TRAP peptide pool. Splenocytes from mice immunized with 5 μg T-cell string polypeptide construct ERMA 48 and 5 μg T-cell string polypeptide construct MAS4f had an average of at least about 500 spots per million after stimulation with a UIS3 peptide pool. Splenocytes from mice immunized with 5 μg T-cell string polypeptide construct ERMA 48 and 5 μg T-cell string polypeptide construct MAS4f had an average of at least about 100 spots per million after stimulation with a ETRAMP10.3 peptide pool. In contrast, upon stimulation with construct specific antigen peptide pools, there was almost no detection of IFN- γ producing cells in splenocytes from mice treated with vehicle. As shown in FIG.5F, upon stimulation with construct specific antigen peptide pools, detection of IFN- γ producing cells was similar in splenocytes from mice immunized with either a combination of T-cell string polypeptide constructs (e.g., ERMA 48 and MAS4f) or individual T-cell string polypeptide constructs (e.g., ERMA 48 or MAS4f). [1379] Thus, the present Example demonstrates that certain T-cell string polypeptide constructs effectively induce an immune response characterized by activation of T-cells secreting pro-inflammatory cytokines (e.g., IFN-γ), e.g., assessed using a ELISpot assay. [1380] As an additional control, T-cell responses induced upon administration of Mas3a and Mas4aMas4f were assessed using two additional versions of codon-optimized polyribonucleotides encoding the same polypeptides as Mas3a (labeled Mas3a-2 and Mas3a-3) and Mas4f (labeled Mas4f-2 and Mas4f-3). Table 18 (Day 7) and Table 19 (Day 35) overview immunization schedules for T cell immunogenicity studies. At Day 7 and 35 post-immunization, antigen-specific IFNɣ T-cell responses above levels observed in a vehicle control group (saline) were detected for all versions of Mas3a and Mas4f encoding polynucleotides tested (FIGS.63A-63D). Results in FIG.63A and 63B were obtained following the single immunization protocol described in Table 18 at day 7. Results in FIG. 63C and 63D were obtained following the prime boost immunization protocol described in Table 19 at day 35. A Day 7 and 35 representative example is shown in FIG.63B and FIG.63D respectively for mice that were administered Mas3a-3 and Mas4f-3 at a 1ug dose each. Table 18: General study plan for Day 7 T cell immunogenicity studies with CSP constructs. Table 19: General study plan for Day 35 T cell immunogenicity studies with CSP constructs. [1381] Additionally, antigen-specific IFNɣ and IL-2 T-cell responses were assessed (as described in example 6) upon administration of (1) Mas3a and Mas4f, (2) Mas3a-2 and Mas4f-2, and (3) Mas3a-3 and Mas4f-3. Antigen- specific IFNɣ and IL-2 T-cell responses above levels observed in a vehicle control group (saline) were detected for Mas3a and Mas4f, as well as Mas3a-2, Mas3a-3, Mas4f-2, and Mas4f-3. (FIGS.64A-64D). [1382] As demonstrated in the present Example, cellular responses elicited by Mas3a and Mas4f were not impaired by combination with ERMA 23-7 or by codon optimization of their polyribonucleotide sequences. Example 4: Immunogenicity Studies of Exemplary Additional Polyribonucleotides Encoding Plasmodium T-Cell String Polypeptide Constructs [1383] The present example further demonstrates the ability of certain polyribonucleotides encoding Plasmodium T-cell string polypeptide constructs, provided by the present disclosure, to induce a T cell response, as assessed in mice. [1384] HLA-A2.1 mice were divided into multiple groups and were immunized at day 0 intramuscularly (IM) with 2.5 μg (for Mas3a and Mas4f) or 5 μg (for Mas4a, Mas4b, Mas4c, and Mas4d) of a T-cell string polypeptide construct, with 2.5 μg Mas3a and 2.5 μg Mas4f, or injected with vehicle. At the end of the experiment (day 7), serum was obtained and splenocytes were harvested and cryopreserved. Splenocytes were incubated overnight with construct specific antigen peptide pools (listed in Table 16 and Table 17), using the Mouse IFN-γ ELISpot Kit (R&D Systems, EL485) following the manufacturer’s instructions, and assessed for IFN-γ responses. [1385] Results are shown in FIG.6. As shown in FIG.6A, IFN- γ producing cells were not detected in splenocytes from mice treated with vehicle, upon stimulation with CSP, LISP1, LISP2, LSA1a, LSA1b, LSAP2, TRAP, UIS3, or ETRAMP10.3 peptide pools. Splenocytes from mice immunized with tested T-cell string polypeptide construct were considered to be responsive if after stimulation with construct specific peptide pools there was a significant difference (as determined by a p value of at least 0.05) in detection of IFN- γ producing cells, as compared to splenocytes from mice treated with vehicle. [1386] As shown in FIG.6B, statistically significant IFN- γ producing cells were detected in splenocytes from mice immunized with 5 μg T-cell string polypeptide construct MAS4a, upon stimulation with LISP1, LISP2, LSA1b, LSAP2, TRAP or UIS3 peptide pools, but not with CSP, LSA1a, or ETRAMP10.3. Splenocytes from mice immunized with tested T-cell string polypeptide construct MAS4a had an average of at least about 10² spots per million after stimulation with LISP1, LISP2, LSA1b, LSAP2, TRAP, and UIS3 peptide pools. Splenocytes from mice immunized with tested T-cell string polypeptide construct MAS4a had the highest response after stimulation with LISP1 with an average of about 10³ spots per million. [1387] As shown in FIG.6C, statistically significant IFN- γ producing cells were detected in splenocytes from mice immunized with 5 μg T-cell string polypeptide construct MAS4b, upon stimulation with LISP1, LSAP2, TRAP or UIS3 peptide pools, but not with CSP, LSA1a, LSA1b or ETRAMP10.3. Splenocytes from mice immunized with tested T-cell string polypeptide construct MAS4b had an average of at least about 10² spots per million after stimulation with LISP1, LSAP2, TRAP, and UIS3 peptide pools. Splenocytes from mice immunized with tested T-cell string polypeptide construct MAS4b had the highest response after stimulation with LISP1 with an average of about 10³ spots per million. [1388] As shown in FIG.6D, statistically significant IFN- γ producing cells were detected in splenocytes from mice immunized with 5 μg T-cell string polypeptide construct MAS4c, upon stimulation with LISP1, LISP2, LSAP2, TRAP or UIS3 peptide pools, but not with CSP or ETRAMP10.3. Splenocytes from mice immunized with tested T-cell string polypeptide construct MAS4c had an average of at least about 10² spots per million after stimulation with LISP1, LISP2, LSAP2, TRAP, and UIS3 peptide pools. Splenocytes from mice immunized with tested T-cell string polypeptide construct MAS4c had the highest response after stimulation with LISP1 with an average of about 10³ spots per million. [1389] As shown in FIG.6E, statistically significant IFN- γ producing cells were detected in splenocytes from mice immunized with 5 μg T-cell string polypeptide construct MAS4d, upon stimulation with all included antigens peptide pools. Splenocytes from mice immunized with tested T-cell string polypeptide construct MAS4d had an average of at least about 10² spots per million after stimulation with CSP, LISP1, LSA1b, LSAP2, TRAP, UIS3 or ETRAMP10.3 peptide pools. Splenocytes from mice immunized with tested T-cell string polypeptide construct MAS4d had the highest response after stimulation with LISP1 with an average of about 10³spots per million. [1390] As shown in FIG.6F, statistically significant IFN- γ producing cells were detected in splenocytes from mice immunized with 2.5 μg T-cell string polypeptide construct MAS3a, upon stimulation with LSAP2 and TRAP peptide pools, but not with CSP, UIS3, or ETRAMP10.3. Splenocytes from mice immunized with tested T-cell string polypeptide construct MAS3a had an average of at least about 10² spots per million after stimulation with LSAP2 and TRAP peptide pools. [1391] As shown in FIG.6G, statistically significant IFN- γ producing cells were detected in splenocytes from mice immunized with 2.5 μg T-cell string polypeptide construct MAS4f, upon stimulation with LISP1, LISP2, LSA1b peptide pools, but not with LSA1a peptide pool. Splenocytes from mice immunized with tested T-cell string polypeptide construct MAS4f had an average of at least about 10³ spots per million after stimulation with LISP1 or LSA1b. Splenocytes from mice immunized with tested T-cell string polypeptide construct MAS4f had an average of about 10² spots per million after stimulation with LISP2. [1392] As shown in FIG.6H, statistically significant IFN- γ producing cells were detected in splenocytes from mice immunized with a combination of 2.5 μg T-cell string polypeptide construct MAS3a and with 2.5 μg construct MAS4f, upon stimulation with all included antigens peptide pools. Splenocytes from mice immunized with a combination of tested T-cell string polypeptide constructs MAS3a and MAS4f had an average of at least about 10³ spots per million after stimulation with LISP1, LISP2 or LSA1b. Splenocytes from mice immunized with a combination of tested T-cell string polypeptide constructs MAS3a and MAS4f had an average of at least about 10² spots per million after stimulation with CSP, LSA1a, LSAP2, TRAP, UIS3 or ETRAMP10.3. As shown in FIG.7A, splenocytes from mice immunized with a combination of T-cell string polypeptide constructs MAS3a and MAS4f, or individually with MAS3a or MAS4f, exhibited similar responses after stimulation with CSP, LISP1, LISP2, LSA1a, LSA1b, LSAP2, TRAP, UIS3 or ETRAMP10.3. As shown in FIG.8A, splenocytes from mice immunized with a combination of shorter T-cell string polypeptide constructs (MAS3a and MAS4f) exhibited an enhanced response after stimulation with CSP, LISP1, LISP2, LSA1a, LSA1b, LSAP2, TRAP, UIS3 or ETRAMP10.3, as compared to splenocytes from mice immunized with longer T-cell string polypeptide construct (MAS4a), which includes the same antigenic content as in MAS3a and MAS4f combined. [1393] Thus, the present Example demonstrates that certain T-cell string polypeptide constructs effectively induce an immune response characterized by activation of T-cells secreting pro-inflammatory cytokines (e.g., IFN-γ), e.g., assessed using a ELISpot assay. [1394] In conclusion, in vivo immunogenicity studies of Example 2 and 3 confirmed that all antigen segments within a combination of Mas3a and Mas4f or within a combination of ERMA48 and Mas4f elicit T-cell responses. Example 5: In-vitro Expression of Exemplary Polyribonucleotides Encoding Plasmodium CSP Polypeptide Constructs [1395] The present Example demonstrates that exemplary polyribonucleotides encoding different Plasmodium CSP polypeptide constructs, as described herein, exhibit in-vitro expression (e.g., intracellular, surface) in mammalian cells (HEK293T cells). [1396] In vitro expression assays were used to assess expression and localization of different malarial polypeptide constructs. Assays were initially performed with non-formulated RNA constructs to determine functionality. Formulated RNA constructs were also assessed. [1397] Briefly, HEK293T cells were transfected with (i) 350 ng of RNA constructs or (ii) 5 ng or 50 ng of LNP formulated RNA constructs. HEK293T cells transfected with 350 ng of RNA constructs or with 5 ng of formulated RNA constructs were assessed for protein expression by antibody staining and FACS. Transfection rate was determined by measuring percentage of positive cells, and total expression was determined by measuring median fluorescence of the total HEK population. HEK293T cells transfected with 50 ng of formulated RNA constructs were assessed for protein secretion by detecting protein in the culture supernatant of transfected cells. (1) Transfection of mammalian cells (e.g., HEK 293T cells) in multi-well plates [1398] A sub confluent T175 flask (e.g., 80-90% confluency) of HEK293T cells was used for cell seeding by detaching cells using an enzyme mixture of proteolytic and collagenolytic enzyme activity (e.g., Accutase®). Detached cells were collected and 0.4x10^5 cells were seeded in 1000 μL/well of a 12-well plate on the day of transfection. [1399] For transfection of mammalian cells with non-formulated mRNA the use of a transfection agent is necessary, and, in this case, cell transfection was performed with MessengerMax Transfection Reagent following the manufacturers protocol. MessengerMax is diluted in OptiMEM so that there is 2 μl of the transfection agent per well, and this mixture was incubated at room temperature (RT) for 10 min. For each tested sample, 100 ng of RNA per well was diluted in 100 μl of OptiMEM and MessengerMax mix. The RNA-MessengerMax-Mix was incubated for 5 min at RT to allow complex formation. About 100 μL/well of the transfection mixture was added dropwise onto the cells. The transfected cells were then incubated overnight (e.g., 18 hours) at 37°C, 5% CO2 under humidified atmosphere. [1400] For transfection of mammalian cells with formulated RNA, the formulated product was diluted (e.g., in a range of 5 ng – 200 ng) in 100 μl OptiMEM per well and the mixture added dropwise on the cells. Culture plates were subsequently centrifuged at 300 x g, 5 min at 21°C and were then incubated overnight (e.g., 18 hours) at 37°C, 5% CO2 under humidified atmosphere. (2) Flow cytometry analysis for detection of protein expression [1401] The transfected cells were subject to flow cytometry analysis quantifying protein expression. Briefly, transfected cells were washed with DPBS and transferred to 96-well plate for staining. Cells were stained firstly for viability (Fixable Viability Dye eFluor™ 450; 1:500), and then with a primary antibody against PfCSP (either human anti-PfCSP L9 targeting minor repeats (1:60,000) or mouse anti-PfCSP 2A10 targeting major repeats (1:2000)) and a fluorescent secondary antibody (either anti-human-AlexaFluor® 674 (1:1000) or anti-mouse-AlexaFluor® 647 (1:500)). A permeabilization step was included prior to staining with antibodies. After staining, cells were resuspended in 180 μl FACS Buffer (DPBS with 1% BSA, 0.5 mM EDTA) and 75 μl of the cells was acquired for flow cytometry analysis using BD FACS Celesta Cell Analyzer. [1402] Both non-formulated (e.g., FIG.9, FIG.67, FIG.68) and formulated (e.g., FIG.10, FIG.69) Plasmodium CSP polypeptide constructs had an overall high transfection rate. As shown in FIG.9A, RNA constructs 7, 25, 28 and 30-40 had the highest transfection rates (at least about 70% positive cells). Furthermore, polyribonucleotides encoding malarial polypeptide constructs with a TM domain or GPI anchor (RNA constructs 7, 23, 25, 28, and 30-41) were expressed on the surface, while those without (RNA constructs 1, 2, 4, 5, 6, 8, 9, 24, 26, 27, and 29) were not. As shown in FIG.9B, RNA constructs 28, 36 and 37 had the highest expression overall, exhibiting intracellular staining with a median fluorescence intensity of at least about 150,000 and surface staining with a median fluorescence intensity of at least about 75,000. [1403] As shown in FIG.10A, all Plasmodium CSP polypeptide constructs were expressed; however, some RNA constructs (22, 25, 26, 28, 32, 34, 36, 38, 42) demonstrated a saturated transfection rate (at least 90% positive cells) at 5 ng formulated RNA construct. Others (constructs 6, 29 and 41) exhibited a low transfection rate (below 25% positive cells) and others (RNA constructs 2, 8, 23, 24, 30, 31, 32, 33, 35, 37, 39, 45) were in an intermediate range (at least 40% positive cells). As shown in FIG.10A, all polyribonucleotides encoding malarial polypeptide constructs with a TM domain or GPI anchor (RNA constructs 22, 23, 25, 28, and 30-41) demonstrated positive surface expression. As shown in FIG.10B , these polyribonucleotides encoding TM domain or GPI anchor-containing malarial polypeptide constructs exhibited varying degrees of total expression, with intracellular staining detected at a median fluorescence intensity of 20,000 to 80,000 and surface staining detected with a median fluorescence intensity of 0 to about 20,000). When protein secretion was assessed by measuring protein levels in culture supernatants, of the polyribonucleotides encoding malarial polypeptide constructs that contain a signal sequence, only constructs 24 and 29 were detected in the culture supernatant (FIG.10C). [1404] Further exemplary Plasmodium CSP polypeptide constructs also had an overall high transfection rate and all constructs express in a mammalian system as shown in FIG.26, and FIG.27. All tested constructs expressed in a mammalian cell line as shown in FIGS.26A-26B and, FIGS.27A-27B. When MessengerMax- formulated RNA was tested, as shown in FIGS.26A-26B, constructs 89, 90, 92, 94 and 99 showed the highest percentage of transfected cells (above 80%), and transfection with constructs 90 and 92 led to the highest protein expression as measured by MFI. When testing LNP-formulated RNA, as shown in FIGS.27A-27B, all constructs express in a mammalian system. RNA constructs 98, 99, 101 and 175 had overall high transfection rates (at least about 70% and above positive cells) and constructs 98 and 99 had the highest MFI signal overall. [1405] A high transfection rate and total expression was also observed for Plasmodium CSP polypeptide construct ERMA 23-7 as shown in FIGS.53A-53B. [1406] Compared between each other, out of RNA constructs 91, 100 and 104, RNA construct 100 demonstrated the highest in vitro expression. Both RNA construct 100 and RNA construct 104 had strong, and equal, surface expression (FIG.67A and 67B). Similar expression was seen for both RNA construct 87 and RNA construct 88 when compared to each other (FIG.68A and 68B); however, both were not expressed on the surface. LNP- formulated RNA constructs 87, 88, 91, 100 and 104 were also tested, at a concentration of 5 ng/well. RNA construct 100 and RNA construct 104 showed the highest level of expression when compared with the rest of the group (FIG. 69A and 69B). Example 6: Immunogenicity Studies of Exemplary Polyribonucleotides Encoding Plasmodium CSP Polypeptide Constructs [1407] The present Example documents the ability of certain polyribonucleotides encoding Plasmodium CSP polypeptide constructs, provided by the present disclosure, to induce immune responses, as assessed in mice. [1408] C57BL6 female mice (10-12-weeks old) were immunized intramuscularly (IM) twice, on days 0 and 21, with 1 μg of a formulated RNA construct (described in Example 4) or injected with phosphate buffer saline (vehicle) (n=8 mice/group). Blood samples were collected before (day 0) and after immunization (on days 7, 14, 21, 28 and 35) to generate serum samples at various time points. At the end of the experiment (day 35), blood and splenocytes were harvested and analyzed. Animals were divided into multiple groups receiving treatment as indicated in Table 20 below. Table 20: Study plan for certain exemplary immunogenicity studies with RNA constructs F1, F2, F3, F4 = LNP formulations comprising RNA construct with modified nucleotides BC = Blood collection / Serum generation (amount of blood that can be collected: 14 days interval between collections: 150μl/20g mouse; 7 days interval between collections: 110μl/20g mouse) * pre-immune serum: blood sample is collected from 10% of all animals = 4 animals. FBC = Final blood collection/ Serum generation; Spleen collection and freezing of splenocytes (for Fluorospot analysis) [1409] Serum and splenocyte samples obtained from each group of immunized animals were analyzed by one or more of the following method(s): (1) Enzyme-linked Immunosorbent Assay (ELISA), (2) multiplex assay, (3) sporozoite ELISA, (4) traversal Assay, (5) inhibition of Liver Stage Development Assay (ILSDA), (6) Fluorospot assay , (7) Sporozoite Immunofluorescence Assay, (8) Circumsporozoite Precipitation Reaction (CSPR) Assay, (9) Cytotoxicity, (10) In vitro gliding Assay, and (11) Binding and Dissociation Measurements by SPR. (1) Enzyme-linked Immunosorbent Assay (ELISA) [1410] Provided polyribonucleotides can be assessed for their ability to induce production of antibodies that may bind to Plasmodium falciparum (Pf) CSP full length protein (“PfCSP-FL”), and/or PfCSP C-terminal domain (“PfCSP-C”). In some embodiments, a provided polyribonucleotide is determined to induce a useful immune response if serum from a subject (e.g., a mouse) immunized with such construct is shown to bind PfCSP-FL, and/or PfCSP-C in an ELISA assay as described herein. [1411] RNA constructs (as described in Example 5), were assessed for their ability to induce production of antibodies that bind to PfCSP-FL, and/or PfCSP-C using an ELISA assay (see Table 21 and/or Table 22). Table 21: List of PfCSP recombinant proteins and peptides assessed by ELISA analyses in the present Example

[1412] Briefly, MaxiSorp 96-well plates were coated with 100 ng/well of PfCSP-FL or PfCSP-C in coating buffer (50mM sodium carbonate, pH 9.6) and incubated overnight at 4°C. Plates were then blocked with 1% BSA in PBS for 1h at 37°C (for PfCSP-FL and PfCSP-C). Bound IgG was detected using horseradish peroxidase (HRP)-conjugated goat anti-mouse IgG. Signal was detected after adding the substrate 3,3',5,5'-Tetramethylbenzidine (TMB) and 25% sulfuric acid to stop the reaction. Optical densities (OD) were read at 450 nm. Table 22: List of PfCSP recombinant proteins used for ELISA analyses in the present Example. [1413] Reciprocal end titers at day 21 and/or day 35 were used as a representative of the antibody response. Results are shown in FIG.11, FIGS.28-29, and FIG.8. As shown in FIG.70, all of the tested RNA constructs (except for RNA construct 6) induced high levels of antibodies to PfCSP-FL (exhibiting a mean reciprocal end titer of about 10⁵ to about 10⁷). In addition, as shown in FIG.11B, most tested RNA constructs (except for RNA construct 6) induced a strong antibody response to PfCSP-C (exhibiting a mean reciprocal end titer of about 10⁵ to about 10⁷). As shown in FIG.28A, all the different RNA constructs induced antibodies to PfCSP-FL after 1 immunization, as measured by ELISA on day 21. As shown in FIG.28B, all RNA constructs, except 99, induced antibody responses to PfCSP-C term 3D7, at day 21. As shown in FIG.29A, all the different RNA constructs induced high antibody titers to PfCSP-FL after 2 immunizations, as measured by ELISA on day 35 (exhibiting a mean reciprocal end titer of about 10⁵ to about 106). As shown in FIG.29B, except for 99, all other RNA constructs induced a strong antibody response to PfCSP-C term 3D7 (exhibiting a mean reciprocal end titer of about 10⁵ to about 10⁶). [1414] As shown in FIG.70A, RNA constructs 87, 88, 91, 100 and 104 induced high levels of antibodies to PfCSP-FL (exhibiting a mean reciprocal end titer of about 105 to about 106). As shown in FIG.70B, RNA constructs 87, 88, and 91 induced a strong antibody response to PfCSP-C term 3D7 (exhibiting a mean reciprocal end titer of about 104 to about 106). Immunization with RNA constructs 100 and 104 did not elicit antibodies against PfCSP-C term 3D7 (FIG.70B) as expected, as neither of these constructs expresses this region of the protein. Immunization with RNA construct 87 elicited lower titers against the C-terminal domain of PfCSP than RNA construct 88 and RNA construct 91. No titers were detected for control mice (injected with the vehicle). [1415] Thus, the present Example demonstrates that certain provided polyribonucleotides effectively induce an immune response characterized by inducing production of antibodies that bind to PfCSP-FL, and/or PfCSP-C, as assessed using an ELISA assay. All but one construct induced antibodies that bind to at least one of PfCSP-FL or PfCSP-C. For example, polyribonucleotides that encoded malarial polypeptide constructs that included a signal peptide (RNA constructs 2, 8, 23, 24, 25, 26, 28, 29, 30, 31, 33, 34, 35, 37, 39, 41, 42, 87, 88, 89, 90, 91, 92, 98, 99, 100, 101, 102, 104, 105, and 175) were shown to have induced a strong antibody response to PfCSP-FL (mean reciprocal end titer of about 10⁵ to about 10⁷); polyribonucleotides encoding malarial polypeptide constructs that included a signal peptide (RNA constructs 2, , 23, 24, 25, 26, 30, 31, 33, 35, 37, 88, 91, 92, 93, 98, 101, 102, 103, 105, and 175) were shown to have induced a strong antibody response to PfCSP-C (mean reciprocal end titer of about 10⁵ to about 10⁷). [1416] Antibody titers against PfCSP-FL, as determined by an ELISA assay, for RNA construct ERMA 23-7 are shown in FIG.54. (2) Multiplex Assay [1417] Provided polyribonucleotides can be assessed for their ability to induce production of antibodies that bind to specific PfCSP epitopes. In some embodiments, a provided polyribonucleotide is determined to induce a useful immune response if serum from a subject (e.g., a mouse) immunized with such construct is shown to target peptides from the central region of PfCSP (e.g., PfCSP peptide 17C, 18C, 19C, 20C, 21C, 22C, 23C, 27C, 29C, and/or 42C) in a multiplex assay, as described herein (see FIG.55A). [1418] RNA constructs (as described in Example 5) were assessed for their ability to induce production of antibodies that bind to specific PfCSP epitopes (see Table 23) by performing a multiplex analysis (Meso Scale Discovery) according to the manufacturer’s instructions. Briefly, ten peptides from the central region of PfCSP (PfCSP peptide 17C, 18C, 19C, 20C, 21C, 22C, 23C, 27C, 29C, or 42C) were conjugated with bovine serum albumin (BSA) and then bound to the wells of a 96-well plate, in a specific spot on the well. After incubation with serum from immunized mice, antibodies bound to each specific peptide were detected with a “Sulfo-Tag” conjugated secondary antibody. A multiplex reader instrument (MESO QuickPlex SQ 120) was used to quantify the light emitted from the Sulfo-Tag. Table 23: PfCSP peptides used in the multiplex analysis [1419] Most tested RNA constructs generated antibodies that exhibited binding to at least some epitopes (FIG. 12, FIGS.30A-30K, FIG.71, FIGS.72A-72J). Only RNA construct 101 and 6 showed an overall low binding to all the epitopes. Peptides 17C and 18C are partially located in the N-terminal domain, R1 and junction of the PfCSP and antibodies against these peptides and were recognized (demonstrating AUC of at least about 600,000) mainly by polyribonucleotides encoding full length malarial polypeptide constructs (RNA constructs 2, 8, 23, 26, 28, 42, 45) and RNA constructs 22 (encoding a malarial polypeptide construct ΔN-term), 25 (encoding a malarial polypeptide construct which lacks major repeats and PfLSA-3 fragment is in place of N-term), 41 (encoding a malarial polypeptide construct in which the N-term, R1 and junction region is repeated 4 times and the major repeats are left out) (FIG. 12B), and 104 (encoding a Plasmodium polypeptide construct in which the R1, junction region, minor repeat, and 6 major repeats are repeated 3 times) (FIG.72A). High binding was observed for RNA constructs 90, 92 and 98 (FIGS.30A-30C). [1420] Peptides 19C and 20C span R1, junctional region and a part of minor repeats and were recognized by antibodies generated from polyribonucleotides encoding full length CSP constructs (RNA constructs 2, 8, 23, 26, 28, 42, and 45) (FIG.12B). As shown in FIG.12B, RNA constructs 6, 29, and 31 did not induce antibodies against 17C, 18C, 19C or 20C. High binding was observed for RNA constructs 99 and 175 (FIG.30A, 30F, and 30G). [1421] All RNA constructs tested encode at least some part of the minor or major repeats of PfCSP, and antibodies to peptides 23C, 42C and 27C, which all span the minor and major repeats in different sections, were observed for most of the constructs (demonstrating AUC of at least about 600,000) depicted in FIG.12B and for all constructs depicted in FIG.30A, 30E, 30I, 30J, and FIG.72G – 72I except construct 101. [1422] Peptides 21C, 22C and 29C span the minor repeats, major repeats, and/or junction and are the main binding epitopes of known neutralizing antibodies, CIS43, L9 and mAb317, respectively (FIGS.12B, 30A, 30D, 30H, 30K, 72E, 72F, and 72J). Antibodies against these regions were produced by immunization with all RNA constructs, except constructs 6, 29, and 31, which induced antibodies only to 29C (major repeats) (FIG.12B), and except for construct 101 (FIG.30A, 30D, 30H, and 30K). [1423] Results for RNA construct ERMA 23-7 are shown in FIG.55. [1424] Thus, the present Example demonstrates that all provided polyribonucleotides effectively induce production of antibodies that bind at least to one specific epitope from the central region of PfCSP (e.g., PfCSP peptide 17C, 18C, 19C, 20C, 21C, 22C, 23C, 27C, 29C, and/or 42C). (3) Sporozoite ELISA [1425] Provided polyribonucleotides can be assessed for their ability to induce production of antibodies that may bind to native CSP antigen from Plasmodium falciparum (Pf) sporozoite lysates. In some embodiments, a provided polyribonucleotide is determined to induce a useful immune response if serum from a subject (e.g., a mouse) immunized with such construct is shown to bind to native CSP antigen from Plasmodium falciparum (Pf) sporozoite lysates in a sporozoite ELISA assay, as described herein. [1426] RNA constructs (as described in Example 5), were assessed for their ability to induce production of antibodies that bind to native CSP antigen from Plasmodium falciparum (Pf) sporozoite lysates, using a sporozoite ELISA assay. Specifically, 384-well plates were coated with non-denatured total protein lysate from Plasmodium falciparum (Pf) NF54 salivary gland sporozoites, in an amount equivalent to about 250 sporozoites per well. Following blocking, serially diluted serum samples (6 dilutions per sample) were added to the corresponding wells. Binding of antibodies present in the serum samples to the native PfCSP protein in the wells was detected using an AP- conjugated secondary antibody followed by luminescent quantification. [1427] As shown in FIG.31A, tested RNA constructs effectively induced production of antibodies that bound a native PfCSP antigen above background (defined by the binding of the vehicle samples). Overall, all RNA constructs performed similarly, except constructs 93 and 175 that displayed higher binding than the other constructs. FIG.31B shows binding of murine anti-CSP mAb3SP2 used as a positive control. [1428] As further shown in FIG.13A, tested RNA constructs effectively induced production of antibodies that bound native PfCSP antigen above the background (defined by the binding of the vehicle samples). Overall, RNA constructs encoding malarial polypeptide constructs (RNA constructs 2, 8, 23, 26, 45, and 29) performed better than others. FIG.13B shows binding of murine anti-Pfs25 mAb32F81 used as negative control, and murine anti-CSP mAb3SP2 used as a positive control. [1429] Thus, the present Example demonstrates that certain provided polyribonucleotides effectively induce an immune response characterized by inducing production of antibodies that bind to native CSP antigen from Plasmodium falciparum (Pf) sporozoite lysates in a sporozoite ELISA assay. All but one of the tested constructs showed higher antibodies compared to the vehicle. [1430] As shown in FIG.94, tested RNA constructs effectively induced production of antibodies that bound a native PfCSP antigen at a level above background (defined by the binding of the vehicle samples). Overall, all RNA constructs performed similarly, except constructs 104 and 100 that displayed higher binding than the other constructs. FIG.31B shows binding of murine anti-CSP mAb3SP2 used as a positive control. (4) Traversal Assay [1431] Provided polyribonucleotides can be assessed for their ability to induce production of antibodies with an inhibitory effect on traversal (a type of motility displayed by Plasmodium falciparum (Pf) sporozoites that is essential for their infectivity). In some embodiments, a provided polyribonucleotide is determined to induce a useful immune response if serum from a subject (e.g., a mouse) immunized with such construct is shown to reduce ability of sporozoite to traverse hepatocytes in a traversal assay, as described herein. [1432] RNA constructs (as described in Example 5) were assessed for their ability to induce production of antibodies that have an inhibitory effect on Plasmodium falciparum (Pf) sporozoites traversal. Briefly, HC-04 cells, a human hepatocyte cell line, were seeded into plates and incubated for 24 h at 5% CO₂ and 37°C. Freshly isolated Plasmodium falciparum (Pf) salivary gland sporozoites were pre-incubated with serially diluted (1:20, 1:80 and 1:320 or 1:40, 1:80, 1:160, 1:320, and 1:640) serum samples from mice immunized with formulated RNA constructs. Sporozoites were then added to the HC-04 cells in a multiplicity of infection (MOI) of 1:1, in the presence of impermeable dye dextran-rhodamine. As a positive control for inhibition, sporozoites were pre-treated with mAb317. Non-treated sporozoites were used as a negative control for inhibition. Ability of Plasmodium falciparum (Pf) sporozoites to traverse cells was quantified by determining a percentage of cells that incorporated dextran- rhodamine, by fluorescence microscopy. Sporozoite traversal of sporozoites pre-incubated with serum samples from mice injected with vehicle or with medium only was set as 0% traversal inhibition. [1433] When sporozoites were pre-incubated with serum from mice injected with vehicle, on average 30% of the cells incorporated dextran-rhodamine, indicating that they were traversed by sporozoites (see FIG.14B). The average of all vehicle samples was considered as 0% inhibition and was a comparator for all samples from mice immunized with RNA constructs in FIG 14A. [1434] As shown in FIGS.14A-14B, 65A-65G, and 66A-66G, the antibodies generated from mice immunized with different formulated RNA constructs are able to inhibit P. falciparum sporozoite traversal. Results for FIGS. 65A-65G and 66A-66G are shown as the percentage of inhibition of traversal activity (mean with SEM) in comparison to the medium control, which was set as 0% inhibition. [1435] As shown in FIGS.65A and 66A, at lower (1:20) dilution of sera, there was about 40-80% inhibition of traversal observed for sera from mice immunized with RNA constructs 88, 89, 90, 91, 92, 100, 104, 175, 93, 94, 103, 99, 102, and 105. The percentage of inhibition of traversal decreased for all RNA constructs with an increase in sera dilution (FIGS.65B-65F and 66B-66F). As shown in FIGS.14A, 65G and 66G, sera from mice immunized with all RNA constructs, except 98, 87, and 88 effectively inhibited sporozoite traversal of HC-04 cells above background (defined by the vehicle samples). Highest inhibition, as assessed by higher AUC or higher dilution at which 50% of traversal is inhibited, was observed for constructs 39, 41, 23, 24, 25, 90, 103, 94, 93, 99 and 175. FIGS.14B and 65H show inhibition of traversal by human anti-CSP mAb317 used as a positive control. Sera from mice immunized with veh (vehicle) was used as a negative control. [1436] Thus, the present example demonstrates that certain polyribonucleotides effectively induce an immune response characterized by inducing production of antibodies that inhibit sporozoite traversal, e.g., as measured using a traversal assay. (5) Inhibition of Liver Stage Development Assay (ILSDA) [1437] Provided polyribonucleotidescan be assessed for their ability to induce production of antibodies that inhibit infection of primary human hepatocytes by Plasmodium falciparum (Pf) sporozoites. In some embodiments, a provided polyribonucleotide is determined to induce a useful immune response if serum from a subject (e.g., a mouse) immunized with such construct is shown to inhibit Plasmodium falciparum (Pf) sporozoite infection in an ILSDA assay as described herein. [1438] In the ILSDA assay, freshly isolated salivary gland sporozoites were pre-incubated with serially diluted serum samples of sera from mice immunized with RNA constructs (as described in Example 5). Pre-incubated sporozoites were then added to primary human hepatocytes that were seeded on a glass-bottom black 96-well plate. After centrifugation to facilitate infection, cells were incubated for 4 days at 5% CO₂ and 37°C. After fixation, parasite cytoplasm was stained with anti-PfHsp70 and DNA (from hepatocytes and from parasites) was stained with DAPI. mAb317, an antibody known to inhibit hepatocyte infection, was used as positive control. Sporozoites incubated with serum from mice injected with vehicle were used as a negative control for inhibition. Ability of Plasmodium falciparum (Pf) sporozoites to infect hepatocytes was quantified by determining a percentage of cells with parasites inside, by fluorescence microscopy. [1439] As shown in FIG.15A and FIG.61A-H at lower (1:40) dilution of sera from mice immunized with RNA constructs 39, 2, 23, 26, 42, 45, 175, 93, 94, 99, 102, 105, 87, 88, 91, 104, and 100 primary human hepatocyte infection was inhibited above 50%. The percentage inhibition decreased for all tested samples with the increase in sera dilution to 1:160. At dilution 1:640, inhibition is detectable for constructs 39, 2, 23, 26, 45, 29, 89, 90, 92, 175, 94, 103, 98, 99, 101, 102, 105, 88, 91, 104, and 100. At dilution 1:2560, inhibition is undetectable or below 20% for all tested RNA constructs (FIG.61D and FIG.61H). As shown in FIGS.61I and 61J, all tested RNA constructs effectively inhibited infection of primary human hepatocytes above background (defined by vehicle (Veh) samples). Highest inhibition, as assessed by higher AUC, was observed for RNA constructs 99, 94, 89, 90, 92, 175, and 100. FIG.61K shows inhibition of primary hepatocyte infection using a positive control human anti-CSP mAb317. [1440] Thus, the present example demonstrates that certain polyribonucleotides effectively induced production of antibodies that inhibited invasion of primary human hepatocytes, e.g., as measured using an inhibition of liver stage development assay. For example, sera from mice immunized with RNA constructs 2, 23, 39, and 42 were able to inhibit infection by approximately 60% at lower dilutions (1:40), while sera from mice immunized with RNA construct 2 and 29 inhibited infection over 20% at higher dilution (1:640). (6) FluoroSpot Assay [1441] Provided polyribonucleotides can be assessed for their ability to induce production of antibodies responsive to recombinant PfCSP, MHC-I, and/or MHC-II peptides (FIGS.16 – 22), and/or provided polyribonucleotides can be assessed for their ability to induce T-cell responses upon stimulation with peptides from Pf antigens (FIGS.32 – 52 and FIGS.73-93). In some embodiments, a polyribonucleotide is determined to induce a useful immune response if splenocytes from a subject (e.g., a mouse) immunized with such construct, following incubation with peptide(s) as described herein, exhibit T-cell secretion of one or more pro-inflammatory cytokines (e.g., IFN-γ, TNF-α, or IL-2) in a FluoroSpot Assay, as described herein. [1442] FluoroSpot assays that produced data depicted in FIGS.16 – 22 were performed with mouse IFN- γ/IL-2/TNF-α FluoroSpot^PLUS kit according to the manufacturer’s instructions (Mabtech). Frozen splenocytes from mice immunized with RNA constructs (as described in Example 5). were thawed and washed twice in DPBS before being resuspended in culture medium (RPMI1640 + 10% heat-inactivated fetal calf serum (FCS) + 1% non-essential amino acids (NEAA) + 1% Sodium Pyruvate + 1% HEPES + 0.5% Penicillin/Streptomycin, + 0.1% β-Mercaptoethanol). [1443] After determining cell concentration for each sample using a cell counter, a total of 5 × 10⁵ splenocytes were added to each well and restimulated ex vivo overnight at 37°C with the peptides indicated in Table 24. For RNA constructs depicted in FIGS.16 – 22, a PfCSP-FL peptide pool (PfCSP-FL_pep), MHC-I peptide pool, MHC-II peptide pool) or with controls (negative control: gp70-AH1 (SPSYVYHQF)( SEQ ID NO: 595), 4 μg/mL; positive control: concanavalin A, 2 μg/mL). On the following day, anti-IFN-γ, anti-IL-2 and anti-TNF-α antibodies were added to the wells to detect production of these cytokines and then secondary antibodies conjugated with different fluorophores were added. Fluorescent spots were counted using a Mabtech IRIS FluoroSpot plate reader. [1444] To produce data depicted in FIGS.32 – 52 and FIGS.73-93, splenocytes were freshly isolated from the spleens of mice immunized with RNA constructs and resuspended in culture medium (RPMI1640 + 10% heat- inactivated fetal calf serum (FCS) + 1% non-essential amino acids (NEAA) + 1% Sodium Pyruvate + 1% HEPES + 0.5% Penicillin/Streptomycin, + 0.1% β-Mercaptoethanol). After determining cell concentration for each sample using a cell counter, a total of 5 × 10⁵ splenocytes were added to each well and restimulated ex vivo overnight at 37°C with the appropriate target peptide pool, e.g., as indicated in Table 24 or with controls (negative control: Trp1, 2 μg/mL; positive control: concanavalin A, 2 μg/mL). On the following day, anti-IFN-γ, anti-IL-2 and anti-TNF-α antibodies were added to the wells to detect production of these cytokines and then secondary antibodies conjugated with different fluorophores were added. Fluorescent spots were counted using a Mabtech IRIS FluoroSpot plate reader. [1445] For assessing specific CD4 and CD8 T cell responses for RNA constructs depicted in FIGS.32 – 52 and FIGS.73-93, CD4 and CD8 isolation kits (Mylteni) were employed to specifically isolate these cells from all the cells isolated from the spleens, according to the manufacturer’s instructions. Shortly, splenocytes were resuspended in MACS buffer, the biotin-labelled antibody cocktail was added to the cells, mixed and incubated for 5 minutes at 2- 8°C. Then, MACS buffer was added again, followed by anti-biotin microbeads and an incubation for 10 minutes at 2- 8°C. Columns were conditioned by adding MACS buffer to them and allowing the MACS buffer to go through the columns completely. Cell suspensions were then added to the columns, followed by a wash with MACS buffer, and the flow-through containing the population of interest (because a negative selection method is used) was collected in a tube. MACS-isolated CD4 and CD8 T cells were counted, and 1 x 10⁵ cells were added per well of a fluorospot plate. Cells were then restimulated ex vivo overnight at 37°C with appropriate target peptide pools, e.g., as indicated in Table 24 or with controls (negative control: Trp1, 2 μg/mL; positive control: concanavalin A, 2 μg/mL), in the presence of antigen-presenting cells, which are added separately. On the following day, anti-IFN-γ, anti-IL-2 and anti-TNF-α antibodies were added to the wells to detect production of these cytokines and then secondary antibodies conjugated with different fluorophores were added. Fluorescent spots were counted using a Mabtech IRIS FluoroSpot plate reader. Table 24: Peptides used for splenocyte stimulation in the FluoroSpot Assay

[ t 600 IFN- γ-producing cells per 5x10⁵ splenocytes after stimulation with PfCSP-FL_pep. Splenocytes from mice immunized with tested RNA constructs (except for RNA construct 24) had an average of at least about 300 IFN-γ- producing cells per 5x10⁵ splenocytes after stimulation with MHC-II specific peptides. Splenocytes from mice immunized with RNA constructs 2, 28, 30, and 41 had the highest average with at least about 600 IFN-γ-producing cells per 5x10⁵ splenocytes after stimulation with MHC-II specific peptides. In contrast, upon stimulation with MHC-I specific peptides, splenocytes from mice immunized only with tested RNA construct 2, 23, or 28 exhibited activation of T-cell IFN-γ secretion (with an average of at least about 300 IFN- γ-producing cells per 5x10⁵ splenocytes). [1447] As shown in FIG.17, TNF-α producing cells were detected in splenocytes from mice immunized with all RNA constructs, upon stimulation with PfCSP-FL_pep or MHC-II-specific peptides, but not with MHC-I specific peptides. Splenocytes from mice immunized with tested RNA construct 23, 25, 28, 35, 37, 39, or 41 had an average of at least 50 TNF-α-producing cells per 5x10⁵ splenocytes after stimulation with PfCSP-FL_pep. Splenocytes from mice immunized with RNA construct 23 had the highest average with about 100 TNF-α-producing cells per 5x10⁵ splenocytes after stimulation with PfCSP-FL_pep. Splenocytes from mice immunized with tested RNA constructs (except for RNA constructs 24, 29, and 34) had an average of at least about 50 TNF-α-producing cells per 5x10⁵ splenocytes after stimulation with MHC-II specific peptides. Splenocytes from mice immunized with RNA construct 28, 35, 37, 41, or 42 had the highest average with at least about 100 TNF-α-producing cells per 5x10⁵ splenocytes after stimulation with MHC-II specific peptides. In contrast, upon stimulation with MHC-I specific peptides, only splenocytes from mice immunized with tested RNA construct 2, 8, 26, 28, 35, 37, or 42 exhibited activation of T-cell TNF-α secretion. [1448] As shown in FIG.18, upon stimulation with PfCSP-FL_pep and/or MHC-II-specific peptides, IL-2 producing cells were detected in splenocytes from mice immunized with most RNA constructs. Splenocytes from mice immunized with tested RNA constructs (except RNA construct 24) had an average of at least about 100 IL-2 - producing cells per 5x10⁵ splenocytes after stimulation with PfCSP-FL_pep. Splenocytes from mice immunized with RNA construct 2, 23, 28, or 41 had the highest average (about 350 to about 800 TNF-α-producing cells per 5x10⁵ splenocytes) after stimulation with PfCSP-FL_pep. Splenocytes from mice immunized with tested RNA constructs (except for RNA construct 24) had an average of at least about 300 IL-2 -producing cells per 5x10⁵ splenocytes after stimulation with MHC-II specific peptides. Splenocytes from mice immunized with RNA construct 30 or 41 had the highest average with at least about 800 TNF-α-producing cells per 5x10⁵ splenocytes after stimulation with MHC-II specific peptides. There was almost no response upon stimulation with MHC-I specific peptides. [1449] As shown in FIG.19, T-cells secreting both IL-2 and IFN-γ were detected in splenocytes from mice immunized with most RNA constructs upon stimulation with PfCSP-FL_pep or MHC-II specific peptides, but not MHC-I specific peptides. Splenocytes from mice immunized with tested RNA constructs (except RNA construct 24) had an average of at least about 50 IL-2 and IFN-γ-producing cells per 5x10⁵ splenocytes after stimulation with PfCSP- FL_pep. Splenocytes from mice immunized with RNA construct 23 or 41 had the highest average (at least about 300 IL-2/IFN-γ-producing cells per 5x10⁵ splenocytes) after stimulation with PfCSP-FL_pep. Splenocytes from mice immunized with tested RNA constructs (except for RNA construct 24) had an average of at least about 150 IL-2/IFN- γ-producing cells per 5x10⁵ splenocytes after stimulation with MHC-II specific peptides. Splenocytes from mice immunized with RNA construct 2, 28, 30 or 41 had the highest average with at least about 350 IL-2/IFN-γ-producing cells per 5x10⁵ splenocytes after stimulation with MHC-II specific peptides. There was almost no response upon stimulation with MHC-I specific peptides. [1450] As shown in FIG.20 and FIG.21, the number of T-cells secreting both IFN-γ and TNF-α, or secreting both IL-2 and TNF-α, was low in splenocytes from mice immunized with tested RNA constructs upon stimulation with PfCSP-FL_pep, MHC-II specific peptides, or MHC-I specific peptides. For example, splenocytes from mice immunized with tested RNA constructs had an average of less than about 20 IFN-γ/TNF-α-producing cells or IL-2/TNF-α- producing cells, per 5x10⁵ splenocytes, after stimulation with PfCSP-FL_pep or after stimulation with MHC-II specific peptides. [1451] As shown in FIG.22, T-cells secreting IFN-γ, IL-2, and TNF-α were detected in splenocytes from mice immunized with most RNA constructs upon stimulation with PfCSP-FL_pep or MHC-II specific peptides, but not upon stimulation with MHC-I specific peptides. Splenocytes from mice immunized with tested RNA constructs (except RNA construct 24, 29, and 30) had an average of at least about 10 IFN-γ/IL-2/TNF-α-producing cells per 5x10⁵ splenocytes after stimulation with PfCSP-FL_pep. Splenocytes from mice immunized with RNA construct 23 or 41 had the highest average (about 55 and about 40 IFN-γ/IL-2/TNF-α-producing cells per 5x10⁵ splenocytes, respectively) after stimulation with PfCSP-FL_pep. Splenocytes from mice immunized with tested RNA constructs (except for RNA constructs 24 and 29) had an average of at least about 25 IFN-γ/IL-2/TNF-α -producing cells per 5x10⁵ splenocytes after stimulation with MHC-II specific peptides. Splenocytes from mice immunized with RNA construct 2, 28, 35, 37, 41, or 42 had the highest average with at least about 50 IFN-γ/IL-2/TNF-α -producing cells per 5x10⁵ splenocytes after stimulation with MHC-II specific peptides. There was almost no response upon stimulation with MHC-I specific peptides. [1452] As shown in FIGS.32A-32C, 33A-33C, 34A-34C, 35A-35C, 36A-36C, 37A-37C, and 38A-38C, the strongest T-cell responses were observed for the splenocytes isolated from mice immunized with RNA constructs 98 and 99. Overall, the responses observed for RNA constructs 101, 102 and 105 were lower than those observed for the other RNA constructs. A response was not observed from splenocytes from mice injected with vehicle alone. Incubation of the splenocytes from immunized mice with the unspecific peptide Trp1 or with culture medium only, also did not elicit a response from the cells. [1453] The ability of the tested RNA constructs to elicit T-cell responses from isolated CD4 was also evaluated. As shown in FIGS.39A-39D, 40A-40D, 41A-41D, 42A-42D, 43A-43D, 44A-44D, and 45A-45D, upon incubation with overlapping peptides spanning a PfCSP full length protein, CD4 T cells from mice immunized with the different constructs produced pro-inflammatory cytokines, such as IFNɣ, IL-2 and TNFα, alone or in different combinations. The strongest responses were observed for RNA constructs 98 and 99, while the weakest was observed for constructs 101 and 102. No response was observed for the vehicle group or upon incubation with the unspecific peptide Trp1 or with culture medium only. [1454] As shown in FIGS.46A-46D, 47A-47D, 48A-48D, 49A-49D, 50A-50D, 51A-51D, and 52A-52D, stimulation with overlapping peptides spanning a PfCSP-FL protein led to the production of pro-inflammatory cytokines, mainly IFNɣ and TNFα, alone or in different combinations, by CD8 T cells. Interestingly, IL-2 production was not observed by this cell population. Overall, the strongest responses were observed for RNA constructs 98 and 99. On the other hand, no CD8 response was observed for constructs 93, 94, 101, 102, 103, and 105. A response was also not observed for the vehicle group or upon incubation with the unspecific peptide Trp1 or with culture medium only. [1455] As shown in FIGS.73-79, the responses observed for RNA constructs 100 and 104 were lower than those observed for RNA constructs 87, 88, and 91. A response was not observed from splenocytes from mice injected with vehicle alone. Incubation of the splenocytes from immunized mice with the unspecific peptide Trp1 or with culture medium only, also did not elicit a response from the cells. [1456] As shown in FIGS.80-93, upon incubation with overlapping peptides spanning the PfCSP-FL protein, CD4 T cells from mice immunized with the different constructs produced pro-inflammatory cytokines, such as IFNɣ, IL-2 and TNFα, alone or in different combinations (FIGS.80-86). A similar CD4 T cell response was observed for all the RNA constructs. On the other hand, no response was observed from CD8 T cells (FIGS.87-93). A response was also not observed for the vehicle group or upon incubation with the unspecific peptide Trp1 or with culture medium only. [1457] Results for RNA construct ERMA 23-7 are shown in FIG.56. [1458] Thus, the present Example demonstrates that certain polyribonucleotides effectively induce an immune response characterized by activation of T-cells secreting one or more pro-inflammatory cytokines (e.g., IFN-γ, TNF-α, and/or IL-2), e.g., assessed using a fluorospot assay. [1459] For the results shown in FIGS.16-22, the peptides within the peptide pools were analyzed and it was found that the data generated upon incubation with MHC-I peptide pool is not representative of the ability of each construct to stimulate CD8 T cell responses. After analysis of the individual peptides, only 2 peptides present in the N-terminus of CSP have shown ability to stimulate cells. Therefore, among the constructs shown in FIGS. 16-22, only constructs with N-terminus had detectable responses, and the absence of a response with MHC-I peptide pool for the remaining constructs did not mean these constructs were unable to elicit a CD8 T cell response. (7) Sporozoite Immunofluorescence Assay [1460] Provided polyribonucleotides can be assessed for their ability to induce production of antibodies that may bind to native PfCSP on PfCSP-expressing Plasmodium berghei (PbPf) sporozoites. In some embodiments, a provided polyribonucleotide is determined to induce a useful immune response if serum from a subject (e.g., a mouse) immunized with such polyribonucleotide is shown to bind to native PfCSP on PbPf sporozoites in a sporozoite immunofluorescence assay, as described herein. [1461] In the sporozoite immunofluorescence assay, sporozoites were fixed with 2% formaldehyde in PBS for 20 min at room temperature. Then, sporozoites were washed on a spin-X centrifuge tube filter 0.45 μm Cellulose Acetate and maintained at 4°C until further experiments.4,000 PfCSP-expressing P. berghei sporozoites per sample were prepared in 1% bovine serum albumin (BSA)-PBS in a total volume of 5 μL. Sporozoites were mixed with 5 μL serum (from mice immunized with either a positive control (e.g., anti-PfCSP 2A10 mAb IV) or with RNA constructs (as described in Example 5) (diluted in 1% BSA-PBS (10-fold serial dilutions, from 1:10³ to 1:10⁸). Samples were incubated overnight at 4°C in a humid chamber in the dark. The day after, samples were incubated with Alexa 647 donkey anti-mouse IgG (H+L) in 1% BSA-PBS (final concentration of 20 μg/mL) for 30 min at 4°C in the dark. Samples were 11-fold diluted with cold PBS prior to acquisition by flow cytometry. The median antigen presenting cells (APC) intensity of the sporozoite population at different dilutions was calculated and log transformed. The cut- off values were determined according to the methods described (Frey et al. 1998), and used to interpolate the titer values from a linear regression. [1462] To determine antibody binding to native PfCSP on the surface of PfCSP-expressing P. berghei sporozoites, serially diluted serum samples were added to fixed PfCSP-expressing P. berghei sporozoites, and binding was assessed by flow cytometry. As shown in FIG.25A higher titers of PfCSP-binding antibodies were observed for mice immunized with RNA constructs 39, 41, 2, 8, 23, 26, 28, 42, 45, 29 and 22 when compared to mice injected with the remaining constructs or with 100 μg of 2A10 monoclonal antibody. [1463] Sporozoite IFA experiments were also performed to assess RNA constructs 2, 22, 23, 29, and 39. As shown in FIG.25F, in Experiment 1, sera from all the tested constructs showed a higher binding to PfCSP on the sporozoites than the sera from the 2A10-injected control. In Experiments 2 and 3, a similar binding was observed for sera from mice immunized with the RNA constructs and sera from mice immunized with Mosquirix®. [1464] Thus, the present Example demonstrates that certain provided RNA constructs effectively induced an immune response characterized by production of antibodies that bind to native PfCSP on PbPf sporozoites as assessed using a sporozoite immunofluorescence assay. For example, sera from mice immunized with RNA constructs 39, 41, 2, 8, 23, 26, 28, 42, 45, 29 or 22 were shown to have induced a stronger antibody response to native PfCSP on PbPf sporozites, as compared to sera from mice immunized with anti-PfCSP 2A10 mAb IV. (8) Circumsporozoite Precipitation Reaction (CSPR) Assay [1465] Provided polyribonucleotides can be assessed for their ability to induce production of antibodies that can elicit a CSP reaction on viable sporozoites. In some embodiments, a provided polyribonucleotide is determined to induce a useful immune response if serum from a subject (e.g., a mouse) immunized with such construct is shown to induce precipitation of CSP on viable sporozoites as measured by flow cytometry, as described herein. [1466] In the circumsporozoite precipitation reaction (CSPR) assay, 12,000 PbPf sporozoites were incubated at 37°C for 45 min with 17% serum (from mice immunized with either a positive control (e.g., anti-PfCSP 2A10 mAb IV) or with RNA constructs (as described in Example 5). Samples were next placed on ice, incubated for 10 min with 5 μg/mL propidium iodide and diluted 21 times with cold PBS prior to acquisition by flow cytometry. CSPR was measured by the estimated sporozoite length assessed by the mean of forward-scatter width (FSC-W). Data were analyzed using the CytExpert 2.0 software, which is incorporated herein by reference in its entirety. [1467] As shown in FIG.25C and FIG.25H, the CS precipitation reaction (CSPR) was estimated by flow cytometry after incubating PfCSP-expressing P. berghei sporozoites with the serum from immunized or control mice. Sera from mice immunized with anti-PfCSP 2A10 mAb had a similar effect on circumsporozoite precipitation as compared to sera from mice immunized with RNA construct 39 (exhibited by a mean FSC W of at least about 1220). Serum from mice immunized with RNA constructs 2, 8, 23, 26, 28, 42, 45, 29 or 22 elicited higher CSPR than serum from mice injected with the remaining RNA constructs, 2A10 or vehicle. [1468] Thus, the present Example demonstrates that certain RNA constructs effectively induced an immune response characterized by production of antibodies that elicit CSP precipitation on viable sporozoites e.g., assessed using a circumsporozoite precipitation reaction (CSPR) Assay. For example, sera from mice immunized with RNA constructs 2, 8, 23, 26, 28, 42, 45, 29 and 22 were shown to have induced a stronger response as compared to sera from mice immunized with anti-PfCSP 2A10 mAb. (9) Cytotoxicity [1469] Provided polyribonucleotides can be assessed for their ability to induce production of antibodies with an inhibitory effect on sporozoite viability. In some embodiments, a provided polyribonucleotide is determined to induce a useful immune response if serum from a subject (e.g., a mouse) immunized with such construct is shown to reduce viable sporozoites in a cytotoxicity assay, as described herein. [1470] In the cytotoxicity assay, 12,000 PbPf sporozoites were incubated at 37°C for 45 min with 17% serum (from mice immunized with either a positive control (e.g., anti-PfCSP 2A10 mAb IV) or with RNA constructs (as described in Example 5). Samples were next placed on ice, incubated for 10 min with 5 μg/mL propidium iodide and diluted 21 times with cold PBS prior to acquisition by flow cytometry. Viability was defined as the percentage of GFP⁺PI⁻ sporozoites to the sum of GFP⁺PI⁻ and GFP⁺PI⁺ sporozoites. Data were analyzed using the CytExpert 2.0 software. [1471] In a following experiment, PbPf sporozoites were mixed on ice with Corning® Matrigel® matrix in a 1:5 ratio. For each condition, the mix was divided into 5 μL reactions containing 12,000 sporozoites. Following polymerization at 37ºC for 5 min, 1 μL serum (17% final concentration; from mice immunized with either a positive control (e.g., anti-PfCSP 2A10 mAb IV) or with RNA constructs (as described in Example 5) was added. After 45 min at 37°C, samples were placed on ice for 10 min to allow depolymerization, followed by an incubation of 10 min with 5 μg/mL propidium iodide and finally diluted 21 times with cold PBS prior to acquisition by flow cytometry. The number of GFP⁺ PI- sporozoites from the negative control group was used to normalize the sporozoite recovery across samples. Viability was defined as the percentage of GFP⁺ PI- sporozoites compared to the negative control. Data was analyzed using the CytExpert 2.0 software. [1472] As demonstrated, in FIG.25D, sera from mice immunized with certain RNA constructs reduced viable sporozoites in suspension (exhibited by a mean of at least about 80% viable sporozoite) as compared to sera from mice administered a vehicle (exhibited by a mean of at least about 95% viable sporozoite). Further, as demonstrated in FIG.25E, sera from mice immunized with certain RNA constructs greatly reduced viable sporozoites in 3D (i.e., Matrigel) (exhibited by a mean of at least about 40% viable sporozoite). Sera from mice immunized with anti-PfCSP 2A10 mAb IV greatly reduced viable sporozoites in suspension (exhibited by a mean of at least about 0% viable sporozoite) and in 3D (i.e., Matrigel) (exhibited by a mean of at least about 10% viable sporozoite). [1473] The cytotoxicity of serum from mice immunized with RNA constructs 2, 22, 23, 29, and 39 was evaluated both in suspension (in PBS) and in a 3D Matrigel matrix as described above across three experiments. As shown in FIG.25I-25J, in Experiment 1, the highest impact in sporozoite viability in PBS was observed for RNA constructs 2, 23 and 22. In Experiments 2 and 3, the lowest viability was observed for sporozoites incubated with sera from mice immunized with RNA constructs 2, 23, 29 and 22, similarly to what was observed for the positive control, Mosquirix®. The decrease in viability of the sporozoites was more pronounced when the incubation was done in Matrigel than when it was done in PBS. [1474] Thus, the present Example demonstrates that certain provided RNA constructs induce an immune response characterized by production of antibodies that are shown to differentially reduce viable sporozoites as assessed using a cytotoxicity assay. For example, in suspension, sera from mice immunized with most RNA constructs tested reduced viable sporozoites (exhibited by a mean of at least about 80% viable sporozoite) compared to vehicle, while sera from mice immunized with all tested RNA constructs reduced viable sporozoites in 3D (i.e., Matrigel) (exhibited by a mean of at least about 40% viable sporozoite) (FIGS.25D-E and FIGS.25I – 25I ). (10) In vitro gliding Assay [1475] Provided polyribonucleotides can be assessed for their ability to induce production of antibodies with an inhibitory effect on sporozoite motility. In some embodiments, a polyribonucleotide is determined to induce a useful immune response if serum from a subject (e.g., a mouse) immunized with such construct is shown to reduce sporozoite gliding speed in an In vitro gliding assay, as described herein. [1476] In the gliding assay, 5,000 PbPf sporozoites were resuspended in Dulbecco’s modified Eagle medium (DMEM) and incubated with 5% serum (from mice immunized with either a positive control anti-PfCSP 2A10 mAb IV or with RNA constructs (as described in Example 5). The resulting suspension was transferred to an 18-well slide and centrifuged at 400 ×g for 3 min at 4°C. The slide was then allowed to equilibrate at 37°C, 5% CO₂ for 3 min in the incubation chamber (Incubation System S) of an inverted epifluorescence wide-field microscope (AxioObserver Z.1) equipped with an LED illumination system (Colibri2), a CCD camera (AxioCam MR) and controlled by the AxioVision software (version 4.8.2.0). Time-lapse movies were then recorded for 2 min at a rate of one image per second with an EC “Plan- Neofluar” 10×/0.3 objective using a 470 nm LED and a matching filter cube (43HE) to excite and detect GFP and thus visualize sporozoites. Average sporozoite velocity over the first 2 min of the acquisition was determined using the MTrack2 plug-in from Fiji. [1477] As shown in FIG.25B, sporozoites incubated with serum from mice immunized with RNA constructs 41, 23, 28, 29 or 22 or those passively immunized with 2A10, displayed a similar decrease in gliding speed in comparison with sporozoites incubated with serum from mice immunized with vehicle alone. [1478] Three sporozoites gliding experiments were performed to assess RNA constructs 2, 22, 23, 29, and 39 specifically. As shown in FIG.25G, in all experiments, all of the RNA constructs showed an inhibition of the gliding motility of sporozoites in comparison to the vehicle groups. In Experiment 1, the strongest inhibition of gliding was observed for RNA constructs 23, 29 and 22, and to a similar extent as the inhibition observed for the 2A10 group. In Experiment 2, the strongest inhibition was observed for RNA construct 23, similarly to Mosquirix®. In Experiment 3, inhibition of gliding was very similar for all the tested constructs, and also for Mosquirix®. [1479] Thus, the present Example demonstrates that most RNA constructs compared to vehicle induced an immune response characterized by production of antibodies that are shown to reduce motility of sporozoites, e.g., assessed using an in vitro gliding assay. For example, RNA constructs 41, 23, 28, 29 and 22 induced an immune response characterized by production of antibodies that are shown to reduce motility of sporozoites similar to the positive control. (11) Total Binding and Dissociation from PfCSP Full Length Protein or Specific Peptides by SPR [1480] Binding and dissociation of the antibodies present in serum from mice immunized with RNA constructs to biotinylated full length PfCSP, junction + minor repeats peptide or major repeats peptide was determined by Surface Plasmon Resonance (SPR). Polypeptides used in the SPR measurements are provided in Table 25 below. Briefly, biotinylated full length P fCSP, junction + minor repeats peptide and major repeats peptide were each immobilized to a different flow cell of a Biacore T200 instrument, while the fourth flow cell was left empty as reference. Serum samples were diluted in analysis buffer (10 mM HEPES (pH 7.4), 150 mM NaCl, 3 mM EDTA, 0.05% Tween 20, 0.22 μm filtered) and ran using a flow rate of 10 μL/min for interaction analysis of the analyte (association and dissociation). Association of the antibodies in the serum was measured for 5 min, while dissociation was measured for 15 min. Analysis was performed in triplicates with individually prepared dilutions. Buffer blanks were implemented regularly and used for referencing. Evaluation of serum sample binding data was performed with regard to two parameters: a) height of binding signals, as relative comparison of the titer, and b) assessment of antibody:antigen complex stability based on dissociation, by calculating the binding signal after 5 min and 15 min, which was determined by calculating the dissociation relative to the maximal signal (% residual response). The higher the % residual response value the higher the complex stability. Table 25: Polypeptides used in the SPR measurements.

[1481] As shown in FIGS.62A, 62C, and 62E, ability of antibodies generated upon immunization with different RNA constructs to bind full length PfCSP, a peptide with a junction region and minor repeats, or a peptide with major repeats was assessed by SPR. Highest binding to full length PfCSP was observed for RNA constructs 42, 8, 26, 23, 45, 39, 22, 89, 175, 98, 99 and 91. Highest binding to a peptide with a junction region and minor repeats was observed for RNA constructs 39, 41, 2, 42, 8, 26, 2345, 25, 89, 92, 175, 98, 99, 91, and 104. Finally, highest binding to a peptide with major repeats was observed for RNA constructs 2, 42, 8, 26, 23, 45. 22, 89, 175 and 99. [1482] As shown in FIG.62B, 62D, and 62F, dissociation of antibodies generated upon immunization with different RNA constructs to the three antigens (full length PfCSP, a peptide with a junction region and minor repeats, or a peptide with major repeats) was also assessed by determining percentage of residual binding after 15 min of dissociation, as a measurement of the strength of the interaction between antibodies and the antigens. All tested constructs shown in FIG.62B and FIG.62F showed 50% or more residual binding for full length PfCSP. Highest residual binding (reflecting slower dissociation) from full length PfCSP protein was observed for RNA constructs 26, 39, 8, 23, 22, 89, 175, 98, 87, 88, and 91. The highest residual binding to the junction+minor repeats peptide was observed for RNA constructs 39, 41, 25, 26, 23 and 42, 89, 175, 98, 99, and 91. Finally, the highest residual binding to the major repeats peptide was observed for Mosquirix®, RNA constructs 26, 8, 23, 2, 39, 22, 89, 175, 98, 99, and 91. Example 7: Protection Studies of Exemplary Polyribonucleotides Encoding Plasmodium CSP Polypeptide Constructs [1483] The present Example documents the ability of certain polyribonucleotides, provided by the present disclosure, to induce immune responses, as assessed in mice. [1484] Provided polyribonucleotides can be assessed for their ability to protect a subject from sporozoite challenge. In some embodiments, a provided polyribonucleotide is determined to induce a useful immune response if a subject (e.g., a mouse) immunized with a polyribonucleotide and injected with sporozoites demonstrated a reduced level of infection as assessed by monitoring blood parasitemia, e.g., in a challenge assay as described herein. [1485] A challenge assay was performed in which C57BL/6 female mice (7-week-old, ~20 g at day 0) were immunized intramuscularly (IM) twice, on days 0 and 21, with 1 μg of a RNA construct (as described in Example 4) or injected with vehicle (n=7 mice/group). Blood samples were collected on days 7, 14, 20, 28, 35, 42, and 49 for analysis of antibody titers and functionality in serum. Sporozoite challenge was performed at day 50 by micro- injection of 5000 Plasmodium falciparum CSP-expressing Plasmodium berghei ANKA GFP-fluorescent sporozoites freshly dissected from the salivary glands of infected female Anopheles mosquitoes. Protection against infection was assessed by monitoring blood parasitemia by flow cytometry until experimental day 60 (day 10 after challenge). The positive control group was passively immunized with 100 μg of anti-PfCSP 2A10 mAb IV, one day before infection. [1486] Antibody titers were assessed by ELISA as described above in Example 6. Pre-challenge samples (day 49) were also used in functionality tests that include a fixed sporozoite assay, an inhibition of sporozoite motility assay, an assay to quantify cytotoxic activity of generated antibodies, and an assay that evaluated occurrence of CSP precipitation reaction as described above in Example 6 (data are shown in Example 6). Animals were divided into multiple treatment receiving groups, as exemplified in Table 26. Table 26: General study plan for challenge studies with CSP constructs F1, F2, F3,…, F8 = LNP formulations comprising RNA construct with modified nucleotides 2A10 – mouse monoclonal antibody against PfCSP major repeats BC = Blood collection / Serum generation Pre-immune serum collected at day -7 from all the mice N/A – not applicable [1487] As shown in FIG.23A, mice immunized with polyribonucleotide encoding a full length CSP construct (RNA construct 2, described in Example 4) exhibited the highest level of protection after challenge with PfCSP- expressing P. berghei sporozoites with 6 out of 7 mice surviving at day 10. Five out of 7 mice immunized with polyribonucleotide encoding full length CSP constructs (RNA constructs 26, 28, 42), a polyribonucleotide encoding a ΔN-term malarial polypeptide construct (RNA construct 22) and a polyribonucleotide encoding a malarial polypeptide construct that only included major repeats and the C-term (RNA construct 29) were protected, which was comparable to protection following immunization with the positive control anti-PfCSP 2A10 mAb IV. Constructs 45, 23, 39, 8, 41 and 35 protected less than 4 mice following challenge, and immunization with RNA constructs 31, 33, 34 and 24 provided no protection. As shown in FIG.23B-C, mice immunized with all tested RNA constructs showed high titers when measured in an ELISA assay against PfCSP full length protein at days 35 and 49, respectively. [1488] Thus, the present Example demonstrates that certain polyribonucleotides effectively induced an immune response sufficient to inhibit infection by PfCSP-expressing P. berghei parasites in some of the mice. For example, RNA construct 2 protected about 85% of mice following challenge, and RNA constructs 22, 26, 28, 29, and 42 protected about 70% of mice following challenge. [1489] For selected constructs the challenge experiment was repeated twice (Experiment 2 and Experiment 3) as described above, except that the positive control was changed in these two experiments and mice were immunized twice IM with 5 μg of Mosquirix as positive control. [1490] The results are shown in FIG.24. As is evident from FIG.24A, three challenge experiments were performed in total with RNA constructs 2, 22, 23, 29 and 39. Results from experiment 1 were described above. In experiment 2, all vehicle mice had blood stage parasitaemia by day 4 post sporozoite injection, whereas 1/7 mice immunized with ERMA 22 were protected, 3/7 mice immunized with ERMA2 and ERMA29 were protected, and 4/7 mice immunized with ERMA39 were protected against infection. All mice from both the ERMA23-immunized group and the Mosquirix immunized group remained uninfected until day 11 post sporozoite challenge and were therefore fully protected. In experiment 3, blood stage infection was detected in all vehicle control mice already on day 3 post sporozoite injection. Six out of 7 mice immunized with Mosquirix were fully protected, 5/7 mice immunized with ERMA2 were protected, immunization with ERMA23 protected 4/7 mice against infection, and mice immunized with ERMA29, ERMA22 and 39 protected less than 4 mice out of 7. As shown in FIG.24B, mice immunized with RNA constructs 2, 22, 23, 29 and 39 showed high titers when measured in an ELISA assay against PfCSP full length protein at days 35 and 49, respectively. Example 8: In vivo Immunogenicity in Mice Following Administration of an Exemplary Combination of Polyribonucleotides Encoding Plasmodium CSP Polypeptide Constructs and Polyribonucleotides Encoding Plasmodium T-cell string Polypeptide Constructs [1491] The present Example demonstrates that exemplary polyribonucleotides encoding different malarial polypeptide, as described herein, are immunogenic in vivo. [1492] The combination of ERMA 23-7, Mas3a, and Mas4f was evaluated in vivo in an immunogenicity study in mice, to identify possible interferences between the different components. [1493] Briefly, HLA-A02 mice were injected IM on Days 0 and 21 with one of three combination doses: ERMA 23-7 (1 μg) was combined with different amounts of Mas3a and Mas4f (0.5 μg, 1 μg or 2 μg of each construct), referred to herein as Compositions 1, 2 and 3, respectively. As controls, three groups were administered IM injections on Days 0 and 21 of either 0.5 μg, 1 μg or 2 μg/animal of a combination of Mas3a+ Mas4f (at ratio 1:1), and one group was administered with 1 μg/animal of ERMA 23-7. The vehicle control group (n=5) was injected with saline on the same days. Blood samples were collected on Days 21 and 35 for analysis of antibody titers in the serum. At the end of the experiment (Day 35), mice were sacrificed and splenocytes were isolated and used for T-cell activation analyses as described above in Example 6. [1494] Endpoint antibodies titers against PfCSP-FL were assessed by ELISA for serum samples collected on Day 21 (pre-boost) and Day 35 (post-boost), as described in Example 6. As shown in FIG.57A and FIG.57B, immunization with ERMA 23-7 alone or with the compositions elicits an antibody response against PfCSP that was detectable on both days analyzed, with the titers at Day 35 being >10x higher than those at Day 21. At the end of the experiment, there were no significant differences between the PfCSP-specific immunoglobulin G (IgG) response to the combination doses when compared to ERMA 23-7 alone, confirming that combining Mas3a and Mas4f with ERMA 23-7 does not interfere with the IgG response elicited by the latter. [1495] A multiplex assay as described in Example 6 was used to quantify the binding of antibodies to 10 specific PfCSP epitopes of the central region of the protein (that spans from the end of the N-terminal domain until the major repeats) (FIG.55A). [1496] The antibodies generated upon immunization with ERMA 23-7 alone or in combination with Mas3a and Mas4f showed a similar pattern of binding to the central region of PfCSP, as shown in FIG.58. Similarly to the group immunized with ERMA 23-7, all compositions had the highest binding for peptides 19C and 20C, which include the junction, and to 27C and 29C, which include the terminal region of minor repeats, and the major repeats region (FIG.55A and FIG.58). [1497] For all epitopes which are well recognized by sera from animals immunized with ERMA 23-7, inclusion of Mas3a and Mas4f did not impair antibody responses to the CSP construct ERMA 23-7. [1498] To assess T-cell responses, mice were euthanized on Day 7 and/or Day 35 and splenocytes were isolated for IFNɣ ELISpot analysis following stimulation with overlapping peptide pools specific for regions of CSP, LSAP2, TRAP, UIS3, ETRAMP10.3, LSA1a, LSA1b, LISP2 and LISP1 contained in Mas3a and Mas4f, as described in Example 3. In the case of PfCSP, the pool designated “CSP” probed the region of the PfCSP present in Mas3a while peptide pool designated “CSP-FL” probed the PfCSP-FL in ERMA 23-7, as described in Example 6. [1499] At Day 35 post-immunization antigen-specific IFNɣ T-cell responses above the levels observed in the vehicle control group (saline) were detected for all components of Mas3a and Mas4f at all tested doses, a representative example is shown in FIG.59 for mice that were administered Composition 3, the highest combination dose. [1500] Next, T-cell responses induced upon administration of Mas3a and Mas4f with and without ERMA 23-7 were compared. No significant differences were detected in the levels of antigen-specific IFNɣ T-cell responses induced upon administration of Mas3a and Mas4f alone or in combination with ERMA 23-7, except in the case of PfCSP-specific T-cell responses where combined administration appeared to boost the response (FIG.60A). Similar results were observed for Composition 1 and Composition 2. The “CSP-FL” peptide pool was used to assess T-cell responses elicited by ERMA 23-7 and significantly higher levels of antigen-specific IFNγ-T-cell responses were observed upon combined administration of ERMA 23-7 with Mas3a and Mas4f in comparison to ERMA 23-7 alone (FIG.60B). Therefore, combination of Mas3a and Mas4f with ERMA 23-7 does not interfere with the T-cell responses induced by Mas3a and Mas4f alone. [1501] In conclusion, the immunogenic responses observed for the exemplary combination of ERMA 23-7 and Mas3a+ Mas4f did not negatively impact those observed with the individual components. In particular, the co- immunization of Mas3a and Mas4 f and ERMA 23-7 did not negatively affect the humoral responses against PfCSP elicited by the ERMA 23-7 component. Overall, the data shown herein support a combination of Mas3a, Mas4f and ERMA 23-7 is suitable as a multi-antigen multi-specific anti-malaria vaccine. Example 9: In vivo Immunogenicity in Humans Following Administration of an Exemplary Combination of Polyribonucleotides Encoding Plasmodium CSP Polypeptide Constructs and Polyribonucleotides E [ 1502] The present Example demonstrates that exemplary polyribonucleotides encoding different malarial polypeptide, as described herein, can be immunogenic in vivo in humans. Specifically, the present Example provides a randomized, dose-escalation trial for the evaluation of safety, tolerability, and immunogenicity of formulated RNA constructs and combination thereof as provided herein (“Part A”). The present Example also provides a randomized, dose-escalation trial for the evaluation of efficacy of formulated RNA constructs and combination thereof as provided herein (“Part B”). [1503] The exemplary formulated RNA constructs to be assessed in this Example includes ERMA 23-7, Mas3a, Mas4f, and combinations thereof. Inclusion Criteria – Part A [1504] Subjects to be included in Part A of a trial as described in this Example: i. Are aged 18 to 55 years. ii. Have a body mass index over 18.5 kg/m² and under 35 kg/m² and weigh at least 45 kg at an initial visit (“Visit 0”). iii. Are healthy, in the clinical judgment of a health practitioner (e.g., a trial investigator) based on reported medical history data, physical examination, 12-lead electrocardiogram (ECG), vital signs, and clinical laboratory test outcomes. Healthy subjects with pre-existing stable disease (e.g., obesity, hypertension, etc.), defined as disease but not requiring significant change in therapy or hospitalization for worsening disease during the three months (e.g., 90 days) before Visit 0, can be included. iv. Agree not to enroll in another trial with an investigational medicinal product (“IMP”) starting from Visit 0 and until 12 weeks after receiving a third dose of a formulated RNA construct or a combination of formulated RNA constructs. v. Have not traveled and agree not to travel to a malaria-endemic region, as defined per Centers for Disease Control and Prevention (CDC) starting 6 months before Visit 0 and continuously until 28 days after receiving a third dose of a formulated RNA construct or a combination of formulated RNA constructs. vi. Have tested negative human immunodeficiency virus (HIV) -1 and -2 blood test result at Visit 0. vii. Have a negative Hepatitis B surface antigen (HBsAg) test result at Visit 0 and negative anti Hepatitis C virus (anti-HCV) antibodies, or negative HCV PCR test result if the anti-HCV is positive at Visit 0. viii. If a subject has childbearing potential, the subject has a negative serum beta-human chorionic gonadotropin (β-HCG) pregnancy test result at Visit 0 and negative urine pregnancy test results before each administration of a formulated RNA construct or a combination of formulated RNA constructs. Subjects born female who are postmenopausal or permanently sterilized are not be considered to have childbearing potential. ix. If a subject has childbearing potential, the subject agree to practice a highly effective form of contraception starting at Visit 0 and continuously until 90 days after receiving a third dose of a formulated RNA construct or a combination of formulated RNA constructs. x. If a subject has childbearing potential, the subject agree not to donate or cryopreserve eggs (ova, oocytes) for the purposes of assisted reproduction during trial, starting at Visit 0 and continuously until 90 days after receiving a third dose of a formulated RNA construct or a combination of formulated RNA constructs. xi. If a subject is male, does not have had a vasectomy and are sexually active with partners of childbearing potential agree to use condoms and to practice a highly effective form of contraception with their sexual partners of childbearing potential during the trial, starting at Visit 0 and continuously until 90 days after receiving a third dose of a formulated RNA construct or a combination of formulated RNA constructs. xii. If a subject is male, will refrain from sperm donation, starting at Visit 0 and continuously until 90 days after receiving a third dose of a formulated RNA construct or a combination of formulated RNA constructs. Exclusion Criteria – Part A [1505] Subjects with the following are excluded from Part A of a trial described in the present Example: i. A history of Plasmodium parasitemia (any species) based on subject-reported medical history. ii. A prior residence for greater than 6 months continuously in a malaria-endemic region as defined per CDC at any point during their lifetime. iii. Participation in breastfeeding or an intention to become pregnant or to father children starting with Visit 0 and continuously until 90 after receiving a third dose of a formulated RNA construct or a combination of formulated RNA constructs. iv. A history of any serious adverse reactions to vaccines or to vaccine components such as lipids, and including history of anaphylaxis and related symptoms such as hives, respiratory difficulty, angioedema, and/or abdominal pain (not excluded from participation: a subject who had an anaphylactic adverse reaction to pertussis vaccine as a child). v. Existence or history of the following medical conditions: a. Uncontrolled or moderate or severe respiratory diseases (e.g., asthma, chronic obstructive pulmonary disease); symptoms of asthma severity as defined in the US National Asthma Education and Prevention Program Expert Panel report, 2020 - e.g., exclude a volunteer who: i. Uses a short-acting rescue inhaler (typically a beta 2 agonist) daily, or ii. Uses high dose inhaled corticosteroids (per American Academy of Allergy Asthma & Immunology), or iii. In the past year has either of the following: 1. Greater than one exacerbation of symptoms treated with oral/parenteral corticosteroids; or 2. Needed hospitalization, or intubation for asthma; b. Diabetes mellitus type 1 or type 2, including cases controlled with diet alone or elevated hemoglobin A1C (HbA1c) ≥6.5% at screening (not excluded: history of isolated gestational diabetes); c. Hypertension: i. If a person has a history of hypertension, or elevated blood pressure detected during screening, exclude for blood pressure that is not well controlled. Well controlled blood pressure is defined as consistently ≤140 mm Hg systolic and ≤90 mm Hg diastolic, with or without medication, with only isolated, brief instances of higher readings, which must be ≤150 mm Hg systolic and ≤100 mm Hg diastolic at screening and enrollment; d. Malignancy within 5 years of screening, excluding localized basal or squamous cell skin cancer; e. Any current or history of cardiovascular diseases, (e.g., myocarditis, pericarditis, myocardial infarction, congestive heart failure, cardiomyopathy or clinically significant arrhythmias), unless such disease is not considered relevant for participation in this trial in a health practitioner’s (e.g., investigator’s) judgment; f. An abnormal screening ECG (i.e., showing the corrected QT interval by Fridericia (QTcF) >150 ms; significant ST-T wave changes suggestive of myocardial ischemia or of an acute or indeterminate- age myocardial infarction; left ventricular hypertrophy; any non-sinus rhythm including isolated premature ventricular contractions; complete right or left bundle branch block [QRS >120 ms]; second-or third-degree atrioventricular [AV] block); or other clinically significant abnormalities on the ECG at the investigator’s discretion; g. Bleeding disorder diagnosed by a doctor (e.g., factor deficiency, coagulopathy, or platelet disorder requiring special precautions); or h. Seizure disorder: History of seizure(s) within past 3 years. Also exclude if volunteer has used medications in order to prevent or treat seizure(s) at any time within the past 3 years. vi. Documented major psychiatric illness, including bipolar disorder, major depressive disorder, schizophrenia, autism, and attention deficit-hyperactivity disorder that at the discretion of the investigator could interfere with participation and follow-up as outlined by the trial. vii. The following diseases associated with immune dysregulation: a. Primary immunodeficiencies; b. History of solid organ or bone marrow transplantation; c. Asplenia: any condition resulting in the absence of a functional spleen; or d. Existence or history of autoimmune disease including and not limited to thyroid autoimmune disease, multiple sclerosis, psoriasis, etc. viii. Previous vaccination with an approved or investigational malaria vaccine at any time or having taken part in a human malaria challenge study. ix. Receipt of any investigational product within 28 days before Visit 0. x. Any planned non-trial vaccinations starting at Visit 0 and continuously until 28 days after a third dose of a formulated RNA construct or a combination of formulated RNA constructs. Seasonal influenza and COVID- 19 vaccines are allowed; however, they should be administered at least 14 days before or 28 days after any IMP administration. Emergency vaccinations, such as tetanus, are allowed to be administered when medically indicated. xi. Received blood/plasma products, monoclonal antibodies or immunoglobulin within 120 days before Visit 1 or planned administration starting at Visit 0 and continuously until Visit 21. xii. Received allergy treatment with antigen injections within 28 days before and after each IMP administration. xiii. Current or planned treatment with immunosuppressive therapy, including systemic corticosteroids (if systemic corticosteroids are administered for ≥14 days at a dose of ≥20 mg/d of prednisone or equivalent) starting at Visit 0 and continuously until a third dose of a formulated RNA construct or a combination of formulated RNA constructs. Intraarticular, intrabursal, or topical (skin or eyes) corticosteroids are permitted. xiv. Have a history of alcohol abuse or drug addiction within 1 year before Visit 0 or have a history (within the past 5 years) of substance abuse, which in the opinion of a health practitioner (e.g., an investigator), could compromise their wellbeing if they participate as a subject in a trial, or that could prevent, limit, or confound the protocol specified assessments. xv. Any existing condition which may affect vaccine injection and/or assessment of local reactions at the injection site, e.g., tattoos, severe scars, etc. xvi. Are vulnerable individuals as per International Council for Harmonisation (ICH) E6 definition, i.e., are individuals whose willingness to volunteer in a clinical trial may be unduly influenced by the expectation, whether justified or not, of benefits associated with participation, or of a retaliatory response from senior members of a hierarchy in case of refusal to participate. xvii. Any screening hematology and/or blood chemistry laboratory value that meets the definition of a Grade ≥2 abnormality or a Grade 1 abnormality at a health practitioner’s (e.g., an investigator’s) discretion at Visit 0. Subjects with abnormal but not clinically significant parameters not included in the toxicity guidance may be considered eligible at discretion of a health practitioner (e.g., an investigator). Trial – Part A [1506] In Part A, ERMA 23-7, Mas3a, Mas4f, and a combination thereof is evaluated in different dose combinations in a 3 dose schedule to select a safe, tolerable, and immunogenic dose combination, and to assess the impact of third dose on immunogenicity. [1507] To assess safety, tolerability, and immunogenicity of the combination, subjects are divided into cohorts. Cohorts are randomized 5:1 active:placebo. Evaluation uses a staggered dose-escalation schema with sentinel subjects in all cohorts. Different cohorts receive different doses of ERMA 23-7, Mas3a, and Mas4f. Table 27 summarizes the cohorts and exemplary formulated RNA constructs for administration. [1508] A placebo cohort that receives isotonic NaCl solution (0.9%) is also assessed. Table 27: Summary of Cohorts and Administered Formulated Constructs [1509] For cohorts 1 to 9, a first dose of a composition (comprising one or more RNA constructs as set out in Table 27) is administered to subject on Day 1. Approximately eight weeks later, a second dose of the composition is administered to the subject. A third dose is administered approximately 18 weeks after the second dose. For Cohort 10, a first dose of a composition (comprising one or more RNA constructs as set out in Table 27) is administered to subject on Day 1. Approximately four weeks later, a second dose of the composition is administered to the subject. A third dose is administered approximately 4 weeks after the second dose. One or more of the dose levels tested in Cohorts 1 to 9 will subsequently be tested with an alternate dosing schedule in Cohort 10, without sentinel dosing. [1510] Subjects are assessed for the following primary outcome measures after each dose of a formulated RNA construct or a combination of formulated RNA constructs: i. Frequency of solicited local reactions at the injection site (e.g., pain, erythema/redness and/or induration/swelling) recorded up to 7 days after each dose; ii. Frequency of solicited systemic reactions (vomiting, diarrhea, headache, fatigue, muscle/joint pain, and fever) recorded up to 7 days after each dose; iii. Frequency of subjects with at least one AE occurring until 28 days after each dose; and iv. Frequency of subjects with at least one medically attended adverse event (MAAE) occurring until 28 days after each dose. [1511] Subjects are assessed to determine a frequency of subjects in each cohort with at least one SAE occurring until 24 weeks after a third dose. [1512] Descriptive statistics on antibody levels at assessed time points are obtained. Inclusion Criteria – Part B [1513] Subjects to be included in Part B of a trial as described in this Example also: i. Are aged 18 to 55 years. ii. Have a body mass index over 18.5 kg/m² and under 35 kg/m² and weigh at least 45 kg at an initial visit (“Visit 0”). iii. Are healthy, in the clinical judgment of a health practitioner (e.g., a trial investigator) based on reported medical history data, physical examination, 12-lead electrocardiogram (ECG), vital signs, and clinical laboratory test outcomes. Healthy subjects with pre-existing stable disease (e.g., obesity, hypertension, etc.), defined as disease but not requiring significant change in therapy or hospitalization for worsening disease during the three months (e.g., 90 days) before Visit 0, can be included. iv. Agree not to enroll in another trial with an IMP starting from Visit 0 and until 28 days after receiving a CHMI. v. Have not traveled and agree not to travel to a malaria-endemic region, as defined per Centers for Disease Control and Prevention (CDC) starting 6 months before Visit 0 and continuously until 28 days after receiving a CHMI. vi. Have tested negative human immunodeficiency virus (HIV) -1 and -2 blood test result at Visit 0. vii. Have a negative Hepatitis B surface antigen (HBsAg) test result at Visit 0 and negative anti Hepatitis C virus (anti-HCV) antibodies, or negative HCV PCR test result if the anti-HCV is positive at Visit 0. viii. If a subject has childbearing potential, the subject has a negative serum beta-human chorionic gonadotropin (β-HCG) pregnancy test result at Visit 0 and negative urine pregnancy test results before each administration of a formulated RNA construct or a combination of formulated RNA constructs. Subjects born female who are postmenopausal or permanently sterilized will not be considered to have childbearing potential. ix. If a subject has childbearing potential, the subject agrees to practice a highly effective form of contraception starting at Visit 0 and continuously until 90 days after receiving a third dose of a formulated RNA construct or a combination of formulated RNA constructs. x. If a subject has childbearing potential, the subject agrees not to donate or cryopreserve eggs (ova, oocytes) for the purposes of assisted reproduction during trial, starting at Visit 0 and continuously until 90 days after receiving a third dose of a formulated RNA construct or a combination of formulated RNA constructs. xi. If a subject is male, does not have had a vasectomy and are sexually active with partners of childbearing potential agrees to use condoms and to practice a highly effective form of contraception with their sexual partners of childbearing potential during the trial, starting at Visit 0 and continuously until 90 days after receiving a third dose of a formulated RNA construct or a combination of formulated RNA constructs. xii. If a subject is male, refrains from sperm donation, starting at Visit 0 and continuously until 90 days after receiving a third dose of a formulated RNA construct or a combination of formulated RNA constructs. xiii. Are willing to refrain from blood donation for 3 years after receiving a CHMI. xiv. Are willing to take curative antimalarial treatment after receiving a CHMI. xv. Are reachable (24/7) by phone during the period between receiving a CHMI and the end of trial. Exclusion Criteria – Part B [1514] Subjects with the following are excluded from Part B of a trial described in the present Example: i. A history of Plasmodium parasitemia (any species) based on subject-reported medical history. ii. A prior residence for greater than 6 months continuously in a malaria-endemic region as defined per CDC at any point during their lifetime. iii. Participation in breastfeeding or an intention to become pregnant or to father children starting with Visit 0 and continuously until 60 days after receiving a controlled human malaria infection (CHMI). iv. A history of any serious adverse reactions to vaccines or to vaccine components such as lipids, and including history of anaphylaxis and related symptoms such as hives, respiratory difficulty, angioedema, and/or abdominal pain (not excluded from participation: a subject who had an anaphylactic adverse reaction to pertussis vaccine as a child). v. Existence or history of the following medical conditions: a. Uncontrolled or moderate or severe respiratory diseases (e.g., asthma, chronic obstructive pulmonary disease); symptoms of asthma severity as defined in the US National Asthma Education and Prevention Program Expert Panel report, 2020 - e.g., exclude a volunteer who: i. Uses a short-acting rescue inhaler (typically a beta 2 agonist) daily, or ii. Uses high dose inhaled corticosteroids (per American Academy of Allergy Asthma & Immunology), or iii. In the past year has either of the following: 1. Greater than one exacerbation of symptoms treated with oral/parenteral corticosteroids; or 2. Needed hospitalization, or intubation for asthma; b. Diabetes mellitus type 1 or type 2, including cases controlled with diet alone or elevated hemoglobin A1C (HbA1c) ≥6.5% at screening (not excluded: history of isolated gestational diabetes); c. Hypertension: i. If a person has a history of hypertension, or elevated blood pressure detected during screening, exclude for blood pressure that is not well controlled. Well controlled blood pressure is defined as consistently ≤140 mm Hg systolic and ≤90 mm Hg diastolic, with or without medication, with only isolated, brief instances of higher readings, which must be ≤150 mm Hg systolic and ≤100 mm Hg diastolic at screening and enrollment; d. Malignancy within 5 years of screening, excluding localized basal or squamous cell skin cancer; e. Any current or history of cardiovascular diseases, (e.g., myocarditis, pericarditis, myocardial infarction, congestive heart failure, cardiomyopathy or clinically significant arrhythmias), unless such disease is not considered relevant for participation in this trial in a health practitioner’s (e.g., investigator’s) judgment; f. An abnormal screening ECG (i.e., showing the corrected QT interval by Fridericia (QTcF) >150 ms; significant ST-T wave changes suggestive of myocardial ischemia or of an acute or indeterminate- age myocardial infarction; left ventricular hypertrophy; any non-sinus rhythm including isolated premature ventricular contractions; complete right or left bundle branch block [QRS >120 ms]; second-or third-degree atrioventricular [AV] block); or other clinically significant abnormalities on the ECG at the investigator’s discretion; g. Bleeding disorder diagnosed by a doctor (e.g., factor deficiency, coagulopathy, or platelet disorder requiring special precautions); or h. Seizure disorder: History of seizure(s) within past 3 years. Also exclude if volunteer has used medications in order to prevent or treat seizure(s) at any time within the past 3 years. vi. Documented major psychiatric illness, including bipolar disorder, major depressive disorder, schizophrenia, autism, and attention deficit-hyperactivity disorder that at the discretion of the investigator could interfere with participation and follow-up as outlined by the trial. vii. The following diseases associated with immune dysregulation: a. Primary immunodeficiencies; b. History of solid organ or bone marrow transplantation; c. Asplenia: any condition resulting in the absence of a functional spleen; or d. Existence or history of autoimmune disease including and not limited to thyroid autoimmune disease, multiple sclerosis, psoriasis, etc. viii. Previous vaccination with an approved or investigational malaria vaccine at any time or having taken part in a human malaria challenge study. ix. Receipt of any investigational product within 28 days before Visit 0. x. Any planned non-trial vaccinations starting at Visit 0 and continuously until 28 days after a third dose of a formulated RNA construct or a combination of formulated RNA constructs. Seasonal influenza and COVID- 19 vaccines are allowed; however, they should be administered at least 14 days before or 28 days after administration of a CHMI. Emergency vaccinations, such as tetanus, are allowed to be administered when medically indicated. xi. Received blood/plasma products, monoclonal antibodies or immunoglobulin within 120 days before Visit 1 or planned administration starting at Visit 0 and continuously until 28 days after administration of a CHMI. xii. Received allergy treatment with antigen injections within 28 days before and after each IMP administration and continuously until 28 days after administration of a CHMI. xiii. Current or planned treatment with immunosuppressive therapy, including systemic corticosteroids (if systemic corticosteroids are administered for ≥14 days at a dose of ≥20 mg/d of prednisone or equivalent) starting at Visit 0 and continuously until and continuously until 28 days after administration of a CHMI. Intraarticular, intrabursal, or topical (skin or eyes) corticosteroids are permitted. xiv. Have a history of alcohol abuse or drug addiction within 1 year before Visit 0 or have a history (within the past 5 years) of substance abuse, which in the opinion of a health practitioner (e.g., an investigator), could compromise their wellbeing if they participate as a subject in a trial, or that could prevent, limit, or confound the protocol specified assessments. xv. Any existing condition which may affect vaccine injection and/or assessment of local reactions at the injection site, e.g., tattoos, severe scars, etc. xvi. Are vulnerable individuals as per International Council for Harmonisation (ICH) E6 definition, i.e., are individuals whose willingness to volunteer in a clinical trial may be unduly influenced by the expectation, whether justified or not, of benefits associated with participation, or of a retaliatory response from senior members of a hierarchy in case of refusal to participate. xvii. Any screening hematology and/or blood chemistry laboratory value that meets the definition of a Grade ≥2 abnormality or a Grade 1 abnormality at a health practitioner’s (e.g., an investigator’s) discretion at Visit 0. Subjects with abnormal but not clinically significant parameters not included in the toxicity guidance may be considered eligible at discretion of a health practitioner (e.g., an investigator). xviii. History of any serious adverse reactions to atovaquone/proguanil or artemether/lumefantrine, including but not limited to anaphylaxis and related symptoms, such as hives, respiratory difficulty, angioedema, and/or abdominal pain. xix. Current or planned treatment with any drug that has antimalarial activity (including, but not limited to artemisinins, TMP-SMX, mefloquine, chloroquine, hydroxychloroquine, atovaquone, tetracycline antibiotics, macrolide antibiotics, quinolone antibiotics, or clindamycin) within 28 days before and after planned administration of a CHMI. xx. Have a history of any SAEs to atovaquone/proguanil and artemether/lumefantrine. xxi. Current or planned use of medications causing drug-interactions with atovaquone-proguanil or an artemisinin-based combination therapy (including, but not limited to cimetidine, metoclopramide, antacids, and kaolin) within 28 days before and after planned administration of a CHMI. Trial – Part B [1515] In Part B, the trial assesses efficacy of a combination of ERMA 23-7, Mas3a, and Mas4f in preventing P. falciparum parasitemia in a homologous controlled human malaria infection (NF54). [1516] In Part B, subjects a divided into two cohorts. Both cohorts receive (i) ERMA 23-7 and (ii) Mas3a and Mas4f in a 1:1 ratio. A first dose is administered to subject on Day 1. Approximately eight weeks later, a second dose of the composition is administered to the subject. A third dose is administered approximately 18 weeks after the second dose. [1517] Doses will be 0 μg, ≤ 10 μg, ≤ 30 μg, ≤ 70 μg, or ≤ 100 μg, e.g., as described above in Part A, Table 27. [1518] A first cohort receives a CHMI via mosquito bite. A second cohort receives a CHMI via direct venous inoculation of P. falciparum sporozoites. [1519] In subjects who received a full dose schedule, underwent a CHMI and did not receive any medication with antimalarial activity before the assessment of a primary endpoint, a number and proportion of subjects protected from blood stage parasitemia 5 days to 28 days after receiving a CHMI is assessed. [1520] Subjects are also assessed for the following primary outcome measures after at least one dose and up to 7 days after receiving a dose: i. Frequency of solicited local reactions at the injection site (pain, erythema/redness, induration/swelling); and ii. Frequency of solicited systemic reactions (vomiting, diarrhea, headache, fatigue, muscle/joint pain, and fever). [1521] Subjects are assessed for the following primary outcome measures after at least one dose and up to 28 days after administration of a dose: i. Frequency of subjects with at least one adverse event; and ii. Frequency of subjects with at least one medically attended adverse event. [1522] Subjects are assessed for the following primary outcome measures after at least one dose and up to 28 days after receiving a CHMI: i. Frequency of subjects with at least one adverse; ii. Frequency of subjects with at least one medically attended adverse event; and iii. Frequency of subjects in each cohort with at least one serious adverse event. [1523] Time to blood stage parasitemia after receiving a CHMI is assessed by qPCR. Descriptive statistics on antibody levels at assessed time points are also determined. Example 10: In vivo Immunogenicity in Humans Following Administration of an Exemplary Combination of Polyribonucleotides Encoding Plasmodium CSP Polypeptide Constructs and Polyribonucleotides Encoding Plasmodium T-cell string Polypeptide Constructs [1524] The present Example provides a trial for the assessment of the efficacy of a combination of ERMA 23-7, Mas3a, and Mas4f in preventing P. falciparum parasitemia in a homologous controlled human malaria infection following challenge with sporozoites. Subjects for this trial reside in Africa, including certain subjects who reside in Kenya, Tanzania, or Gabon. Subjects may have had pre-exposure to malaria (e.g., P. falciparum). [1525] Subjects are divided into two cohorts. Both cohorts receive (i) ERMA 23-7 and (ii) Mas3a and Mas4f. A first dose is administered to subject on Day 1. Approximately eight weeks later, a second dose of the composition is administered to subjects in both cohorts. For the second cohort (but not the first cohort), a third dose is administered approximately 16-18 weeks after the second dose. [1526] Four weeks after the last dose received by the first or second cohort, a CHMI is introduced via direct venous inoculation of P. falciparum sporozoites. [1527] Vaccine efficacy is then assessed. As a primary endpoint, vaccine efficacy is assessed by PCR for P. falciparum. Infection is defined as one positive PCR result for P. falciparum. Time to a positive PCR result for P. falciparum is used a secondary endpoint. Example 11: In vivo Immunogenicity in Humans Following Administration of an Exemplary Combination of Polyribonucleotides Encoding Plasmodium CSP Polypeptide Constructs and Polyribonucleotides Encoding Plasmodium T-cell string Polypeptide Constructs [1528] The present Example demonstrates that exemplary polyribonucleotides encoding different malarial polypeptides, as described herein, can be immunogenic in vivo in human subjects that have previously been exposed to malaria (e.g., P. falciparum). Specifically, the present Example provides a randomized, dose-escalation trial for the evaluation of safety, tolerability, and immunogenicity of formulated RNA constructs and combination thereof as provided herein in human subjects that have previously been exposed to malaria (e.g., P. falciparum) (“Part A”). The present Example also provides a randomized, dose-escalation trial for the evaluation of efficacy of formulated RNA constructs and combination thereof as provided herein in human subjects that have previously been exposed to malaria (e.g., P. falciparum) (“Part B”). [1529] Parts A and B of the present Example are performed as described in Example 9 above with the exception that subjects of the present Example are human subjects that have previously been exposed to malaria (e.g., P. falciparum). Human subjects may also be from malaria-endemic regions (e.g., certain countries in Africa or Asia). As such, select inclusion and exclusion criteria relating to prior malarial exposure and presence is certain geographic regions do not apply to the trial of the present Example. EQUIVALENTS [1530] Those skilled in the art will recognize, or be able to ascertain using no more than routine experimentation, many equivalents to the specific embodiments of technologies described herein. The scope of the present disclosure is not intended to be limited to the above Description, but rather is as set forth in the following claims.

Claims

CLAIMS 1. A combination comprising: (i) a first pharmaceutical composition comprising a first polyribonucleotide, wherein the first polyribonucleotide encodes a first polypeptide, and the first polypeptide comprises one or more Plasmodium T-cell antigens; and (ii) a second pharmaceutical composition comprising a second polyribonucleotide, wherein the second polyribonucleotide encodes a second polypeptide, and the second polypeptide comprises one or more Plasmodium polypeptides or antigenic portions thereof.

2. The combination of claim 1, wherein: (a) the first polypeptide comprises an amino acid sequence with at least 85% identity to an amino acid sequence according to any one of SEQ ID NOs: 167, 170, 173, 176, 179, 182, 185, 188, 191, 194, 197, 200, 203, 206, 209, 212, 215, 218, and 221; and (b) the second polypeptide comprises an amino acid sequence with at least 85% identity to an amino acid sequence according to any one of SEQ ID NOs: 5, 8, 10, 12, 15, 18, 21, 24, 27, 30, 33, 36, 39, 42, 45, 48, 51, 54, 57, 60, 63, 66, 69, 72, 75, 78, 81, 84, 87, 90, 93, 96, 99, 102, 105, 107-111, 112, 117, 122, 125, 130, 135, 138, and 141. 3. The combination of claim 1, wherein: (a) the first polypeptide comprises: (i) an antigenic Plasmodium CSP polypeptide fragment, (ii) an antigenic Plasmodium TRAP polypeptide fragment, (iii) an antigenic Plasmodium UIS3 polypeptide fragment, (iv) an antigenic Plasmodium ETRAMP10.

3 polypeptide fragment, and (v) an antigenic Plasmodium LSAP2 polypeptide fragment; and (b) the second polypeptide comprises: (i) a secretory signal, (ii) a Plasmodium CSP N-terminal region, (iii) a Plasmodium CSP N-terminal end region, (iv) a Plasmodium CSP junction region, (v) three repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223), (vi) a Plasmodium CSP major repeat region, (vii) a Plasmodium CSP C-terminal region, and (viii) a transmembrane region.

4. The combination of claim 3, wherein the first polypeptide comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 203.

5. The combination of claim 3 or 4, wherein the second polypeptide comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 33.

6. The combination of any one of claims 3-5, wherein the second polypeptide comprises an amino acid sequence with 100% sequence identity to an amino acid sequence according to SEQ ID NO: 33.

7. The combination of any one of claims 3-6, wherein the combination further comprises a third pharmaceutical composition comprising a third polyribonucleotide, wherein the third polyribonucleotide encodes a third polypeptide, and the third polypeptide comprises: (i) an antigenic Plasmodium LSA-1(a) polypeptide fragment, (ii) an antigenic Plasmodium LSA-1(b) polypeptide fragment, (iii) an antigenic Plasmodium LISP-2 polypeptide fragment, and (iv) an antigenic Plasmodium LISP-1 polypeptide fragment.

8. The combination of claim 7, wherein the third polypeptide comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 209.

9. The combination of claim 1, wherein: (a) the first polypeptide comprises: (i) an antigenic Plasmodium CSP polypeptide fragment, (ii) an antigenic Plasmodium TRAP polypeptide fragment, (iii) an antigenic Plasmodium UIS3 polypeptide fragment, (iv) an antigenic Plasmodium ETRAMP10.3 polypeptide fragment, and (v) an antigenic Plasmodium LSAP2 polypeptide fragment; and (b) the second polypeptide comprises: (i) a secretory signal, (ii) a Plasmodium CSP N-terminal end region, (iii) a Plasmodium CSP junction region, (iv) nine repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223), (v) a Plasmodium CSP C-terminal region, (vi) a serine-valine sequence immediately following the Plasmodium CSP C-terminal region, (vii) a linker, and (viii) a transmembrane region, and wherein the second polypeptide does not comprise any of: (a) a Plasmodium CSP N-terminal region or portion thereof, and (b) an amino acid sequence of NPNA (SEQ ID NO: 228).

10. The combination of claim 9, wherein the first polypeptide comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 203.

11. The combination of claim 9 or 10, wherein the second polypeptide comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 81.

12. The combination of claim 1, wherein: (a) the first polypeptide comprises: (i) an antigenic Plasmodium LSA-1(a) polypeptide fragment, (ii) an antigenic Plasmodium LSA-1(b) polypeptide fragment, (iii) an antigenic Plasmodium LISP-2 polypeptide fragment, and (iv) an antigenic Plasmodium LISP-1 polypeptide fragment; and (b) the second polypeptide comprises: (i) a secretory signal, (ii) a Plasmodium CSP N-terminal region, (iii) a Plasmodium CSP N-terminal end region, (iv) a Plasmodium CSP junction region, (v) three repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223), (vi) a Plasmodium CSP major repeat region, (vii) a Plasmodium CSP C-terminal region, and (viii) a transmembrane region.

13. The combination of claim 12, wherein the first polypeptide comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 209.

14. The combination of claim 12 or 13, wherein the second polypeptide comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 33.

15. The combination of any one of claims 12-14, wherein the second polypeptide comprises an amino acid sequence with 100% sequence identity to an amino acid sequence according to SEQ ID NO: 33.

16. The combination of claim 1, wherein: (a) the first polypeptide comprises: (i) an antigenic Plasmodium LSA-1(a) polypeptide fragment, (ii) an antigenic Plasmodium LSA-1(b) polypeptide fragment, (iii) an antigenic Plasmodium LISP-2 polypeptide fragment, and (iv) an antigenic Plasmodium LISP-1 polypeptide fragment; and (b) the second polypeptide comprises: (i) a secretory signal, (ii) a Plasmodium CSP N-terminal end region, (iii) a Plasmodium CSP junction region, (iv) nine repeats of the amino acid sequence of NANPNVDP (SEQ ID NO: 223), (v) a Plasmodium CSP C-terminal region, (vi) a serine-valine sequence immediately following the Plasmodium CSP C-terminal region, (vii) a linker, and (viii) a transmembrane region, and wherein the second polypeptide does not comprise any of: (a) a Plasmodium CSP N-terminal region or portion thereof, and (b) an amino acid sequence of NPNA (SEQ ID NO: 228).

17. The combination of claim 16, wherein the first polypeptide comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 209.

18. The combination of claim 16 or 17, wherein the second polypeptide comprises or consists of an amino acid sequence with at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence according to SEQ ID NO: 81.

19. The combination of any one of claims 1-18, wherein the one or more Plasmodium T-cell antigens are one or more P. falciparum T-cell antigens.

20. The combination of any one of claims 1-19, wherein the one or more Plasmodium CSP polypeptide regions or portions thereof are one or more P. falciparum CSP polypeptide regions or portions thereof.

21. The combination of any one of claims 1-20, wherein the first polyribonucleotide and/or second polyribonucleotide is an isolated polyribonucleotide.

22. The combination of claim 7 or 8, wherein the third polyribonucleotide is an isolated polyribonucleotide.

23. The combination of any one of claims 1-22, wherein the first polyribonucleotide and/or second polyribonucleotide is an engineered polyribonucleotide.

24. The combination of any one of claims 7, 8, or 22, wherein the third polyribonucleotide is an engineered polyribonucleotide.

25. The combination of any one of claims 1-24, wherein the first polyribonucleotide and/or second polyribonucleotide is a codon-optimized polyribonucleotide.

26. The combination of any one of claims 7, 8, 22, or 24, wherein the third polyribonucleotide is a codon- optimized polyribonucleotide.

27. The combination of any one of claims 1-26, wherein the first polyribonucleotide is comprised in a first RNA construct, wherein the first RNA construct comprises in 5' to 3' order: (i) a 5' UTR; (ii) the first polyribonucleotide; (iii) a 3' UTR; and (iv) a polyA tail sequence.

28. The combination of any one of claims 1-27, wherein the second polyribonucleotide is comprised in a second RNA construct, wherein the second RNA construct comprises in 5' to 3' order: (i) a 5' UTR; (ii) the second polyribonucleotide; (iii) a 3' UTR; and (iv) a polyA tail sequence.

29. The combination of claim 27 or 28, wherein: (i) the 5' UTR of the first and/or second RNA construct comprises or consists of a modified human alpha-globin 5'-UTR; and (ii) the 3' UTR of the first and/or second RNA construct comprises or consists of a first sequence from the amino terminal enhancer of split (AES) messenger RNA and a second sequence from the mitochondrial encoded 12S ribosomal RNA.

30. The combination of any one of claims 27-29, wherein the 5' UTR of the first and/or second RNA construct consists of a ribonucleic acid sequence according to SEQ ID NO: 565.

31. The combination of any one of claims 27-30, wherein the 3' UTR of the first and/or second RNA construct consists of a ribonucleic acid sequence according to SEQ ID NO: 567.

32. The combination of any one of claims 27-31, wherein the polyA tail sequence of the first and/or second RNA construct is a split polyA tail sequence.

33. The combination of claim 32, wherein the split polyA tail sequence consists of a ribonucleic acid sequence according to SEQ ID NO: 569.

34. The combination of any one of claims 27-33, wherein the first and/or second RNA construct further comprise a 5' cap.

35. The combination of claim 34, wherein the first and/or second RNA construct comprise a cap proximal sequence comprising positions +1, +2, +3, +4, and +5 of the polyribonucleotide.

36. The combination of claim 34 or 35, wherein the 5' cap comprises or consists of m7(3’OMeG)(5')ppp(5')(2'OMeA₁)pG₂, wherein A₁ is position +1 of the polyribonucleotide, and G₂ is position +2 of the polyribonucleotide.

37. The combination of claim 35 or 36, wherein the cap proximal sequence comprises A₁ and G₂ of the Cap1 structure, and a sequence comprising: A₃A₄U₅ (SEQ ID NO: 571) at positions +3, +4 and +5 respectively of the polyribonucleotide.

38. The combination of any one of claims 1-37, wherein the first and/or second RNA construct includes modified uridines in place of all uridines.

39. The combination of claim 38, wherein modified uridines are each N1-methyl-pseudouridine.

40. The combination of any one of claims 1-39, wherein the first and/or second pharmaceutical composition further comprises lipid nanoparticles, polyplexes (PLX), lipidated polyplexes (LPLX), or liposomes.

41. The combination of claim 40, wherein the first and/or second polyribonucleotide is fully or partially encapsulated within the lipid nanoparticles, polyplexes (PLX), lipidated polyplexes (LPLX), or liposomes.

42. The combination of any one of claims 1-41, wherein the first and/or second pharmaceutical composition further comprises lipid nanoparticles.

43. The combination of any one of claims 40-42, wherein the first polyribonucleotide is encapsulated within the lipid nanoparticles.

44. The combination of any one of claims 40-43, wherein the second polyribonucleotide is encapsulated within the lipid nanoparticles.

45. The combination of any one of claims 1-44, wherein the first and/or second pharmaceutical composition comprises at least one pharmaceutically acceptable excipient.

46. The combination of any one of claims 1-45 for use in the treatment of a malaria infection.

47. The combination of any one of claims 1-46 for use in the prevention of a malaria infection.

48. A combination comprising: (i) a first pharmaceutical composition comprising a first polyribonucleotide, wherein the first polyribonucleotide encodes a first peptide that comprises or consists of an amino acid sequence with at least 85% sequence identity to an amino acid sequence according to SEQ ID NO: 203; (ii) a second pharmaceutical composition comprising a second polyribonucleotide, wherein the second polyribonucleotide encodes a second peptide that comprises or consists of an amino acid sequence with at least 85% sequence identity to an amino acid sequence according to SEQ ID NO: 33; and (iii) a second pharmaceutical composition comprising a third polyribonucleotide, wherein the third polyribonucleotide encodes a third peptide that comprises or consists of an amino acid sequence with at least 85% sequence identity to an amino acid sequence according to SEQ ID NO: 209.

49. A combination comprising: (i) a first pharmaceutical composition comprising a first polyribonucleotide, wherein the first polyribonucleotide encodes a first peptide that comprises or consists of an amino acid sequence with 100% sequence identity to an amino acid sequence according to SEQ ID NO: 203; (ii) a second pharmaceutical composition comprising a second polyribonucleotide, wherein the second polyribonucleotide encodes a second peptide that comprises or consists of an amino acid sequence with 100% sequence identity to an amino acid sequence according to SEQ ID NO: 33; and (iii) a second pharmaceutical composition comprising a third polyribonucleotide, wherein the third polyribonucleotide encodes a third peptide that comprises or consists of an amino acid sequence with 100% sequence identity to an amino acid sequence according to SEQ ID NO: 209.

50. A method comprising administering a combination of any one of claims 1-49 to a subject.

51. The method of claim 50, wherein the method is a method of treating a malaria infection.

52. The method of claim 50 or 51, wherein the method is a method of preventing a malaria infection.

53. The method of any one of claims 50-52, wherein the subject has or is at risk of developing a malaria infection.

54. The method of any one of claims 50-53, wherein the subject is a human.

55. The method of any one of claims 50-54, wherein administration induces an anti-malaria immune response in the subject.

56. Use of the combination of any one of claims 1-49 in the treatment of a malaria infection.

57. Use of the combination of any one of claims 1-49 in the prevention of a malaria infection.