WO2026010947A1 - Neutralizing antibodies against hiv env - Google Patents

Abstract

The present disclosure relates to anti-HIV antibodies and their use in the treatment or prevention of HIV/AIDS and in the development of HIV vaccines.

Description

NEUTRALIZING ANTIBODIES AGAINST HIV ENV CROSS-REFERENCE TO RELATED APPLICATIONS [0001] This application claims the benefit of priority of U.S. Provisional Application No. 63/667,124, filed July 2, 2024, each of which is herein incorporated by reference in its entirety. REFERENCE TO SEQUENCE LISTING SUBMITTED ELECTRONICALLY: [0002] The content of the electronically submitted sequence listing (Name: 6765_1701_Sequence_Listing.txt; Size: 97,855 bytes; and Date of Creation: June 25, 2025) is incorporated herein by reference in its entirety. FIELD OF THE INVENTION [0003] The field of the invention generally relates to anti-HIV antibodies and their use in the treatment or prevention of HIV/AIDS, and in the development of HIV vaccines. GOVERNMENT INTEREST [0004] This invention was made with government support under Grant Number AI147870 awarded by the National Institutes of Health. The government has certain rights in the invention. BACKGROUND [0005] A key goal in HIV vaccine design is to elicit broadly neutralizing antibodies (bnAbs). Burton & Hangartner, Annu Rev Immunol 34, 635-659 (2016). Most bnAbs to HIV-1 have been cloned from elite donors whose plasma shows broad neutralizing activity. These bnAbs target six distinct sites on the HIV-1 envelope glycoprotein (Env) spike, including the CD4-binding site (CD4bs), V2 apex, N332/V3 base supersite (also referred to as high-mannose patch epitope), silent face, gp120-gp41 interface including the fusion peptide, and membrane-proximal external region (MPER). As bnAbs arise from complex affinity maturation pathways, efforts are underway to dissect the structural and genetic bases of bnAb function to uncover common elements that can simplify vaccine design. Kwong & Mascola, Immunity 48, 855-871 (2018). [0006] Given the absence of an effective vaccine for protection against HIV-1 infection, passive immunization strategies that utilize potent broadly neutralizing antibodies (bnAbs) to block acquisition of HIV-1 are being rigorously pursued in the clinical setting. Walsh & Seaman, Front Immunol. 2021; 12: 712122. bnAbs have demonstrated robust protection in preclinical animal models, and several leading bnAb candidates have shown favorable safety and pharmacokinetic profiles when tested individually or in combinations in early phase human clinical trials. However, the currently available bnAbs fail to neutralize all circulating HIV strains. [0007] Thus, there remains a need for the development of neutralizing antibodies that can be used in the treatment or prevention of HIV/AIDS. BRIEF SUMMARY [0008] In one aspect, provided herein are monoclonal antibodies and antigen-binding fragments thereof that specifically bind to HIV Env. In some embodiments, an antibody described herein is a monoclonal antibody. In some embodiments, an antibody described herein is an engineered antibody. In some embodiments, an antibody described herein is an engineered variant of the N49P7 antibody. In some embodiments, an antibody described herein is a broadly neutralizing antibody (bnAb). In some embodiments, an antibody described herein is a bispecific antibody. In some embodiments, an antibody described herein is a trispecific antibody. In some embodiments, an antibody described herein specifically binds to HIV Env of at least two HIV isolates in the 56 cross-clade virus panel disclosed herein (Table 10). In some embodiments, an antibody described herein specifically binds the Env of at least two, at least three, at least four, or at least five HIV isolates in the 56 cross-clade indicator virus panel. In some embodiments, an antibody described herein specifically binds the Env of the Du422.1, BJOX2000, 6540.v4.c1 or 6545.v4.c1 isolates. [0009] In one aspect, provided herein are pharmaceutical compositions comprising a monoclonal antibody or antigen-binding fragments thereof described herein that specifically binds to HIV Env. [0010] In one aspect, provided herein are isolated polynucleotides encoding a monoclonal antibody or antigen-binding fragments thereof described herein that specifically binds to HIV Env. [0011] In one aspect, provided herein are methods of producing a monoclonal antibody or antigen-binding fragments thereof described herein that specifically binds to HIV Env. [0012] In one aspect, provided herein are methods of neutralizing an HIV virus, comprising contacting the virus with a monoclonal antibody or antigen-binding fragments thereof described herein that specifically binds to HIV Env. [0013] In one aspect, provided herein are methods of reducing the likelihood of HIV infection in a subject exposed to HIV comprising administering to the subject a monoclonal antibody or antigen-binding fragments thereof described herein that specifically binds to HIV Env. [0014] In one aspect, provided herein are methods of treating HIV/AIDS comprising administering to a subject in need thereof a monoclonal antibody or antigen-binding fragments thereof described herein that specifically binds to HIV Env. [0015] In one aspect, provided herein are methods of reducing viral load comprising administering to a subject in need thereof a monoclonal antibody or antigen-binding fragments thereof described herein that specifically binds to HIV Env. [0016] In one aspect, provided herein are methods of producing an engineered variant of a monoclonal antibody or antigen-binding fragments thereof described herein that specifically binds to HIV Env. [0017] In one aspect, provided herein are methods of identifying an agent as an HIV vaccine candidate, comprising contacting a protein with an antibody or antigen-binding fragment thereof described herein under conditions sufficient to form an immune complex and detecting the presence of the immune complex. [0018] In some embodiments, the disclosure provides: [1.] An isolated monoclonal antibody that is capable of binding HIV Env and comprises a heavy chain variable region (VH) comprising a VH CDR1, VH CDR2, and VH CDR3 and a light chain variable region (VL) comprising a VL CDR1, VL CDR2, and VL CDR3, wherein the VH CDR1, VH CDR2, VH CDR3, VL CDR1, VL CDR2, and VL CDR3 comprise the amino acid sequence of the eN49P7-FRv1-23, eN49P7-FRv1-65 or eN49P7- FRv1-85 VH CDR1, VH CDR2, VH CDR3, VL CDR1, VL CDR2, and VL CDR3, respectively. [2.] The isolated monoclonal antibody of [1], wherein the VH comprises an amino acid sequence that is at least about 90%, 95%, 97%, 98%, 99% or 100% identical to the eN49P7- FRv1-23 VH, eN49P7-FRv1-65 VH or eN49P7-FRv1-85 VH.. [3.] The isolated monoclonal antibody of [1] or [2], wherein the VL comprises an amino acid sequence that is at least about 90%, 95%, 97%, 98%, 99% or 100% identical to eN49P7-FRv1-23 VL, eN49P7-FRv1-65 VL or eN49P7-FRv1-85 VL. [4.] The isolated monoclonal antibody of any one of [1] to [3], wherein the VH comprises the eN49P7-FRv1-23 VH, eN49P7-FRv1-65 VH or eN49P7-FRv1-85 VH and the VL comprises the eN49P7-FRv1-23 VL, eN49P7-FRv1-65 VL or eN49P7-FRv1-85 VL. [5.] The monoclonal antibody of any one of [1] to [4], further comprising a heavy and/or light chain constant region. [6.] The monoclonal antibody of any one of [1] to [4], further comprising a human heavy and/or light chain constant region. [7.] The monoclonal antibody of [5] or [6], wherein the heavy chain constant region is selected from the group consisting of a human immunoglobulin IgG1, IgG2, IgG3, IgG4 constant region. [8.] The monoclonal antibody of any one of [5] to [7], wherein the heavy chain constant region comprises a native amino acid sequence. [9.] The monoclonal antibody of any one of [5] to [7], wherein the heavy chain constant region comprises a non-native variant amino acid sequence. [10.] The monoclonal antibody of any one of [1] to [9], wherein the antibody is a recombinant antibody, a chimeric antibody, a human antibody, an antibody fragment, a bispecific antibody, or a trispecific antibody. [11.] The monoclonal antibody of [10], wherein the antibody is an antigen binding fragment comprising a single-chain Fv (scFv), Fab fragment, F(ab’)2 fragment, or an isolated VH domain. [12.] The monoclonal antibody of [10], wherein the antibody is a bispecific antibody. [13.] The monoclonal antibody of [10], wherein the antibody is a trispecific antibody. [14.] The monoclonal antibody of [13], which is a trispecific antibody comprising (i) a first scFv linked to a first Fc domain, (ii) an antibody heavy chain comprising a second Fc domain, and (iii) second scFv domain linked to an antibody light chain], wherein the first scFv linked to a first Fc domain, the antibody heavy chain comprising the second Fc domain, and the second scFv domain linked to the antibody light chain comprise an amino acid sequence having at least 80%, at least 85%, at least 90%, at least 95%, at least 97% or 100% identity to SEQ ID NOs: 75, 76, and 79, respectively, SEQ ID NOs: 75, 76, and 81, respectively, or SEQ ID NOs: 75, 76, and 83, respectively. [15.] A pharmaceutical composition comprising the antibody or antigen-binding fragment thereof of any one of [1] to [14] and a pharmaceutically acceptable excipient. [16.] An isolated polynucleotide encoding the antibody or antigen-binding fragment thereof of any one of [1] to [14]. [17.] The isolated polynucleotide of [16], which is a DNA. [18.] The isolated polynucleotide of [16], which is an mRNA. [19.] The isolated polynucleotide of [18], wherein the mRNA comprises a modified nucleotide. [20.] An isolated vector comprising the polynucleotide of [16]. [21.] The isolated vector of [20], wherein the vector is a viral vector. [22.] A recombinant virus comprising the polynucleotide of [16]. [23.] The recombinant virus of [22], which is a recombinant adeno-associated virus (AAV). [24.] A host cell comprising the polynucleotide of [16] or the vector of [20]. [25.] A method of producing the antibody or antigen-binding fragment thereof of any one of [1] to [14] comprising culturing the host cell of [24] so that the antibody or antigen- binding fragment thereof is expressed and the antibody or antigen-binding fragment thereof is produced. [26.] A method of neutralizing an HIV virus comprising contacting the virus with a sufficient amount of the antibody or antigen-binding fragment thereof of any one of [1] to [14]. [27.] A method of reducing the likelihood of HIV infection in a subject exposed to HIV comprising administering to the subject a therapeutically sufficient amount of the antibody or antigen-binding fragment thereof of any one of [1] to [14]. [28.] A method of treating HIV/AIDS comprising administering to a subject in need thereof a therapeutically sufficient amount of the antibody or antigen-binding fragment thereof of any one of [1] to [14]. [29.] A method of reducing viral load comprising administering to a subject in need thereof a therapeutically sufficient amount of the antibody or antigen-binding fragment thereof of any one of [1] to [14]. [30.] The method of any one of [27] to [29], further comprising administering at least one additional therapeutic agent. [31.] A method for detecting HIV in a sample comprising contacting the sample with the antibody of any one of [1] to [14]. [32.] A method of producing an engineered variant of an antibody of any one of [1] to [11] comprising (a) substituting one or more amino acid residues of the VH; and/or substituting one or more amino acid residues of the VL to create an engineered variant antibody, and (b) producing the engineered variant antibody. [33.] The method of [32] wherein the antibody is eN49P7-FRv1-23, eN49P7-FRv1-65 or eN49P7-FRv1-85. BRIEF DESCRIPTION OF THE DRAWINGS [0019] Figure 1. Neutralization breadth and potency on HIV-1 pseudovirus cross-clade Seaman global panel. [0020] Figure 2. Neutralization breadth and potency on pseudoviruses derived from AMP trial placebo group clade B HIV. [0021] Figure 3. Neutralization breadth and potency on pseudoviruses derived from AMP trial placebo group clade B HIV . [0022] Figure 4. Examples of trispecific antibody compositions. [0023] Figure 5. Neutralization potency of trispecific bnAbs against cross-clade Seaman global HIV-1 panel. [0024] Figure 6. Neutralization potency of trispecific bnAbs against HIV-1 panel from VRC01 AMP trials. [0025] Figure 7. Neutralization results for a select group of eight HIV-1 pseudoviruses. [0026] Figure 8. Neutralization potency of TriS-27 against HIV-1 panel from VRC01 AMP trials. [0027] Figure 9. Neutralization breadth and potency of TriS-27. DETAILED DESCRIPTION [0028] Provided herein are broadly neutralizing anti-HIV Env engineered antibodies derived from N49P7-FR, a variant of N49P7 that contains the extended heavy-chain framework region 3 loop of VRC03. The engineered antibodies are able to neutralize pseudoviruses comprising the Env of the Du422.1, BJOX2000, 6540.v4.c1 or 6545.v4.c1 isolates The engineered antibodies possess several-fold improved neutralization breadth and potency compared to VRC01 and the parental bnAb against a large panel of HIV-1 pseudoviruses representing globally circulating strains. In some embodiments, the engineered antibodies comprise an Fc region with the LS mutation and have a high serum half-life. Based on the results of the VRC01 Antibody Mediated Prevention (AMP) trials, the engineered antibodies provided herein should provide protection from the acquisition of in vitro neutralized viruses (IC₈₀ ≤0.1 µg/mL), including 95% of the tested VRC01 AMP trial viruses, with prevention efficacy exceeding 90% [Corey et al., 2021]. This makes the engineered antibodies disclosed herein suitable for use in therapeutic applications. The engineered antibodies disclosed herein can be used in combination with other potent bnAbs to confer extremely broad and potent protection or to lower the risk of the emergence of viral escape mutant strains during therapy. [0029] [0030] One aspect of the present disclosure relates to anti-HIV antibodies, and to nucleotide sequences encoding, compositions comprising, and kits comprising thereof. In another aspect, it relates to methods of treatment and prevention of HIV using an antibody disclosed herein. In another aspect, it relates to methods of diagnosing and monitoring of HIV infection using an antibody disclosed herein. In another aspect, it relates to methods of identifying an agent as an HIV vaccine candidate. I. Definitions [0031] To facilitate an understanding of the present invention, a number of terms and phrases are defined below. [0032] The terms "human immunodeficiency virus" or "HIV," as used herein, refer generally to a retrovirus that is the causative agent for acquired immunodeficiency syndrome (AIDS), variants thereof (e.g., simian acquired immunodeficiency syndrome, SAIDS), and diseases, conditions, or opportunistic infections associated with AIDS or its variants, and includes HIV-Type 1 (HIV-1) and HIV-Type 2 (HIV-2) of any clade or strain therein, related retroviruses (e.g., simian immunodeficiency virus (SIV)), and variants thereof (e.g., engineered retroviruses, e.g., chimeric HIV viruses, e.g., simian-human immunodeficiency viruses (SHIVs)). In some embodiments, an HIV virus is an HIV-Type- 1 virus. Previous names for HIV include human T-lymphotropic virus-III (HTLV-III), lymphadenopathy-associated virus (LAV), and AIDS-associated retrovirus (ARV). [0033] As used herein, the term "clade" refers to related human immunodeficiency viruses (HIVs) classified according to their degree of genetic similarity. There are currently four known groups of HIV-1 isolates: M, N, O, and P. Group M (major strains) viruses are responsible for the majority of the global HIV epidemic. The other three groups, i.e., N, O and P are quite uncommon and only occur in Cameroon, Gabon and Equatorial Guinea. In some embodiments, an HIV virus is a Group M HIV virus. Within group M, there are known to be at least nine genetically distinct subtypes or clades of HIV-1: subtypes or clades A, B, C, D, F, G, H, J and K. Additionally, different subtypes can combine genetic material to form a hybrid virus, known as a 'circulating recombinant form' (CRFs). Subtype/clade B is the dominant HIV subtype in the Americas, Western Europe and Australasia. Subtype/clade C is very common in the high AIDS prevalence countries of Southern Africa, as well as in the horn of Africa and India. Just under half of all people living with HIV have subtype C. In certain exemplary embodiments, methods described herein can be used to treat a subject (e.g., a human) infected with HIV (e.g., HIV-1) or to block or prevent HIV (e.g., HIV-1) infection in subject (e.g., a human) at risk of HIV transmission. The HIV may be of two, three, four, five, six, seven, eight, nine, ten, or more clades and/or two or more groups of HIV. [0034] Acquired immune deficiency syndrome ("AIDS") is a disease caused by the human immunodeficiency virus, or HIV. [0035] As used herein, the term "envelope glycoprotein" or "Env" refers to the glycoprotein that is expressed on the surface of the envelope of HIV virions and the surface of the plasma membrane of HIV infected cells. "Envelope glycoprotein" or "Env" encompass, but are not limited to, native Env, an isoform of Env, or a variant of Env (e.g., well-ordered trimer variant) derived from an HIV isolate, for example, 15-101765-029 (#2) and 15-15-101591-165. In some embodiments, Env is a MD-39 variant Env (Steichen et al, 2016), repaired and stabilized (RnS) variant Env (Rutten et al, 2018), DS variant Env (Kwon et al, 2015), NFL-TD variant Env (Guenaga et al, 2016), or DS-BG505-chimera variant Env (Joyce et al, 2018). Env is the sole virally encoded gene product on the surface of the virus and, as such, is the only target of neutralizing antibodies. Env is a trimer of heterodimers composed of two non-covalently associated subunits: the receptor-binding gp120 and the gp41 containing the fusion machinery. Each subunit is derived from a gp160 precursor glycoprotein following cleavage by cellular furins. HIV-1 gp120 binds the CD4 molecule on the surface of human target T cells to initiate the viral entry process, and following co-receptor engagement, fusion is mediated by gp41. The gp41 domain comprises the fusion peptide, fusion peptide proximal region, heptad repeats 1 and 2 (HR1, HR2), the membrane proximal external region (MPER), the transmembrane domain (TM) and the cytoplasmic tail (CT). gp140 env is the uncleaved ectodomain of gp160. In some embodiments, gp140 comprises MPER. In some embodiments, Env is BG505 Env (SEQ ID NO: 85). In some embodiments, Env is a Du422.1 (SEQ ID NO: 86), BJOX2000 (SEQ ID NO: 87), 6540.v4.c1 (SEQ ID NO: 88) or 6545.v4.c1 (SEQ ID NO: 89) Env polypeptide. [0036] The term "well-ordered Env trimer" or "well-ordered trimer" as used herein refers to an envelope glycoprotein trimer comprising three cleaved gp140 polypeptides that closely mimic the quaternary structure of the Env ectodomain on the surface of the envelope of HIV or SIV virions and the surface of the plasma membrane of HIV or SIV infected cells. In some embodiments, the gp120 and gp41 ectodomain is linked by a covalent linkage, for example, a disulfide bond. In some embodiments, the gp140 polypeptide comprises one or more mutations to promote trimer formation. In some embodiments, the gp140 polypeptide comprises one or more Cys substitutions to promote disulfide formation. In some embodiments, the well-ordered trimer is a SOSIP gp140 trimer. Well-ordered SOSIP trimers have been disclosed in US Patent Appl. Pub. No. 2014/0212458, and Sanders, R. W. et al., PLoS Pathog.9, e1003618 (2013), each of which is incorporated by reference herein in its entirety. In some embodiments, the well-ordered trimer is a MD-39 trimer (Steichen et al, 2016), repaired and stabilized (RnS) trimer (Rutten et al, 2018), DS trimer (Kwon et al, 2015), NFL-TD trimer (Guenaga et al, 2016), or DS-BG505-chimera trimer (Joyce et al, 2018). In some embodiments, a well-ordered trimer is formed from a clade A Env. In some embodiments, a well-ordered trimer is formed from a clade B Env. In some embodiments, a well-ordered trimer is formed from a clade C Env. In some embodiments, a well-ordered trimer is formed from a circulating recombinant form Env, wherein 'circulating recombinant form' (CRF) refers to a hybrid virus comprising a combination of genetic material from different subtypes. In some embodiments, a well-ordered trimer is a SOSIP of Du422.1, BJOX2000, 6540.v4.c1 or 6545.v4.c1. In some embodiments, a well-ordered trimer is BG505-SOSIP.664 (SEQ ID NO: 85). In some embodiments, a well-ordered trimer is a DS-BGN chimera of Du422.1 (SEQ ID NO: 86), BJOX2000 (SEQ ID NO: 87), 6540.v4.c1 (SEQ ID NO: 88) or 6545.v4.c1 (SEQ ID NO: 89). In some embodiments, a well-ordered Env trimer is a native flexibly linked (NFL) trimer as described in Sharna, et al., Cell Reports, 11(4):539-50 (2015). In some embodiments, a well-ordered Env trimer is a DS-SOSIP as described in Chuang GY, et al., J. Virology, 91(10). pii: e02268-16 (2017). In some embodiments, a well-ordered trimer is formed from an SIV Env. In some embodiments, a well-ordered trimer is an SIV Env SOSIP. In some embodiments, the gp120 and gp41 ectodomain is linked by a peptide linker, for example, a Gly-Ser linker, as described in Georgiev IS, et al., J. Virology 89(10): 5318-5329 (2015). In some embodiments, the well-ordered Env trimer is stable. [0037] The term "antibody" means an immunoglobulin molecule (or a group of immunoglobulin molecules) that recognizes and specifically binds to a target, such as a protein, polypeptide, peptide, carbohydrate, polynucleotide, lipid, or combinations of the foregoing through at least one antigen recognition site within the variable region of the immunoglobulin molecule. As used herein, the terms "antibody" and "antibodies" are terms of art and can be used interchangeably herein and refer to a molecule with an antigen- binding site that specifically binds an antigen. [0038] Antibodies can include, for example, monoclonal antibodies, recombinantly produced antibodies, human antibodies, humanized antibodies, resurfaced antibodies, chimeric antibodies, immunoglobulins, synthetic antibodies, tetrameric antibodies comprising two heavy chain and two light chain molecules, an antibody light chain monomer, an antibody heavy chain monomer, an antibody light chain dimer, an antibody heavy chain dimer, an antibody light chain- antibody heavy chain pair, intrabodies, heteroconjugate antibodies, single domain antibodies, monovalent antibodies, single chain antibodies or single-chain Fvs (scFv), affybodies, Fab fragments, F(ab')2 fragments, disulfide-linked Fvs (sdFv), anti-idiotypic (anti-Id) antibodies (including, e.g., anti-anti-Id antibodies), bispecific antibodies, and multi-specific antibodies. In certain embodiments, antibodies described herein refer to polyclonal antibody populations. Antibodies can be of any type (e.g., IgG, IgE, IgM, IgD, IgA, or IgY), any class (e.g., IgG1, IgG2, IgG3, IgG4, IgA₁, or IgA₂), or any subclasses (isotypes) thereof (e.g. IgG1, IgG2, IgG3, IgG4, IgA1 and IgA2), of immunoglobulin molecule, based on the identity of their heavy-chain constant domains referred to as alpha, delta, epsilon, gamma, and mu, respectively. The different classes of immunoglobulins have different and well-known subunit structures and three-dimensional configurations. Antibodies can be naked or conjugated or fused to other molecules such as toxins, radioisotopes, other polypeptides etc. [0039] As used herein, the terms "antigen-binding domain," "antigen-binding region," "antigen-binding site," and similar terms refer to the portion of antibody molecules, which comprises the amino acid residues that confer on the antibody molecule its specificity for the antigen (e.g., HIV Env). The antigen-binding region can be derived from any animal species, such as mouse and humans. [0040] As used herein, the terms "variable region" or "variable domain" are used interchangeably and are common in the art. The variability in sequence is concentrated in those regions called complementarity determining regions (CDRs) while the more highly conserved regions in the variable domain are called framework regions (FR). Without wishing to be bound by any particular mechanism or theory, it is believed that the CDRs of the light and heavy chains are primarily responsible for the interaction and specificity of the antibody with antigen (e.g., HIV Env). In certain embodiments, the variable region comprises 3 CDRs (CDR1, CDR2, and CDR3) and 4 framework regions (FR1, FR2, FR3, and FR4) in the order of FR1-CDR1-FR2-CDR2-FR3-CDR3-FR4 from the N terminus to the C terminus. In certain embodiments, the variable region is a human variable region. In certain embodiments, the variable region comprises human CDRs and human framework regions (FRs). In certain embodiments, the variable region comprises CDRs and framework regions (FRs) wherein one or more of the CDRs were modified by a substitution, deletion, or insertion relative to the CDRs of a parental antibody. In certain embodiments, the variable region comprises CDRs and framework regions (FRs) wherein one or more of the FRs were modified by a substitution, deletion, or insertion relative to the FRs of a parental antibody. In certain embodiments, the variable region comprises CDRs and framework regions (FRs) wherein one or more of the CDRs and one or more of the FRs were modified by a substitution, deletion, or insertion relative to the CDRs and FRs of a parental antibody. In certain embodiments, the parental antibody is N49P7-FR. In certain embodiments, the variable region comprises human CDRs and primate (e.g., non- human primate) framework regions (FRs). [0041] A skilled artisan understands that there are several methods for determining CDRs. One approach is based on cross-species sequence variability (i.e., Kabat EA, et al., Sequences of Proteins of Immunological Interest, (5th ed., 1991, National Institutes of Health, Bethesda Md.) ("Kabat"). Another approach is based on crystallographic studies of antigen-antibody complexes (Al-lazikani B., et al, J. Mol. Biol. 273:927-948 (1997)) ("Chothia"). In addition, combinations of these two approaches are sometimes used in the art to determine CDRs. In some embodiments, the CDR sequences are identified according to Kabat. In some embodiments, the CDR sequences are identified according to Chothia. It is understood that the identification of CDRs in a variable region also identifies the FRs as the sequences flanking the CDRs. [0042] The Kabat numbering system is generally used when referring to a residue in the variable domain (approximately residues 1-107 of the light chain and residues 1-113 of the heavy chain) (e.g., Kabat EA, et al., Sequences of Immunological Interest. (5th Ed., 1991, National Institutes of Health, Bethesda, Md.) ("Kabat"). [0043] The amino acid position numbering as in Kabat, refers to the numbering system used for heavy chain variable domains or light chain variable domains of the compilation of antibodies in Kabat EA, et al. (Sequences of Immunological Interest. (5th Ed., 1991, National Institutes of Health, Bethesda, Md.), "Kabat"). Using this numbering system, the actual linear amino acid sequence can contain fewer or additional amino acids corresponding to a shortening of, or insertion into, a FR or CDR of the variable domain. For example, a heavy chain variable domain can include a single amino acid insert (residue 52a according to Kabat) after residue 52 of H2 and inserted residues (e.g. residues 82a, 82b, and 82c, etc. according to Kabat) after heavy chain FR residue 82. The Kabat numbering of residues can be determined for a given antibody by alignment at regions of homology of the sequence of the antibody with a "standard" Kabat numbered sequence. Chothia refers instead to the location of the structural loops (Chothia and Lesk, J. Mol. Biol. 196:901-917 (1987)). The end of the Chothia CDR-H1 loop when numbered using the Kabat numbering convention varies between H32 and H34 depending on the length of the loop (this is because the Kabat numbering scheme places the insertions at H35A and H35B; if neither 35A nor 35B is present, the loop ends at 32; if only 35A is present, the loop ends at 33; if both 35A and 35B are present, the loop ends at 34). The AbM hypervariable regions represent a compromise between the Kabat CDRs and Chothia structural loops, and are used by Oxford Molecular's AbM antibody modeling software, available, for example, at bioinf.org.uk/abs/software. In some embodiments, the CDR sequences are identified according to Kabat. In some embodiments, the CDR sequences are identified according to Chothia. In some embodiments, the CDR sequences are identified according to AbM. In some embodiments, the VH CDR3 sequence is identified according to Kabat. In some embodiments, the VH CDR3 sequence is identified according to Chothia. In some embodiments, the VH CDR3 sequence is identified according to AbM. Loop Kabat AbM Chotia L1 L24-L34 L24-L34 L24-L34 L2 L50-L56 L50-L56 L50-L56 L3 L89-L97 L89-L97 L89-L97 H1 H31-H35B H26-H35B H26-H32..34 (Kabat numbering) H1 H31-H35 H26-H35 H26-H32 (Chothia numbering) H2 H50-H65 H50-H58 H52-H56 H3 H95-H102 H95-H102 H95-H102 [0044] The terms "VL" and "VL domain" are used interchangeably to refer to the light chain variable region of an antibody. [0045] The terms "VH" and "VH domain" are used interchangeably to refer to the heavy chain variable region of an antibody. [0046] The term "antibody fragment" refers to a portion of an intact antibody. An "antigen- binding fragment" refers to a portion of an intact antibody that binds to an antigen. An antigen-binding fragment can contain the antigenic determining variable regions of an intact antibody. Examples of antibody fragments include, but are not limited to Fab, Fab', F(ab')₂, and Fv fragments, linear antibodies, and single chain antibodies. [0047] A "monoclonal" antibody or antigen-binding fragment thereof refers to a homogeneous antibody or antigen-binding fragment population involved in the highly specific recognition and binding of a single antigenic determinant, or epitope. This is in contrast to polyclonal antibodies that typically include different antibodies directed against different antigenic determinants. The term "monoclonal" antibody or antigen-binding fragment thereof encompasses both intact and full-length monoclonal antibodies as well as antibody fragments (such as Fab, Fab', F(ab')₂, Fv), single chain (scFv) mutants, fusion proteins comprising an antibody portion, and any other modified immunoglobulin molecule comprising an antigen recognition site. Furthermore, "monoclonal" antibody or antigen-binding fragment thereof refers to such antibodies and antigen-binding fragments thereof made in any number of manners including but not limited to by hybridoma, phage selection, recombinant expression, and transgenic animals. [0048] The term "polyclonal antibody" describes a composition of different (diverse) antibody molecules, which are capable of binding to or reacting with several different specific antigenic determinants on the same or on different antigens. Usually, the variability of a polyclonal antibody is primarily located in the so-called variable regions of the polyclonal antibody, in particular in the CDR regions. In the present disclosure, a mixture of two or more polyclonal antibodies (a polycomposition) is produced in one mixture from a polyclonal polycomposition cell line, which is produced from two or more parental polyclonal cell lines each expressing antibody molecules, which are capable of binding to a distinct target, but it may also be a mixture of two or more polyclonal antibodies produced separately. A mixture of monoclonal antibodies providing the same antigen/epitope coverage as a polyclonal antibody described herein will be considered as an equivalent of a polyclonal antibody. [0049] The term "chimeric" antibodies or antigen-binding fragments thereof refers to antibodies or antigen-binding fragments thereof wherein the amino acid sequence is derived from two or more species. Typically, the variable region of both light and heavy chains corresponds to the variable region of antibodies or antigen-binding fragments thereof derived from one species of mammals (e.g., mouse) with the desired specificity, affinity, and capability, while the constant regions are homologous to the sequences in antibodies or antigen-binding fragments thereof derived from another (usually human) to avoid eliciting an immune response in that species. [0050] The term "epitope" or "antigenic determinant" are used interchangeably herein and refer to that portion of an antigen capable of being recognized and specifically bound by a particular antibody. When the antigen is a polypeptide, epitopes can be formed both from contiguous amino acids and noncontiguous amino acids juxtaposed by tertiary folding of a protein. Epitopes formed from contiguous amino acids are typically retained upon protein denaturing, whereas epitopes formed by tertiary folding are typically lost upon protein denaturing. An epitope typically includes at least 3, and more usually, at least 5 or 8-10 amino acids in a unique spatial conformation. [0051] "Binding affinity" generally refers to the strength of the sum total of non-covalent interactions between a single binding site of a molecule (e.g., an antibody) and its binding partner (e.g., an antigen). Unless indicated otherwise, as used herein, "binding affinity" refers to intrinsic binding affinity, which reflects a 1:1 interaction between members of a binding pair (e.g., antibody and antigen). The affinity of a molecule X for its partner Y can generally be represented by the dissociation constant (KD). Affinity can be measured by common methods known in the art, including those described herein. Low-affinity antibodies generally bind antigen slowly and tend to dissociate readily, whereas high- affinity antibodies generally bind antigen faster and tend to remain bound longer. A variety of methods of measuring binding affinity are known in the art, any of which can be used for purposes of the present invention. Specific illustrative embodiments are described in the following. In certain embodiments, an anti-HIV antibody disclosed herein binds to HIV Env with a KD of at least about 0.1 µM or less, at least about 0.01 µM or less, at least about 1 nM or less, or at least about 0.1 nM or less. In certain embodiments, an anti-HIV antibody disclosed herein binds to HIV Env with a K_D of at least about 0.01 µM or less. In some embodiments, the HIV Env is Du422.1, BJOX2000, 6540.v4.c1 or 6545.v4.c1 Env. In some embodiments, an anti-HIV antibody disclosed herein is capable of binding to cells that express functional, well-ordered HIV-1 membrane Env trimers. In some embodiments, an anti-HIV antibody disclosed herein is capable of binding to HIV Env in biolayer interferometry (BLI) assay. In some embodiments, an anti-HIV antibody disclosed herein is capable of binding to HIV Env peptide in ELISA. In some embodiments, an anti-HIV antibody disclosed herein is capable of binding Env trimers from detergent-solubilized HIV-1 virions in an ELISA assay. In some embodiments, an anti-HIV antibody disclosed herein is capable of binding Env trimers from detergent-solubilized HIV-1 virions in a BN- PAGE gel mobility-shift assay. [0052] "Or better" when used herein to refer to binding affinity refers to a stronger binding between a molecule and its binding partner. "Or better" when used herein refers to a stronger binding, represented by a smaller numerical KD value. For example, an antibody, which has an affinity for an antigen of "0.6 nM or better", the antibody's affinity for the antigen is <0.6 nM, i.e. 0.59 nM, 0.58 nM, 0.57 nM etc. or any value less than 0.6 nM. [0053] As used herein, the terms "immunospecifically binds," "immunospecifically recognizes," "specifically binds," and "specifically recognizes" are analogous terms in the context of antibodies and refer to molecules that bind to an antigen (e.g., epitope or immune complex) as such binding is understood by one skilled in the art. For example, a molecule that specifically binds to an antigen can bind to other peptides or polypeptides, generally with lower affinity as determined by, e.g., immunoassays, BIAcore^®, KinExA 3000 instrument (Sapidyne Instruments, Boise, ID), ELISA, biolayer interferometry (BLI), flow cytometry or other assays known in the art. In a specific embodiment, molecules that immunospecifically bind to an antigen bind to the antigen with a K_D that is at least 2 logs, 2.5 logs, 3 logs, or 4 logs lower than the K_D when the molecules bind non-specifically to another antigen. In one example, the antibody may specifically bind to cells that express functional, well-ordered HIV-1 membrane Env trimers. In one example, the antibody may specifically bind to the HIV Env. In one example, the antibody may specifically bind to the HIV Env in biolayer interferometry (BLI) assay. In one example, the antibody may specifically bind to the HIV Env in ELISA assay. In one example, the antibody may specifically bind to Env trimers from detergent-solubilized HIV-1 virions. In one example, the antibody may specifically bind to Env trimers from detergent-solubilized HIV-1 virions in an ELISA assay. In one example, the antibody may specifically bind to Env trimers from detergent-solubilized HIV-1 virions in a BN-PAGE gel mobility-shift assay. The antibody may bind to HIV Env with a K_D at least 2 logs, 2.5 logs, 3 logs, or 4 logs lower than K_D of binding to other viral or non-viral polypeptides. An antibody that specifically binds to Env encompass, but are not limited to, antibodies that specifically bind to native Env, an isoform of Env, or a variant of Env (e.g., DS BGN chimera) derived from an HIV isolate, for example, Du422.1, BJOX2000, 6540.v4.c1 or 6545.v4.c1. In some embodiments, the antibody specifically binds to Du422.1, BJOX2000, 6540.v4.c1 or 6545.v4.c1 Env. [0054] By "preferentially binds," it is meant that the antibody specifically binds to an epitope more readily than it would bind to a related, similar, homologous, or analogous epitope. Thus, an antibody, which "preferentially binds" to a given epitope would more likely bind to that epitope than to a related epitope, even though such an antibody may cross-react with the related epitope. [0055] An antibody is said to "competitively inhibit" binding of a reference antibody to a given epitope if it preferentially binds to that epitope or an overlapping epitope to the extent that it blocks, to some degree, binding of the reference antibody to the epitope. Competitive inhibition may be determined by any method known in the art, for example, competition ELISA assays. An antibody may be said to competitively inhibit binding of the reference antibody to a given epitope by at least 90%, at least 80%, at least 70%, at least 60%, or at least 50%. [0056] The term "broadly neutralizing antibody" or "bnAb," as used herein, with respect to HIV (e.g., HIV-1), refers to an antibody that recognizes HIV Env of more than one isolate or strain of HIV and inhibits or prevents receptor binding of target cells as evaluated in an in vitro neutralization assay. In some embodiments, a broadly neutralizing antibody inhibits infection of a susceptible target cell by HIV. In some embodiments, a neutralizing (e.g., broadly neutralizing) antibody specifically binds an HIV Env and inhibits infection of a susceptible target cell (e.g., TZM-bl) by an HIV pseudovirus comprising an Env polypeptide. HIV pseudovirus neutralization assays have been disclosed in the art, for example, in Walker L.M., et al., Nature 477, 466–470 (2011), Li M., et al., J. Virol. 79:10108-10125 (2005), each of which is incorporated herein by reference in its entirety for all purposes. In some embodiments, a broadly neutralizing antibody neutralizes 2, 3, 4, 5, 6, 7, 8, 9, or more HIV strains or pseudoviruses. In some embodiments, a broadly neutralizing antibody neutralizes 2, 3, 4, 5, 6, 7, 8, 9, or more HIV strains or pseudoviruses that belong to the same or different clades. In some embodiments, a broadly neutralizing antibody is capable of neutralizing HIV strains or pseudoviruses from at least two different clades. In some embodiments, a broadly neutralizing antibody is capable of neutralizing at least one clade B strain or pseudovirus and one clade C strain or pseudovirus. In some embodiments, a broadly neutralizing antibody is capable of neutralizing more than one clade B strain or pseudovirus and more than one clade C strain or pseudovirus. In some embodiments, a broadly neutralizing antibody is capable of neutralizing an HIV strain or pseudovirus from at least one, at least two, at least three, at least four, at least five, at least six, at least seven, at least eight, at least nine, or at least ten clades. In some embodiments, a broadly neutralizing antibody is capable of neutralizing an HIV strain or pseudovirus from at least one, at least two, at least three, at least four, at least five, at least six, at least seven, at least eight, at least nine, at least ten, at least eleven, at least twelve, at least thirteen, at least fourteen, or all fifteen clades selected from the group consisting of clades A, A (T/F), AC, ACD, B, B (T/F), BC, C, C (T/F), CD, CRF01_AE, CRF01_AE (T/F), CRF02_AG, D, and G. In some embodiments, a broadly neutralizing antibody is capable of neutralizing an HIV strain or pseudovirus from at least one, at least two, at least three, at least four, at least five, at least six, at least seven, at least eight, at least nine, at least ten, or all eleven clades selected from the group consisting of clades A, AC, ACD, AE, AG, B, BC, C, CD, D, G. [0057] In some embodiments, the breadth of neutralization is tested on an indicator virus panel comprising cross-clade HIV isolates. In some embodiments, the virus panel comprises the 56 cross-clade isolates listed in Table 10. In some embodiments, a broadly neutralizing antibody is capable of neutralizing at least 2, 3, 4, 5, 6, 7, 8, 9 or 10 of the cross-clade HIV isolates in the 56 cross-clade indicator virus panel. In some embodiments, a broadly neutralizing antibody is capable of neutralizing at least about 30%, 40%, 50%, 60%, 70%, 80%, 90%, 95%, or 100% of cross-clade HIV isolates in the 56 cross-clade indicator virus panel. In some embodiments, a broadly neutralizing antibody is capable of neutralizing at least about 40% of cross-clade HIV isolates in the 56 cross-clade indicator virus panel. In some embodiments, a broadly neutralizing antibody is capable of neutralizing at least about 50% of cross-clade HIV isolates in the 56 cross-clade indicator virus panel. In some embodiments, a broadly neutralizing antibody is capable of neutralizing at least about 60% of cross-clade HIV isolates in the 56 cross-clade indicator virus panel. In some embodiments, a broadly neutralizing antibody is capable of neutralizing at least about 70% of cross-clade HIV isolates in the 56 cross-clade indicator virus panel. In some embodiments, a broadly neutralizing antibody is capable of neutralizing at least about 80% of cross-clade HIV isolates in the 56 cross-clade indicator virus panel. In some embodiments, a broadly neutralizing antibody is capable of neutralizing at least about 90% of cross-clade HIV isolates in the 56 cross-clade indicator virus panel. [0058] In some embodiments, a broadly neutralizing antibody is capable of neutralizing at least about 30%, 40%, 50%, 60%, 70%, 80%, 90%, 95%, or 100% of cross-clade HIV isolates in the 56 cross-clade indicator virus panel with a median IC50 equal to or less than about 2 µg/ml, about 1.5 µg/ml, about 1 µg/ml, about 0.75 µg/ml, about 0.5 µg/ml, about 0.25 µg/ml, about 0.1 µg/ml, 0.07 µg/ml, 0.06 µg/ml, 0.05 µg/ml, 0.025 µg/ml, 0.01 µg/ml or 0.005 µg/ml. In some embodiments, a broadly neutralizing antibody is capable of neutralizing at least about 40% of cross-clade HIV isolates in the 56 cross-clade indicator virus panel with a median IC50 equal to or less than 0.75 µg/ml. In some embodiments, a broadly neutralizing antibody is capable of neutralizing at least about 40% of cross-clade HIV isolates in the 56 cross-clade indicator virus panel with a median IC₅₀ equal to or less than 0.5 µg/ml. In some embodiments, a broadly neutralizing antibody is capable of neutralizing at least about 40% of cross-clade HIV isolates in the 56 cross-clade indicator virus panel with a median IC50 equal to or less than 0.25 µg/ml. [0059] The term "IC₅₀" refers to the half maximal inhibitory concentration of an inhibitor, e.g., a broadly neutralizing antibody. For example, IC50 is the concentration of an inhibitor, e.g., a broadly neutralizing antibody, where the response, e.g., infection by pseudovirus, is reduced by half. [0060] A polypeptide, antibody, polynucleotide, vector, cell, or composition, which is "isolated" is a polypeptide, antibody, polynucleotide, vector, cell, or composition, which is in a form not found in nature. Isolated polypeptides, antibodies, polynucleotides, vectors, cell or compositions include those which have been purified to a degree that they are no longer in a form in which they are found in nature. In some embodiments, an antibody, polynucleotide, vector, cell, or composition, which is isolated is substantially pure. [0061] The terms "polypeptide," "peptide," and "protein" are used interchangeably herein to refer to polymers of amino acids of any length. The polymer can be linear or branched, it can comprise modified amino acids, and it can be interrupted by non-amino acids. The terms also encompass an amino acid polymer that has been modified naturally or by intervention; for example, disulfide bond formation, glycosylation, lipidation, acetylation, phosphorylation, or any other manipulation or modification, such as conjugation with a labeling component. Also included within the definition are, for example, polypeptides containing one or more analogs of an amino acid (including, for example, unnatural amino acids, etc.), as well as other modifications known in the art. It is understood that, because the polypeptides described herein are based upon antibodies, in certain embodiments, the polypeptides can occur as single chains or associated chains. [0062] The terms "identical" or percent "identity" in the context of two or more nucleic acids or polypeptides, refer to two or more sequences or subsequences that are the same or have a specified percentage of nucleotides or amino acid residues that are the same, when compared and aligned (introducing gaps, if necessary) for maximum correspondence, not considering any conservative amino acid substitutions as part of the sequence identity. The percent identity can be measured using sequence comparison software or algorithms or by visual inspection. Various algorithms and software are known in the art that can be used to obtain alignments of amino acid or nucleotide sequences. One such non-limiting example of a sequence alignment algorithm is the algorithm described in Karlin S., et al, Proc. Natl. Acad. Sci., 87:2264-2268 (1990), as modified in Karlin S., et al., Proc. Natl. Acad. Sci., 90:5873-5877 (1993), and incorporated into the NBLAST and XBLAST programs (Altschul SF, et al., Nucleic Acids Res., 25:3389-3402 (1991)). In certain embodiments, Gapped BLAST can be used as described in Altschul SF, et al., Nucleic Acids Res. 25:3389-3402 (1997). BLAST-2, WU-BLAST-2 (Altschul SF, et al., Methods in Enzymology, 266:460-480 (1996)), ALIGN, ALIGN-2 (Genentech, South San Francisco, California) or Megalign (DNASTAR) are additional publicly available software programs that can be used to align sequences. In certain embodiments, the percent identity between two nucleotide sequences is determined using the GAP program in GCG software (e.g., using a NWSgapdna.CMP matrix and a gap weight of 40, 50, 60, 70, or 90 and a length weight of 1, 2, 3, 4, 5, or 6). In certain alternative embodiments, the GAP program in the GCG software package, which incorporates the algorithm of Needleman and Wunsch (J. Mol. Biol. (48):444-453 (1970)) can be used to determine the percent identity between two amino acid sequences (e.g., using either a Blossum 62 matrix or a PAM250 matrix, and a gap weight of 16, 14, 12, 10, 8, 6, or 4 and a length weight of 1, 2, 3, 4, 5). Alternatively, in certain embodiments, the percent identity between nucleotide or amino acid sequences is determined using the algorithm of Myers and Miller (CABIOS, 4:11-17 (1989)). For example, the percent identity can be determined using the ALIGN program (version 2.0) and using a PAM120 with residue table, a gap length penalty of 12 and a gap penalty of 4. Appropriate parameters for maximal alignment by particular alignment software can be determined by one skilled in the art. In certain embodiments, the default parameters of the alignment software are used. In certain embodiments, the percentage identity "X" of a first amino acid sequence to a second sequence amino acid is calculated as 100 x (Y/Z), where Y is the number of amino acid residues scored as identical matches in the alignment of the first and second sequences (as aligned by visual inspection or a particular sequence alignment program) and Z is the total number of residues in the second sequence. If the length of a first sequence is longer than the second sequence, the percent identity of the first sequence to the second sequence will be higher than the percent identity of the second sequence to the first sequence. [0063] As a non-limiting example, whether any particular polynucleotide has a certain percentage sequence identity (e.g., is at least 80% identical, at least 85% identical, at least 90% identical, and in some embodiments, at least 95%, 96%, 97%, 98%, or 99% identical) to a reference sequence can, in certain embodiments, be determined using the Bestfit program (Wisconsin Sequence Analysis Package, Version 8 for Unix, Genetics Computer Group, University Research Park, 575 Science Drive, Madison, WI 53711). Bestfit uses the local homology algorithm of Smith and Waterman (Advances in Applied Mathematics 2: 482489 (1981)) to find the best segment of homology between two sequences. When using Bestfit or any other sequence alignment program to determine whether a particular sequence is, for instance, 95% identical to a reference sequence described herein, the parameters are set such that the percentage of identity is calculated over the full length of the reference nucleotide sequence and that gaps in identity of up to 5% of the total number of nucleotides in the reference sequence are allowed. [0064] In some embodiments, two nucleic acids or polypeptides described herein are substantially identical, meaning they have at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, and in some embodiments at least 95%, 96%, 97%, 98%, 99% nucleotide or amino acid residue identity, when compared and aligned for maximum correspondence, as measured using a sequence comparison algorithm or by visual inspection. Identity can exist over a region of the sequences that is at least about 10, about 20, about 40-60 residues in length or any integral value there between, and can be over a longer region than 60-80 residues, for example, at least about 90-100 residues, and in some embodiments, the sequences are substantially identical over the full length of the sequences being compared, such as the coding region of a nucleotide sequence for example. [0065] A "conservative amino acid substitution" is one in which one amino acid residue is replaced with another amino acid residue having a similar side chain. Families of amino acid residues having similar side chains have been defined in the art, including basic side chains (e.g., lysine, arginine, histidine), acidic side chains (e.g., aspartic acid, glutamic acid), uncharged polar side chains (e.g., asparagine, glutamine, serine, threonine, tyrosine, cysteine), nonpolar side chains (e.g., alanine, valine, leucine, isoleucine, proline, phenylalanine, methionine, tryptophan), beta-branched side chains (e.g., threonine, valine, isoleucine) and aromatic side chains (e.g., tyrosine, phenylalanine, tryptophan, histidine). For example, substitution of a phenylalanine for a tyrosine is a conservative substitution. In some embodiments, conservative substitutions in the sequences of the polypeptides and antibodies described herein do not abrogate the binding of the polypeptide or antibody containing the amino acid sequence, to the antigen(s). Methods of identifying nucleotide and amino acid conservative substitutions, which do not eliminate antigen binding are well- known in the art (see, e.g., Brummell DA, et al., Biochem. 32: 1180-1 187 (1993); Kobayashi et al., Protein Eng. 12(10):879-884 (1999); and Burks EA, et al., Proc. Natl. Acad. Sci. USA 94:.412-417 (1997)). [0066] As used herein, the terms "treatment" or "therapy" (as well as different forms thereof, including curative or palliative) refer to treatment of an infected person. As used herein, the term "treating" includes alleviating or reducing at least one adverse or negative effect or symptom of a condition, disease or disorder. This condition, disease or disorder can be HIV infection. [0067] Terms such as "treating" or "treatment" or "to treat" or "alleviating" or "to alleviate" refer to therapeutic measures that cure, slow down, lessen symptoms of, and/or halt progression of a diagnosed pathologic condition or disorder, such as HIV or AIDS. Thus, those in need of treatment include those already diagnosed with or suspected of having the disorder. In certain embodiments, a subject is successfully "treated" for the disorder according to the methods described herein if the patient shows one or more of the following: a reduction in the number of or complete absence of viral load; a reduction in the viral burden; inhibition of or an absence of the virus into peripheral organs; relief of one or more symptoms associated with the disorder; reduced morbidity and mortality; improvement in quality of life or any combination thereof. [0068] As used herein, the terms "prevention" or "prophylaxis" refer to preventing a subject from becoming infected with, or reducing the risk of a subject from becoming infected with, or halting transmission of, or the reducing the risk of transmission of a virus. Prophylactic or preventative measures refer to measures that prevent and/or slow the development of a targeted pathological condition or disorder. Thus, those in need of prophylactic or preventative measures include those prone to have the disorder and those in whom the disorder is to be prevented. In some embodiments, prevention encompasses passive immunization of a subject in need thereof comprising administering an effective amount of an antibody disclosed herein. [0069] As employed above and throughout the disclosure the term "effective amount" refers to an amount effective, at dosages, and for periods of time necessary, to achieve the desired result with respect to the treatment of the relevant disorder, condition, or side effect. An "effective amount" can be determined empirically and in a routine manner, in relation to the stated purpose. It will be appreciated that the effective amount of components of the present invention will vary from patient to patient not only with the particular vaccine, component or composition selected, the route of administration, and the ability of the components to elicit a desired result in the individual, but also with factors such as the disease state or severity of the condition to be alleviated, hormone levels, age, sex, weight of the individual, the state of being of the patient, and the severity of the pathological condition being treated, concurrent medication or special diets then being followed by the particular patient, and other factors, which those skilled in the art will recognize, with the appropriate dosage being at the discretion of the attending physician. Dosage regimes may be adjusted to provide the improved therapeutic response. An effective amount is also one in which any toxic or detrimental effects of the components are outweighed by the therapeutically beneficial effects. [0070] The term "therapeutically effective amount" refers to an amount of an antibody, recombinant virus, immunoconjugate, or other drug effective to "treat" a disease or disorder in a subject or mammal. To the extent an antibody can prevent growth and/or kill existing cells, it can be cytostatic and/or cytotoxic. A "prophylactically effective amount" refers to an amount effective, at dosages and for periods of time necessary, to achieve the desired prophylactic result. Typically but not necessarily, since a prophylactic dose is used in subjects prior to or at an earlier stage of disease, the prophylactically effective amount will be less than the therapeutically effective amount. [0071] The terms "subject," "individual," and "patient" are used interchangeably herein, and refer to an animal, for example a human, to whom treatment, including prophylactic treatment, with the antibody or pharmaceutical composition according to the present disclosure, is provided. In some embodiments, the subject, individual, or patient has been infected with HIV. In some embodiments, the subject, individual, or patient suffers from AIDS. In some embodiments, the subject, individual, or patient has been exposed to HIV. In some embodiments, the subject, individual, or patient is at risk of being exposed to HIV. [0072] Administration "in combination with" one or more further therapeutic agents includes simultaneous (concurrent) or consecutive administration in any order. [0073] The terms "pharmaceutically composition," "pharmaceutical formulation," "pharmaceutically acceptable formulation," or "pharmaceutically acceptable composition" all of which are used interchangeably, refer to those compounds, materials, compositions, and/or dosage forms which are, within the scope of sound medical judgment, suitable for contact with the tissues of human beings and animals without excessive toxicity, irritation, allergic response, or other problem complications commensurate with a reasonable benefit/risk ratio. "Pharmaceutically acceptable" or "pharmaceutical formulation" refers to a preparation, which is in such form as to permit the biological activity of the active ingredient to be effective, and which contains no additional components, which are unacceptably toxic to a subject to which the formulation would be administered. The formulation can be sterile. [0074] The term "antiretroviral therapy" or "ART," as used herein, refers to any of the therapies used to manage progression of a retrovirus (e.g., HIV) infection in a subject (e.g., a human), including, for example, nucleoside reverse transcriptase inhibitors (NRTIs), non- nucleoside reverse transcriptase inhibitors (NNRTIs), protease inhibitors (PIs), fusion inhibitors, entry inhibitors, maturation inhibitors, cellular inhibitors, integrase strand transfer inhibitors, and multi-class combinations. Such drugs include, but are not limited to, lamivudine and zidovudine, emtricitabine (FTC), zidovudine (ZDV), azidothymidine (AZT), lamivudine (3TC), zalcitabine, dideoxycytidine (ddC), tenofovir disoproxil fumarate (TDF), didanosine (ddl), stavudine (d4T), abacavir sulfate (ABC), etravirine (ETR), delavirdine (DLV), efavirenz (EFV), nevirapine (NVP), amprenavir (APV), tipranavir (TPV), indinavir (IDV), saquinavir, saquinavir mesylate (SQV), lopinavir (LPV), ritonavir (RTV), fosamprenavir calcium (FOS-APV), ritonavir (RTV), darunavir (DRV), atazanavir sulfate (ATV), nelfinavir mesylate (NFV), enfuvirtide (T-20), maraviroc and raltegravir. ART drugs can also include antibodies that target HIV proteins or cellular proteins associated with disease progression. Also included are immune-based therapies, such as IL-2, IL-12, and alpha-epibromide. Each of these drugs can be administered alone or in combination with any other ART drug or any HIV-specific neutralizing antibody, such as a broadly neutralizing antibody, which is incorporated by reference herein in its entirety for all purposes. [0075] The term "reservoir activator," as used herein, refers to an agent capable of activating a viral reservoir (e.g., an HIV reservoir). In some embodiments, a reservoir activator comprises a histone deacytelase (HDAC) inhibitor (e.g., romidepsin, vorinostat, and panobinostat), immunologic activator (e.g., cytokines and TLR agonists), or a dedicated small molecule drug. [0076] The term "immunomodulator," as used herein, refers to an agent, such as an antibody or peptide, which is capable of increasing, inducing, or extending an immune response (e.g., a cell-mediated immune response and/or a humoral immune response) when administered to a subject (e.g., a human, e.g., a human infected with HIV or at risk of an HIV infection or transmission). Immunomodulators include, but are not limited to immune checkpoint inhibitors, for example, a PD-1, PD-L1, LAG-3, or TIGIT antagonist. In some embodiments, an immunomodulator used in the methods described herein comprises an anti-PD-1 antibody, anti-PD-L1 antibody, anti-LAG3 antibody, or an anti-TIGIT antibody. An immunomodulator can be administered in conjunction with (e.g., prior to, concurrently with, or subsequent to, or within the context of a treatment regimen that includes the administration of a broadly neutralizing antibody described herein. [0077] As used in this specification and the appended claims, the singular forms "a," "an," and "the" include plural referents unless the content clearly dictates otherwise. Thus, for example, reference to "a cell" includes a combination of two or more cells, and the like. [0078] The term "and/or" as used in a phrase such as "A and/or B" herein is intended to include both "A and B," "A or B," "A," and "B." Likewise, the term "and/or" as used in a phrase such as "A, B, and/or C" is intended to encompass each of the following embodiments: A, B, and C; A, B, or C; A or C; A or B; B or C; A and C; A and B; B and C; A (alone); B (alone); and C (alone). [0079] The term "about" as used herein when referring to a measurable value such as an amount, a temporal duration, and the like, is meant to encompass variations of up to ±20% from the specified value, as such variations are appropriate to perform the disclosed methods. Unless otherwise indicated, all numbers expressing quantities of ingredients, properties such as molecular weight, reaction conditions, and so forth used in the specification and claims are to be understood as being modified in all instances by the term "about." Accordingly, unless indicated to the contrary, the numerical parameters set forth in the following specification and attached claims are approximations that may vary depending upon the desired properties sought to be obtained by the present invention. At the very least, and not as an attempt to limit the application of the doctrine of equivalents to the scope of the claims, each numerical parameter should at least be construed in light of the number of reported significant digits and by applying ordinary rounding techniques. [0080] Notwithstanding that the numerical ranges and parameters setting forth the broad scope described herein are approximations, the numerical values set forth in the specific examples are reported as precisely as possible. Any numerical value, however, inherently contain certain errors necessarily resulting from the standard deviation found in their respective testing measurements. [0081] It is understood that wherever embodiments are described herein with the language "comprising," otherwise analogous embodiments described in terms of "consisting of" and/or "consisting essentially of" are also provided. II. Anti-HIV antibodies [0082] In one aspect, provided herein are anti-HIV antibodies and antigen-binding fragments thereof that bind to HIV Env. In some embodiments, an antibody described herein is a monoclonal antibody. In some embodiments, an antibody described herein is an engineered antibody. In some embodiments, an antibody described herein is a broadly neutralizing antibody. In some embodiments, an antibody described herein specifically binds the Env of at least one HIV isolate in the 56 cross-clade indicator virus panel of Table 10. In some embodiments, an antibody described herein specifically binds the Env of at least two, at least three, at least four, or at least five HIV isolates in the 56 cross-clade indicator virus panel of Table 10. In some embodiments, an antibody described herein binds Env at the CD4 binding site (CD4bs) epitope region. In some embodiments, an antibody described herein binds to cells that express well-ordered HIV-1 membrane Env trimers. In some embodiments, an antibody described herein binds to Env trimers from detergent-solubilized HIV-1 virions. In some embodiments, the Env is a clade B Env. In some embodiments, the Env is Du422.1, BJOX2000, 6540.v4.c1 or 6545.v4.c1. [0083] In one aspect, provided herein is an antibody and an antigen-binding fragment thereof that is capable of neutralizing the Du422.1, BJOX2000, 6540.v4.c1 or 6545.v4.c1 HIV isolate. [0084] In one aspect, provided herein is antibody and an antigen-binding fragment thereof that is capable of neutralizing at least two cross-clade isolates of HIV. In some embodiments, the antibody is capable of neutralizing at least one clade B isolate and at least one clade AG isolate. In some embodiments, the antibody is capable of neutralizing at least one clade B isolate and at least one clade AC isolate. [0085] In some embodiments, an antibody or antigen-binding fragment thereof disclosed herein is a broadly neutralizing antibody. [0086] In some embodiments, an antibody or antigen-binding fragment thereof disclosed herein neutralizes 2, 3, 4, 5, 6, 7, 8, 9, or more HIV strains or pseudoviruses that belong to the same or different clades. In some embodiments, an antibody disclosed herein is capable of neutralizing HIV strains or pseudoviruses from at least two different clades. In some embodiments, an antibody disclosed herein is capable of neutralizing at least one clade B strain or pseudovirus and one clade AG strain or pseudovirus. In some embodiments, an antibody disclosed herein is capable of neutralizing at least one clade B strain or pseudovirus and one clade AC strain or pseudovirus. In some embodiments, an antibody disclosed herein is capable of neutralizing more than one clade B strain or pseudovirus. [0087] In some embodiments, an antibody or antigen-binding fragment thereof disclosed herein is a broadly neutralizing anti-HIV Env antibody. In some embodiments, an antibody or antigen-binding fragment thereof disclosed herein specifically binds to the CD4 binding site (CD4bs) epitope. In some embodiments, an antibody disclosed herein specifically binds to a well-ordered HIV Env trimer. In some embodiments, an antibody disclosed herein is a monoclonal antibody. In some embodiments, an antibody disclosed herein is an F(ab) or F(ab')2. In some embodiments, an antibody disclosed herein is a recombinant antibody, a chimeric antibody, an antibody fragment, a bispecific antibody, or a trispecific antibody. [0088] In some embodiments, an antibody or antigen-binding fragment thereof disclosed herein is a not polyreactive. Table 1. Variable heavy chain (VH) and light chain (VL) domains. eN49P7-FRv1- ADLVQSGAVTKKPGDSVRISCEAQGYRFTDYFIHWIRQAPGK 23 VH GPEWMGWINPYYGQVNIPWKFQGRISMTRQRSQDPYDPDWG W K Y Table 2. Example VH and VL CDR sequences. The CDRs have been determined according to Kabat. CDR1 CDR2 CDR3 N4 P7 YRFTDYF INPYY V E VRDR Y KLFE DN ) N ) N ) [0089] In some embodiments, an isolated monoclonal antibody described herein specifically binds to HIV Env and comprises a VH, a VL, or a VH and VL as shown in Table 1. [0090] In some embodiments, an isolated monoclonal antibody described herein specifically binds to HIV Env and comprises one, two, three, four, five or six of the VH CDR1, VH CDR2, VH CDR3, VL CDR1, VL CDR2, and VL CDR3 sequences of a VH or VL shown in Table 1. In some embodiments, the VH CDR1, VH CDR2, VH CDR3, VL CDR1, VL CDR2, and VL CDR3 is according to Kabat. [0091] In some embodiments, an isolated monoclonal antibody described herein specifically binds to HIV Env and comprises one, two, three, four, five or six of the VH CDR1, VH CDR2, VH CDR3, VL CDR1, VL CDR2, and VL CDR3 sequences shown in Table 2. [0092] In some embodiments, an isolated monoclonal antibody described herein specifically binds to HIV Env and comprises a VH CDR3 sequence of a VH shown in Table 1. In some embodiments, the VH CDR3 is according to Kabat. [0093] In some embodiments, an isolated monoclonal antibody described herein specifically binds to HIV Env and comprises a VH CDR3 sequence shown in Table 2. [0094] In some embodiments, an isolated monoclonal antibody described herein specifically binds to HIV Env and comprises a VH CDR1, VH CDR2, VH CDR3, VL CDR1, VL CDR2, and VL CDR3 sequence of a VH or VL shown in Table 1. In some embodiments, the VH CDR1, VH CDR2, VH CDR3, VL CDR1, VL CDR2, and VL CDR3 is according to Kabat. [0095] Also provided herein are polypeptides that comprise an amino acid sequence having at least about 80% sequence identity, at least about 85% sequence identity, at least about 90% sequence identity, at least about 95% sequence identity, at least about 96% sequence identity, at least about 97% sequence identity, at least about 98% sequence identity, or at least about 99% sequence, or is identical to the sequences shown in Tables 1 and 2. [0096] In some embodiments, an isolated monoclonal antibody described herein specifically binds to HIV Env and comprises a VH CDR1, VH CDR2, VH CDR3, VL CDR1, VL CDR2, and VL CDR3, wherein the VH CDR3 comprises an amino acid sequence that is at least about 90%, 95%, 97%, 98%, 99% or 100% identical to the VH CDR3 of eN49P7-FRv1-23, eN49P7-FRv1-65 or eN49P7-FRv1-85. In some embodiments, the antibody comprises the VH CDR1, VH CDR2, VL CDR1, VL CDR2, and VL CDR3 of eN49P7-FRv1-23, eN49P7-FRv1-65 or eN49P7-FRv1-85. [0097] In some embodiments, an isolated monoclonal antibody described herein specifically binds to HIV Env and comprises a VH CDR1, VH CDR2, VH CDR3, VL CDR1, VL CDR2, and VL CDR3, wherein the VH CDR3 comprises an amino acid sequence that is at least about 90%, 95%, 97%, 98%, 99% or 100% identical to a VH CDR3 shown in Table 2. In some embodiments, the antibody comprises a VH CDR1, VH CDR2, VL CDR1, VL CDR2, and VL CDR3 shown in Table 2. [0098] In some embodiments, an isolated monoclonal antibody described herein specifically binds to HIV Env and comprises a VH CDR1, VH CDR2, VH CDR3, VL CDR1, VL CDR2, and VL CDR3, wherein the VH CDR3 comprises the VH CDR3 of eN49P7-FRv1-23, eN49P7-FRv1-65 or eN49P7-FRv1-85 comprising 0, 1, 2, 3, 4, or 5 substitutions, insertions, or deletions. In some embodiments, the antibody comprises the VH CDR1, VH CDR2, VL CDR1, VL CDR2, and VL CDR3 of eN49P7-FRv1-23, eN49P7-FRv1-65 or eN49P7-FRv1-85. In some embodiments, the antibody comprises a VH CDR1, VH CDR2, VL CDR1, VL CDR2, and VL CDR3 shown in Table 2. [0099] In some embodiments, an isolated monoclonal antibody described herein specifically binds to HIV Env and comprises a VH CDR1, VH CDR2, VH CDR3, VL CDR1, VL CDR2, and VL CDR3, wherein the VH CDR3 comprises a VH CDR3 shown in Table 2 comprising 0, 1, 2, 3, 4, or 5 substitutions, insertions, or deletions. In some embodiments, the antibody comprises the VH CDR1, VH CDR2, VL CDR1, VL CDR2, and VL CDR3 of eN49P7-FRv1-23, eN49P7-FRv1-65 or eN49P7-FRv1-85. In some embodiments, the antibody comprises a VH CDR1, VH CDR2, VL CDR1, VL CDR2, and VL CDR3 shown in Table 2. [00100] In some embodiments, an isolated monoclonal antibody described herein specifically binds to HIV Env and comprises a heavy chain variable region comprising a VH CDR1, VH CDR2, and VH CDR3 and a light chain variable region comprising a VL CDR1, VL CDR2, and VL CDR3, wherein (a) the VH CDR1 comprises an amino acid sequence that is at least about 90%, 95%, 97%, 98%, 99% or 100% identical to the VH CDR1 of eN49P7-FRv1-23, eN49P7-FRv1-65 or eN49P7-FRv1-85; (b) the VH CDR2 comprises an amino acid sequence that is at least about 90%, 95%, 97%, 98%, 99% or 100% identical to the VH CDR2 of eN49P7-FRv1-23, eN49P7-FRv1-65 or eN49P7-FRv1- 85; and (c) the VH CDR3 comprises an amino acid sequence that is at least about 90%, 95%, 97%, 98%, 99% or 100% identical to the VH CDR3 of eN49P7-FRv1-23, eN49P7- FRv1-65 or eN49P7-FRv1-85. In some embodiments, the antibody comprises the VL CDR1, VL CDR2, and VL CDR3 of eN49P7-FRv1-23, eN49P7-FRv1-65 or eN49P7- FRv1-85. In some embodiments, the antibody comprises a VL CDR1, VL CDR2, and VL CDR3 shown in Table 2. [00101] In some embodiments, an isolated monoclonal antibody described herein specifically binds to HIV Env and comprises a heavy chain variable region comprising a VH CDR1, VH CDR2, and VH CDR3 and a light chain variable region comprising a VL CDR1, VL CDR2, and VL CDR3, wherein (a) the VH CDR1 comprises an amino acid sequence that is at least about 90%, 95%, 97%, 98%, 99% or 100% identical to a VH CDR1 shown in Table 2; (b) the VH CDR2 comprises an amino acid sequence that is at least about 90%, 95%, 97%, 98%, 99% or 100% identical to a VH CDR2 shown in Table 2; and (c) the VH CDR3 comprises an amino acid sequence that is at least about 90%, 95%, 97%, 98%, 99% or 100% identical to a VH CDR3 shown in Table 2. In some embodiments, the antibody comprises the VL CDR1, VL CDR2, and VL CDR3 of eN49P7-FRv1-23, eN49P7-FRv1-65 or eN49P7-FRv1-85. In some embodiments, the antibody comprises a VL CDR1, VL CDR2, and VL CDR3 shown in Table 2. [00102] In some embodiments, an isolated monoclonal antibody described herein specifically binds to HIV Env and comprises a heavy chain variable region comprising a VH CDR1, VH CDR2, and VH CDR3 and a light chain variable region comprising a VL CDR1, VL CDR2, and VL CDR3, wherein (a) the VH CDR1 comprises the VH CDR1 of eN49P7-FRv1-23, eN49P7-FRv1-65 or eN49P7-FRv1-85 comprising 0, 1, 2, 3, 4, or 5 substitutions, insertions, or deletions; (b) the VH CDR2 comprises the VH CDR2 of eN49P7-FRv1-23, eN49P7-FRv1-65 or eN49P7-FRv1-85 comprising 0, 1, 2, 3, 4, or 5 substitutions, insertions, or deletions; and (c) the VH CDR3 comprises the VH CDR3 of eN49P7-FRv1-23, eN49P7-FRv1-65 or eN49P7-FRv1-85comprising 0, 1, 2, 3, 4, or 5 substitutions, insertions, or deletions. In some embodiments, the antibody comprises the VL CDR1, VL CDR2, and VL CDR3 of eN49P7-FRv1-23, eN49P7-FRv1-65 or eN49P7- FRv1-85. In some embodiments, the antibody comprises a VL CDR1, VL CDR2, and VL CDR3 shown in Table 2. [00103] In some embodiments, an isolated monoclonal antibody described herein specifically binds to HIV Env and comprises a heavy chain variable region comprising a VH CDR1, VH CDR2, and VH CDR3 and a light chain variable region comprising a VL CDR1, VL CDR2, and VL CDR3, wherein (a) the VH CDR1 comprises a VH CDR1 shown in Table 2 comprising 0, 1, 2, 3, 4, or 5 substitutions, insertions, or deletions; (b) a VH CDR2 comprises the VH CDR2 shown in Table 2 comprising 0, 1, 2, 3, 4, or 5 substitutions, insertions, or deletions; and (c) a VH CDR3 comprises the VH CDR3 shown in Table 2 comprising 0, 1, 2, 3, 4, or 5 substitutions, insertions, or deletions. In some embodiments, the antibody comprises the VL CDR1, VL CDR2, and VL CDR3 of eN49P7-FRv1-23, eN49P7-FRv1-65 or eN49P7-FRv1-85. In some embodiments, the antibody comprises a VL CDR1, VL CDR2, and VL CDR3 shown in Table 2. In some embodiments, an isolated monoclonal antibody described herein specifically binds to HIV Env and comprises a heavy chain variable region comprising a VH CDR1, VH CDR2, and VH CDR3 and a light chain variable region comprising a VL CDR1, VL CDR2, and VL CDR3, wherein (a) the VH CDR1 comprises the VH CDR1 of eN49P7-FRv1-23, eN49P7-FRv1-65 or eN49P7-FRv1-85; (b) the VH CDR2 comprises the VH CDR2 of eN49P7-FRv1-23, eN49P7-FRv1-65 or eN49P7-FRv1-85; and (c) the VH CDR3 comprises the eN49P7-FRv1-23, eN49P7-FRv1-65 or eN49P7-FRv1-85. In some embodiments, the antibody comprises the VL CDR1, VL CDR2, and VL CDR3 of eN49P7-FRv1-23, eN49P7-FRv1-65 or eN49P7-FRv1-85. In some embodiments, the antibody comprises a VL CDR1, VL CDR2, and VL CDR3 shown in Table 2. In some embodiments, an isolated monoclonal antibody described herein specifically binds to HIV Env and comprises a heavy chain variable region comprising a VH CDR1, VH CDR2, and VH CDR3 and a light chain variable region comprising a VL CDR1, VL CDR2, and VL CDR3, wherein (a) the VH CDR1 comprises a VH CDR1 shown in Table 2; (b) the VH CDR2 comprises a VH CDR2 shown in Table 2; and (c) the VH CDR3 comprises a VH CDR3 shown in Table 2. In some embodiments, the antibody comprises the VL CDR1, VL CDR2, and VL CDR3 of eN49P7-FRv1-23, eN49P7-FRv1- 65 or eN49P7-FRv1-85. In some embodiments, the antibody comprises a VL CDR1, VL CDR2, and VL CDR3 shown in Table 2. In some embodiments, an isolated monoclonal antibody described herein specifically binds to HIV Env and comprises a heavy chain variable region comprising a VH CDR1, VH CDR2, and VH CDR3 and a light chain variable region comprising a VL CDR1, VL CDR2, and VL CDR3, wherein (a) the VL CDR1 comprises an amino acid sequence that is at least about 90%, 95%, 97%, 98%, 99% or 100% identical to the VL CDR1 of eN49P7-FRv1-23, eN49P7-FRv1-65 or eN49P7-FRv1-85; (b) the VL CDR2 comprises an amino acid sequence that is at least about 90%, 95%, 97%, 98%, 99% or 100% identical to the VL CDR2 of eN49P7-FRv1-23, eN49P7-FRv1-65 or eN49P7-FRv1- 85; and (c) the VL CDR3 comprises an amino acid sequence that is at least about 90%, 95%, 97%, 98%, 99% or 100% identical to the VL CDR3 of eN49P7-FRv1-23, eN49P7- FRv1-65 or eN49P7-FRv1-85. In some embodiments, the antibody comprises the VH CDR1, VH CDR2, and VH CDR3 of eN49P7-FRv1-23, eN49P7-FRv1-65 or eN49P7- FRv1-85. In some embodiments, the antibody comprises a VH CDR1, VH CDR2, and VH CDR3 shown in Table 2. In some embodiments, an isolated monoclonal antibody described herein specifically binds to HIV Env and comprises a heavy chain variable region comprising a VH CDR1, VH CDR2, and VH CDR3 and a light chain variable region comprising a VL CDR1, VL CDR2, and VL CDR3, wherein (a) the VL CDR1 comprises an amino acid sequence that is at least about 90%, 95%, 97%, 98%, 99% or 100% identical to a VL CDR1 shown in Table 2; (b) the VL CDR2 comprises an amino acid sequence that is at least about 90%, 95%, 97%, 98%, 99% or 100% identical to a VL CDR2 shown in Table 2; and (c) the VL CDR3 comprises an amino acid sequence that is at least about 90%, 95%, 97%, 98%, 99% or 100% identical to a VL CDR3 shown in Table 2. In some embodiments, the antibody comprises the VH CDR1, VH CDR2, and VH CDR3 of eN49P7-FRv1-23, eN49P7-FRv1-65 or eN49P7-FRv1-85. In some embodiments, the antibody comprises a VH CDR1, VH CDR2, and VH CDR3 shown in Table 2. In some embodiments, an isolated monoclonal antibody described herein specifically binds to HIV Env and comprises a heavy chain variable region comprising a VH CDR1, VH CDR2, and VH CDR3 and a light chain variable region comprising a VL CDR1, VL CDR2, and VL CDR3, wherein (a) the VL CDR1 comprises the VL CDR1 of eN49P7-FRv1-23, eN49P7-FRv1-65 or eN49P7-FRv1-85 comprising 0, 1, 2, 3, 4, or 5 substitutions, insertions, or deletions; (b) the VL CDR2 comprises the VL CDR2 of eN49P7-FRv1-23, eN49P7-FRv1-65 or eN49P7-FRv1-85 comprising 0, 1, 2, 3, 4, or 5 substitutions, insertions, or deletions; and (c) the VL CDR3 comprises the VL CDR3 of eN49P7-FRv1-23, eN49P7-FRv1-65 or eN49P7-FRv1-85 comprising 0, 1, 2, 3, 4, or 5 substitutions, insertions, or deletions. In some embodiments, the antibody comprises the VH CDR1, VH CDR2, and VH CDR3 of eN49P7-FRv1-23, eN49P7-FRv1-65 or eN49P7- FRv1-85. In some embodiments, the antibody comprises a VH CDR1, VH CDR2, and VH CDR3 shown in Table 2. In some embodiments, an isolated monoclonal antibody described herein specifically binds to HIV Env and comprises a heavy chain variable region comprising a VH CDR1, VH CDR2, and VH CDR3 and a light chain variable region comprising a VL CDR1, VL CDR2, and VL CDR3, wherein (a) the VL CDR1 comprises a VL CDR1 shown in Table 2 comprising 0, 1, 2, 3, 4, or 5 substitutions, insertions, or deletions; (b) the VL CDR2 comprises a VL CDR2 shown in Table 2 comprising 0, 1, 2, 3, 4, or 5 substitutions, insertions, or deletions; and (c) the VL CDR3 comprises a VL CDR3 shown in Table 2 comprising 0, 1, 2, 3, 4, or 5 substitutions, insertions, or deletions. In some embodiments, the antibody comprises the VH CDR1, VH CDR2, and VH CDR3 of eN49P7-FRv1-23, eN49P7-FRv1-65 or eN49P7-FRv1-85. In some embodiments, the antibody comprises a VH CDR1, VH CDR2, and VH CDR3 shown in Table 2. In some embodiments, an isolated monoclonal antibody described herein specifically binds to HIV Env and comprises a heavy chain variable region comprising a VH CDR1, VH CDR2, and VH CDR3 and a light chain variable region comprising a VL CDR1, VL CDR2, and VL CDR3, wherein (a) the VL CDR1 comprises the VL CDR1 of eN49P7-FRv1-23, eN49P7-FRv1-65 or eN49P7-FRv1-85; (b) the VL CDR2 comprises the VL CDR2 of eN49P7-FRv1-23, eN49P7-FRv1-65 or eN49P7-FRv1-85; and (c) the VL CDR3 comprises the VL CDR3 of eN49P7-FRv1-23, eN49P7-FRv1-65 or eN49P7-FRv1- 85. In some embodiments, the antibody comprises the VH CDR1, VH CDR2, and VH CDR3 of eN49P7-FRv1-23, eN49P7-FRv1-65 or eN49P7-FRv1-85. In some embodiments, the antibody comprises a VH CDR1, VH CDR2, and VH CDR3 shown in Table 2. In some embodiments, an isolated monoclonal antibody described herein specifically binds to HIV Env and comprises a heavy chain variable region comprising a VH CDR1, VH CDR2, and VH CDR3 and a light chain variable region comprising a VL CDR1, VL CDR2, and VL CDR3, wherein (a) the VL CDR1 comprises a VL CDR1 shown in Table 2; (b) the VL CDR2 comprises a VL CDR2 shown in Table 2; and (c) the VL CDR3 comprises a VL CDR3 shown in Table 2. In some embodiments, the antibody comprises the VH CDR1, VH CDR2, and VH CDR3 of eN49P7-FRv1-23, eN49P7-FRv1- 65 or eN49P7-FRv1-85. In some embodiments, the antibody comprises a VH CDR1, VH CDR2, and VH CDR3 shown in Table 2. In some embodiments, an isolated monoclonal antibody described herein specifically binds to HIV Env and comprises a heavy chain variable region comprising a VH CDR1, VH CDR2, and VH CDR3 and a light chain variable region comprising a VL CDR1, VL CDR2, and VL CDR3, wherein the VH CDR1, VH CDR2, VH CDR3, VL CDR1, VL CDR2, and VL CDR3 comprise the amino acid sequence of the eN49P7-FRv1- 23, eN49P7-FRv1-65 or eN49P7-FRv1-85 VH CDR1, VH CDR2, VH CDR3, VL CDR1, VL CDR2, and VL CDR3, respectively. In some embodiments, an isolated monoclonal antibody described herein specifically binds to HIV Env and comprises a heavy chain variable region comprising a VH CDR1, VH CDR2, and VH CDR3 and a light chain variable region comprising a VL CDR1, VL CDR2, and VL CDR3, wherein the VH CDR1, VH CDR2, VH CDR3, VL CDR1, VL CDR2, and VL CDR3 comprise the amino acid sequence of the eN49P7-FRv1- 23, eN49P7-FRv1-65 or eN49P7-FRv1-85 VH CDR1, VH CDR2, VH CDR3, VL CDR1, VL CDR2, and VL CDR3, respectively, shown in Table 2. In some embodiments, an isolated monoclonal antibody described herein specifically binds to HIV Env and comprises a heavy chain variable region comprising a VH CDR1, VH CDR2, and VH CDR3 and a light chain variable region comprising a VL CDR1, VL CDR2, and VL CDR3, wherein the VH CDR1, VH CDR2, VH CDR3, VL CDR1, VL CDR2, and VL CDR3 comprise the amino acid sequence of the eN49P7-FRv1- 23 VH CDR1, VH CDR2, VH CDR3, VL CDR1, VL CDR2, and VL CDR3, respectively. In some embodiments, an isolated monoclonal antibody described herein specifically binds to HIV Env and comprises a heavy chain variable region comprising a VH CDR1, VH CDR2, and VH CDR3 and a light chain variable region comprising a VL CDR1, VL CDR2, and VL CDR3, wherein the VH CDR1, VH CDR2, VH CDR3, VL CDR1, VL CDR2, and VL CDR3 comprise the amino acid sequence of the eN49P7-FRv1- 65 VH CDR1, VH CDR2, VH CDR3, VL CDR1, VL CDR2, and VL CDR3, respectively. In some embodiments, an isolated monoclonal antibody described herein specifically binds to HIV Env and comprises a heavy chain variable region comprising a VH CDR1, VH CDR2, and VH CDR3 and a light chain variable region comprising a VL CDR1, VL CDR2, and VL CDR3, wherein the VH CDR1, VH CDR2, VH CDR3, VL CDR1, VL CDR2, and VL CDR3 comprise the amino acid sequence of the eN49P7-FRv1- 85 VH CDR1, VH CDR2, VH CDR3, VL CDR1, VL CDR2, and VL CDR3, respectively. In some embodiments, an isolated monoclonal antibody described herein specifically binds to HIV Env and comprises a heavy chain variable region comprising a VH CDR1, VH CDR2, and VH CDR3 and a light chain variable region comprising a VL CDR1, VL CDR2, and VL CDR3, wherein the VH CDR1, VH CDR2, VH CDR3, VL CDR1, VL CDR2, and VL CDR3 comprise the amino acid sequence of the eN49P7-FRv1- 23 VH CDR1, VH CDR2, VH CDR3, VL CDR1, VL CDR2, and VL CDR3, respectively, shown in Table 2. In some embodiments, an isolated monoclonal antibody described herein specifically binds to HIV Env and comprises a heavy chain variable region comprising a VH CDR1, VH CDR2, and VH CDR3 and a light chain variable region comprising a VL CDR1, VL CDR2, and VL CDR3, wherein the VH CDR1, VH CDR2, VH CDR3, VL CDR1, VL CDR2, and VL CDR3 comprise the amino acid sequence of the eN49P7-FRv1- 65 VH CDR1, VH CDR2, VH CDR3, VL CDR1, VL CDR2, and VL CDR3, respectively, shown in Table 2. In some embodiments, an isolated monoclonal antibody described herein specifically binds to HIV Env and comprises a heavy chain variable region comprising a VH CDR1, VH CDR2, and VH CDR3 and a light chain variable region comprising a VL CDR1, VL CDR2, and VL CDR3, wherein the VH CDR1, VH CDR2, VH CDR3, VL CDR1, VL CDR2, and VL CDR3 comprise the amino acid sequence of the eN49P7-FRv1- 85 VH CDR1, VH CDR2, VH CDR3, VL CDR1, VL CDR2, and VL CDR3, respectively, shown in Table 2. In some embodiments, an isolated monoclonal antibody described herein specifically binds to HIV Env and comprises a heavy chain variable region (VH) and a light chain variable region (VL), wherein the VH comprises an amino acid sequence that is at least about 90%, 95%, 97%, 98%, 99% or 100% identical to the VH of eN49P7-FRv1- 23, eN49P7-FRv1-65 or eN49P7-FRv1-85. In some embodiments, the antibody comprises the VH CDR1, VH CDR2, VH CDR3, VL CDR1, VL CDR2, and VL CDR3 of eN49P7- FRv1-23, eN49P7-FRv1-65 or eN49P7-FRv1-85. In some embodiments, the antibody comprises a VH CDR1, VH CDR2, VH CDR3, VL CDR1, VL CDR2, and VL CDR3 shown in Table 2. In some embodiments, the antibody comprises the VL of eN49P7-FRv1- 23, eN49P7-FRv1-65 or eN49P7-FRv1-85. In some embodiments, an isolated monoclonal antibody described herein specifically binds to HIV Env and comprises a heavy chain variable region (VH) and a light chain variable region (VL), wherein the VL comprises an amino acid sequence that is at least about 90%, 95%, 97%, 98%, 99% or 100% identical to the VL of eN49P7-FRv1- 23, eN49P7-FRv1-65 or eN49P7-FRv1-85. In some embodiments, the antibody comprises the VH CDR1, VH CDR2, VH CDR3, VL CDR1, VL CDR2, and VL CDR3 of eN49P7- FRv1-23, eN49P7-FRv1-65 or eN49P7-FRv1-85. In some embodiments, the antibody comprises a VH CDR1, VH CDR2, VH CDR3, VL CDR1, VL CDR2, and VL CDR3 shown in Table 2. In some embodiments, the antibody comprises the VH of an antibody described herein. In some embodiments, the antibody comprises the VH of eN49P7-FRv1- 23, eN49P7-FRv1-65 or eN49P7-FRv1-85. In some embodiments, an isolated monoclonal antibody described herein specifically binds to HIV Env and comprises a heavy chain variable region (VH) and a light chain variable region (VL), wherein the VH and VL comprise an amino acid sequence that is at least about 90%, 95%, 97%, 98%, 99% or 100% identical to the eN49P7-FRv1- 23, eN49P7-FRv1-65 or eN49P7-FRv1-85 VH and VL, respectively. In some embodiments, the antibody comprises the VH CDR1, VH CDR2, VH CDR3, VL CDR1, VL CDR2, and VL CDR3 of eN49P7-FRv1-23, eN49P7-FRv1-65 or eN49P7-FRv1-85. In some embodiments, the antibody comprises a VH CDR1, VH CDR2, VH CDR3, VL CDR1, VL CDR2, and VL CDR3 shown in Table 2. In some embodiments, an isolated monoclonal antibody described herein specifically binds to HIV Env and comprises a heavy chain variable region (VH) and a light chain variable region (VL), and the VH further comprises a VH FR1, VH FR2, VH FR3, and VH FR4, wherein the VH FR1, VH FR2, VH FR3, and VH FR4 comprises an amino acid sequence with at least about 80%, at least about 85%, at least about 90%, at least about 95%, at least about 97%, at least about 98%, at least about 99% or 100% identity to the VH FR1, VH FR2, VH FR3, and VH FR4, respectively, of eN49P7-FRv1-23, eN49P7-FRv1-65 or eN49P7-FRv1-85. In some embodiments, an isolated monoclonal antibody described herein specifically binds to HIV Env and comprises a heavy chain variable region (VH) and a light chain variable region (VL), and the VL further comprises a VL FR1, VL FR2, VL FR3, and VL FR4, wherein the VL FR1, VL FR2, VL FR3, and VL FR4 comprises an amino acid sequence with at least about 80%, at least about 85%, at least about 90%, at least about 95%, at least about 97%, at least about 98%, at least about 99% or 100% identity to the VL FR1, VL FR2, VL FR3, and VL FR4, respectively, of eN49P7-FRv1-23, eN49P7-FRv1-65 or eN49P7-FRv1-85. In some embodiments, an isolated monoclonal antibody described herein specifically binds to HIV Env and comprises a heavy chain variable region (VH) and a light chain variable region (VL), and further comprises a VH FR1, VH FR2, VH FR3, VH FR4, VL FR1, VL FR2, VL FR3, and VL FR4, wherein the VH FR1, VH FR2, VH FR3, VH FR4, VL FR1, VL FR2, VL FR3, and VL FR4 comprise an amino acid sequence with at least about 80%, at least about 85%, at least about 90%, at least about 95%, at least about 97%, at least about 98%, at least about 99% or 100% identity to the VH FR1, VH FR2, VH FR3, VH FR4, VL FR1, VL FR2, VL FR3, and VL FR4, respectively, of eN49P7-FRv1- 23, eN49P7-FRv1-65 or eN49P7-FRv1-85. In some embodiments, an isolated monoclonal antibody described herein specifically binds to HIV Env and comprises a heavy chain variable region (VH) and a light chain variable region (VL), wherein the VH comprises the VH FR1, VH FR2, VH FR3, and VH FR4 of eN49P7-FRv1-23, eN49P7-FRv1-65 or eN49P7-FRv1-85. In some embodiments, an isolated monoclonal antibody described herein specifically binds to HIV Env and comprises a heavy chain variable region (VH) and a light chain variable region (VL), wherein the VL comprises the VL FR1, VL FR2, VL FR3, and VL FR4 eN49P7- FRv1-23, eN49P7-FRv1-65 or eN49P7-FRv1-85. In some embodiments, the antibody comprises the VH CDR1, VH CDR2, VH CDR3, VL CDR1, VL CDR2, and VL CDR3 of eN49P7-FRv1-23, eN49P7-FRv1-65 or eN49P7-FRv1-85. In some embodiments, the antibody comprises a VH CDR1, VH CDR2, VH CDR3, VL CDR1, VL CDR2, and VL CDR3 shown in Table 2. In some embodiments, the antibody comprises the VH or VL of eN49P7-FRv1-23, eN49P7-FRv1-65 or eN49P7-FRv1-85. In some embodiments, an isolated monoclonal antibody described herein specifically binds to HIV Env and comprises a heavy chain variable region (VH) and a light chain variable region (VL), wherein the VH and VL comprise the VH FR1, VH FR2, VH FR3, VH FR4, VL FR1, VL FR2, VL FR3, and VL FR4 of eN49P7-FRv1-23, eN49P7- FRv1-65 or eN49P7-FRv1-85. In some embodiments, an antibody described herein is eN49P7-FRv1-23 comprising the eN49P7-FRv1-23 VH and eN49P7-FRv1-23 VL as shown in Table 1. In some embodiments, an antibody described herein is eN49P7-FRv1-65 comprising the eN49P7-FRv1-65 VH and eN49P7-FRv1-65 VL as shown in Table 1. In some embodiments, an antibody described herein is eN49P7-FRv1-85 comprising the eN49P7-FRv1-85 VH and eN49P7-FRv1-85 VL as shown in Table 1. In some embodiments, an isolated monoclonal antibody described herein further comprises heavy and/or light chain constant regions. In some embodiments, an isolated monoclonal antibody described herein further comprises human heavy and/or light chain constant regions. In some embodiments, the heavy chain constant region is selected from the group consisting of human immunoglobulins IgG1, IgG2, IgG3, IgG4, IgA1, and IgA2. In some embodiments, the heavy chain constant region comprises a native amino acid sequence. In some embodiments, the heavy chain constant region comprises a non-native variant amino acid sequence. In some embodiments, an antibody described herein is a recombinant antibody, a chimeric antibody, a bispecific antibody, a trispecific antibody, or a multispecific antibody. In some embodiments, the antibody fragment comprises a single-chain Fv (scFv), F(ab) fragment, F(ab’)2 fragment, or an isolated VH domain. In some embodiments, an antibody described herein is a multispecific antibody, e.g. a bispecific or trispecific antibody. Multispecific antibodies are monoclonal antibodies that have binding specificities for at least two different sites. In some embodiments, one of the binding specificities is for HIV Env and the other is for any other antigen. In some embodiments, bispecific antibodies bind to two different epitopes of HIV Env. Bispecific antibodies can be prepared as full length antibodies or antibody fragments. Techniques for making multispecific antibodies, e.g., bispecific antibodies include, but are not limited to, recombinant co-expression of two immunoglobulin heavy chain- light chain pairs having different specificities (see Milstein and Cuello, Nature 305: 537 (1983)), WO 93/08829, and Traunecker A., et al., EMBO J. 10: 3655 (1991)), and "knob- in-hole" engineering (see, e.g., U.S. Patent No. 5,731,168). Multi-specific antibodies may also be made by engineering electrostatic steering effects for making antibody Fc- heterodimeric molecules (WO 2009/089004A1); cross-linking two or more antibodies or fragments (see, e.g., US Patent No.4,676,980, and Brennan et al., Science, 229: 81 (1985)); using leucine zippers to produce bi-specific antibodies (see, e.g., Kostelny et al., J. Immunol., 148(5):1547-1553 (1992)); using "diabody" technology for making bispecific antibody fragments (see, e.g., Hollinger et al., Proc. Natl. Acad. Sci. USA, 90:6444-6448 (1993)); and using single-chain Fv (scFv) dimers (see, e.g. Gruber et al., J. Immunol., 152:5368 (1994)); and preparing trispecific antibodies as described, e.g., in Tutt et al. J. Immunol. 147: 60 (1991). Engineered antibodies with three or more functional antigen- binding sites, including "Octopus antibodies" and dual variable domain (DVD) immunoglobulins are also included herein (see, e.g. US 2006/0025576A1 and US Patent 10,093,733). The antibody or fragment disclosed herein also includes a "Dual Acting Fab" or "DAF" comprising an antigen-binding site that binds to different epitopes, e.g., two different HIV Env epitopes (see, US 2008/0069820, for example). In some embodiments, a multispecific antibody described herein comprises Fc regions comprising knob-in-hole engineered variations (see, e.g., "knob" Fc regions of SEQ ID NO: 93, 94 and 95 and "hole" Fc regions of SEQ ID NO: 96, 97 and 98). In some embodiments, an antibody described herein comprises a first variant Fc region comprising a "knob" mutation (see, e.g., SEQ ID NO: 93) and a second variant Fc region comprising a "hole" mutation (see, e.g., SEQ ID NO: 96). In some embodiments, an antibody described herein comprises a first variant Fc region comprising a "knob" mutation and an "LS" mutation (see, e.g., SEQ ID NO: 94) and a second variant Fc region comprising a "hole" mutation and an 'LS" mutation (see, e.g., SEQ ID NO: 97). In some embodiments, an antibody described herein comprises a first variant Fc region comprising a "knob" mutation and an "YTE" mutation (see, e.g., SEQ ID NO: 95) and a second variant Fc region comprising a "hole" mutation and an 'YTE" mutation (see, e.g., SEQ ID NO: 98). In some embodiments, an antibody described herein is a multispecific antibody, e.g. a bispecific antibody comprising a first antigen-binding domain comprising a VH domain or VH and VL domains disclosed herein, and a second antigen-binding region capable of binding an HIV Env epitope. In some embodiments, the second antigen-binding region binds to an HIV Env epitope region different from the HIV Env epitope region bound by an antibody disclosed herein. In some embodiments, the second agent is one or more anti-HIV Env antibody that binds to the CD4 binding site (CD4bs), V2 apex, N332/V3 base supersite, silent face, gp120-gp41 interface or membrane-proximal external region (MPER). In some embodiments, the second agent is one or more anti-HIV Env antibody that binds to the V2 apex, N332/V3 base supersite, silent face, gp120-gp41 interface or membrane-proximal external region (MPER). In some embodiments, the second antigen-binding region binds to the CD4 binding site (CD4bs) epitope region. In some embodiments, the second antigen-binding region binds to the V2 apex. In some embodiments, the second antigen-binding region binds to the N332/V3 base supersite. In some embodiments, the second antigen-binding region binds to the gp120-gp41 interface epitope region. In some embodiments, the second antigen-binding region binds to the silent face. In some embodiments, the second antigen-binding region binds to the membrane- proximal external region (MPER). Multispecific (e.g., bispecific and trispecific) anti-HIV Env antibodies and methods of producing thereof are known to those skilled in the art, for example, as described in WO2024192203, which is incorporated herein by reference in its entirety for all purposes. In one aspect, provided herein is a multispecific anti-HIV antibody comprising at least two antigen binding domains selected from the group consisting of (a) an antigen binding domain that binds to the V3 loop epitope region of HIV Env; (b) an antigen binding domain that binds to the V1/V2 apex epitope region of HIV Env; and (c) an antigen binding domain that binds to the CD4bs epitope region of HIV Env. In some embodiments, the multispecific antibody is a bispecific antibody. In some embodiments, the multispecific antibody is a trispecific antibody. In some embodiments, the antigen binding domain that binds to the V3 loop epitope region of HIV Env comprises a VH domain and a VL domain comprising the 3 VH CDRs and 3 VL CDRs, respectively, of PGT121 or an engineered variant of PGT121. In some embodiments, the antigen binding domain that binds to the V3 loop epitope region of HIV Env comprises a VH domain and a VL domain comprising the 3 VH CDRs and 3 VL CDRs, respectively, of ePGT121v1 or ePGT121v2. In some embodiments, the antigen binding domain that binds to the V1/V2 apex epitope region of HIV Env comprises a VH domain and a VL domain comprising the 3 VH CDRs and 3 VL CDRs, respectively, of PGDM1400 or an engineered variant of PGDM1400. In some embodiments, the antigen binding domain that binds to the V1/V2 apex epitope region of HIV Env comprises a VH domain and a VL domain comprising the 3 VH CDRs and 3 VL CDRs, respectively, of ePGDM1400v9. In some embodiments, the antigen binding domain that binds to the CD4bs epitope region of HIV Env comprises a VH domain and a VL domain comprising the 3 VH CDRs and 3 VL CDRs, respectively, of eN49P7-FRv1-23, eN49P7-FRv1-65 or eN49P7-FRv1-85. Multispecific (e.g., bispecific and trispecific) anti- HIV Env antibodies are known to those skilled in the art, for example, as described in WO2024192203, which is incorporated herein by reference in its entirety for all purposes. Table 3. SEQ ID NOs of VH, VL, and CDR sequences of ePGT121v1, ePGT121v2, and ePGDM1400v9 VH VL VH VH VH VL VL VL CDR1 CDR2 CDR3 CDR1 CDR2 CDR n some embod men s, e an gen b nd ng doma n a b nds o e V3 loop epitope region of HIV Env comprises a VH domain and a VL domain comprising the 3 VH CDRs and 3 VL CDRs, respectively, of PGT121 or an engineered variant of PGT121. PGT121 has been disclosed, for example, in U.S. patent No. 9,464,131, which is incorporated by reference herein for all purposes. Engineered PGT121 variants have been disclosed, for example, in Int. Pat. Appl. Pub. No. WO/2020/023827, which is incorporated by reference herein for all purposes. In some embodiments, the VH domain comprises the VH CDR1, VH CDR2, VH CDR3 of ePGT121v1 or ePGT121v2, and the VL domain comprises the VL CDR1, VL CDR2 and VL CDR3 of ePGT121v1 or ePGT121v2. In some embodiments, the VH CDR1, VH CDR2, VH CDR3, VL CDR1, VL CDR2 and VL CDR3 comprise the amino acid sequence of SEQ ID NO: 42, 43, 44, 46, 47, and 48, respectively, or SEQ ID NO: 52, 53, 54, 56, 57, and 58, respectively. In some embodiments, the VH domain and VL domain comprises an amino acid sequence having at least 80%, at least 85%, at least 90%, at least 95%, at least 97% or 100% identity to SEQ ID NO: 41 and 45, respectively, or 51 and 55, respectively. In some embodiments, the antigen binding domain comprises an scFv domain or an Fab domain. In some embodiments, the antigen binding domain that binds to the V1/V2 apex epitope region of HIV Env comprises a VH domain and a VL domain comprising the 3 VH CDRs and 3 VL CDRs, respectively, of PGDM1400 or an engineered variant of PGDM1400. PGDM1400 has been disclosed, for example, in U.S. Pat. Appl. Pub. No. 20150361160, which is incorporated by reference herein for all purposes. Engineered PGDM1400 variants have been disclosed, for example, in Int. Pat. Appl. Pub. No. WO2021087015, which is incorporated by reference herein for all purposes. In some embodiments, the VH domain comprises the VH CDR1, VH CDR2, VH CDR3 of ePGDM1400v9, and the VL domain comprises the VL CDR1, VL CDR2 and VL CDR3 of ePGDM1400v9. In some embodiments, the VH CDR1, VH CDR2, VH CDR3, VL CDR1, VL CDR2 and VL CDR3 comprise the amino acid sequence of SEQ ID NO: 62, 63, 64, 66, 67, and 68, respectively. In some embodiments, the VH domain and VL domain comprises an amino acid sequence having at least 80%, at least 85%, at least 90%, at least 95%, at least 97% or 100% identity to SEQ ID NO: 61 and 65, respectively. In some embodiments, the antigen binding domain comprises an scFv domain or an Fab domain. In some embodiments, the antigen binding domain that binds to the CD4bs epitope region of HIV Env comprises a VH domain and a VL domain comprising the 3 VH CDRs and 3 VL CDRs, respectively, of eN49P7-FRv1-23, eN49P7-FRv1-65 or eN49P7- FRv1-85. In some embodiments, the VH domain comprises the VH CDR1, VH CDR2, VH CDR3 of N49P7, and the VL domain comprises the VL CDR1, VL CDR2 and VL CDR3 of eN49P7-FRv1-23, eN49P7-FRv1-65 or eN49P7-FRv1-85. In some embodiments, the VH CDR1, VH CDR2, VH CDR3, VL CDR1, VL CDR2 and VL CDR3 as shown in Table 2. In some embodiments, the eN49P7-FRv1-23, eN49P7-FRv1-65 or eN49P7-FRv1-85 VH domain and VL domain comprises an amino acid sequence having at least 80%, at least 85%, at least 90%, at least 95%, at least 97% or 100% identity to the sequences shown in Table 1. In some embodiments, the antigen binding domain comprises an scFv domain or an Fab domain. In some embodiments, a multispecific anti-HIV antibody described herein comprises at least two antigen binding domains selected from the group consisting of (a) an antigen binding domain that binds to the V3 loop epitope region of HIV Env and comprises a VH domain and a VL domain comprising the 3 VH CDRs and 3 VL CDRs, respectively, of ePGT121v1 or ePGT121v2; (b) an antigen binding domain that binds to the V1/V2 apex epitope region of HIV Env and comprises a VH domain and a VL domain comprising the 3 VH CDRs and 3 VL CDRs, respectively, of ePGDM1400v9; and (c) an antigen binding domain that binds to the CD4bs epitope region of HIV Env and comprises a VH domain and a VL domain comprising the 3 VH CDRs and 3 VL CDRs, respectively, of eN49P7-FRv1-23, eN49P7-FRv1-65 or eN49P7-FRv1-85. In some embodiments, the multispecific antibody is a bispecific antibody. In some embodiments, the multispecific antibody is a trispecific antibody. In some embodiments, a multispecific anti-HIV antibody described herein comprises an scFv domain linked to an antibody, wherein the scFv domain and the antibody have different binding specificities. In some embodiments, the C-terminal end of the scFv domain is linked to the N-terminal end of the antibody light chain. In some embodiments, the linker comprises between 15 and 35 amino acid residues. In some embodiments, the linker comprises between 25 and 45 amino acid residues. In some embodiments, the multispecific antibody is a bispecific antibody. In some embodiments, the multispecific antibody is a trispecific antibody. In some embodiments, the linker comprises between 20 and 30 amino acid residues, between 20 and 27 amino acid residues, between 23 and 30 amino acid residues, or between 23 and 27 amino acid residues. In some embodiments, the linker comprises 20, 21, 22, 23, 24, 25, 26, 27, 28, 29 or 30 amino acid residues, optionally wherein the linker comprises 23, 24, 25, 26, or 27 amino acid residues. In some embodiments, the linker comprises one or more copies of the amino acid sequence of SEQ ID NO: 71, 72, 73, or 74. In some embodiments, the multispecific antibody is a bispecific antibody. In some embodiments, the multispecific antibody is a trispecific antibody. In some embodiments, the linker comprises between 30 and 40 amino acid residues, between 30 and 37 amino acid residues, between 33 and 40 amino acid residues, or between 33 and 37 amino acid residues. In some embodiments, the linker comprises 30, 31, 32, 33, 34, 35, 36, 37, 38, 39 or 40 amino acid residues, optionally wherein the linker comprises 33, 34, 35, 36, or 37 amino acid residues. In some embodiments, the linker comprises one or more copies of the amino acid sequence of SEQ ID NO: 71, 72, 73, or 74. In some embodiments, the multispecific antibody is a bispecific antibody. In some embodiments, the multispecific antibody is a trispecific antibody. In some embodiments, a multispecific antibody disclosed herein is a trispecific antibody. In some embodiments, a trispecific antibody disclosed herein comprises a first scFv linked to a first Fc domain, an antibody heavy chain comprising a second Fc domain, and second Fc domain linked to an antibody light chain. In some embodiments, a trispecific antibody disclosed herein comprises a first and second scFv linked to a first Fc domain, an antibody heavy chain comprising a second Fc domain, and an antibody light chain. In some embodiments, a trispecific antibody disclosed herein comprises a first scFv linked to a first Fc domain, second Fc domain linked to an antibody heavy chain comprising a second Fc domain, and an antibody light chain. In some embodiments, the first and second Fc domains are IgG Fc domains. In some embodiments, the first and/or second Fc domain has been modified to promote heterodimer formation. In some embodiments, the first Fc domain comprises the T366W substitution and the second Fc domain comprises the T366S, L368A and Y407V substitutions. In some embodiments, the first Fc domain comprises the T366S, L368A and Y407V substitutions and the second Fc domain comprises the T366W substitution. In some embodiments, the first Fc domain comprises the K409R substitution and the second Fc domain comprises the F405L substitution, or the first Fc domain comprises the F405L substitution and the second Fc domain comprises the K409R substitution. In some embodiments, a trispecific antibody described herein comprises a first scFv linked to a first Fc domain, an antibody heavy chain comprising a second Fc domain, and second scFv domain linked to an antibody light chain, wherein the first scFv linked to a first Fc domain, the antibody heavy chain comprising a second Fc domain, and the second scFv domain linked to an antibody light chain comprise an amino acid sequence having at least 80%, at least 85%, at least 90%, at least 95%, at least 97% or 100% identity to SEQ ID NOs: 75, 76, and 79, respectively, SEQ ID NOs: 75, 76, and 81, respectively, or SEQ ID NOs: 75, 76, and 83, respectively. In some embodiments, a trispecific antibody described herein is TriS 27, TriS 28, or TriS 29. Table 4. Polypeptide chains of exemplary multispecific antibodies Multispecific Chain 1 Chain 2 Chain 3 antibody p p yp p p equence having at least about 80% sequence identity, at least about 85% sequence identity, at least about 90% sequence identity, at least about 95% sequence identity, at least about 96% sequence identity, at least about 97% sequence identity, at least about 98% sequence identity, or at least about 99% sequence, or is identical to the sequences listed in Table 4. In some embodiments, an antibody described herein comprises a heavy and/or light chain constant region. In some embodiments, an antibody described herein comprises a human heavy and/or light chain constant region. In some embodiments, the heavy chain constant region is human immunoglobulin IgG1, IgG2, IgG3, IgG4, IgA1, or IgA2 constant region. In some embodiments, the heavy chain constant region is human immunoglobulin IgG1 constant region. In some embodiments, the heavy chain constant region comprises a native amino acid sequence. In some embodiments, an antibody disclosed herein is capable of neutralizing at least about 40%, at least about 50%, at least about 60%, at least about 70%, at least about 80%, at least about 90%, or 100% of cross-clade HIV isolates in the 56 cross-clade indicator virus panel. In some embodiments, an antibody disclosed herein is capable of neutralizing at least about 40% of cross-clade HIV isolates in the 56 cross-clade indicator virus panel. In some embodiments, an antibody disclosed herein is capable of neutralizing at least about 50% of cross-clade HIV isolates in the 56 cross-clade indicator virus panel. In some embodiments, an antibody disclosed herein is capable of neutralizing at least about 60% of cross-clade HIV isolates in the 56 cross-clade indicator virus panel. In some embodiments, an antibody disclosed herein is capable of neutralizing at least about 70% of cross-clade HIV isolates in the 56 cross-clade indicator virus panel. In some embodiments, an antibody disclosed herein is capable of neutralizing at least about 80% of cross-clade HIV isolates in the 56 cross-clade indicator virus panel. In some embodiments, an antibody disclosed herein is capable of neutralizing at least about 90% of cross-clade HIV isolates in the 56 cross-clade indicator virus panel. In some embodiments, an antibody disclosed herein is capable of neutralizing at least about 95% of cross-clade HIV isolates in the 56 cross-clade indicator virus panel. In some embodiments, an antibody disclosed herein is capable of neutralizing at least about 98% of cross-clade HIV isolates in the 56 cross-clade indicator virus panel. In some embodiments, an antibody disclosed herein is capable of neutralizing 100% of cross-clade HIV isolates in the 56 cross-clade indicator virus panel. In some embodiments, an antibody disclosed herein is capable of neutralizing the cross- clade HIV isolates of the 56 cross-clade indicator virus panel with a median IC50 equal to or less than about 2 µg/ml, about 1.5 µg/ml, about 1 µg/ml, about 0.75 µg/ml, about 0.5 µg/ml, about 0.3 µg/ml, about 0.2 µg/ml, about 0.1 µg/ml, about 0.05 µg/ml, about 0.025 µg/ml, about 0.01 µg/ml, or about 0.005 µg/ml. In some embodiments, an antibody disclosed herein is capable of neutralizing at least about 40% of cross-clade HIV isolates in the 56 cross-clade indicator virus panel with a median IC50 equal to or less than 0.5 µg/ml. In some embodiments, an antibody disclosed herein is capable of neutralizing at least about 40% of cross-clade HIV isolates in the 56 cross-clade indicator virus panel with a median IC₅₀ equal to or less than 0.25 µg/ml. In some embodiments, an antibody disclosed herein is capable of neutralizing the cross-clade HIV isolates of the 56 cross- clade indicator virus panel with a median IC50 equal to or less than about 2 µg/ml. In some embodiments, an antibody disclosed herein is capable of neutralizing the cross-clade HIV isolates of the 56 cross-clade indicator virus panel with a median IC50 equal to or less than about 1.5 µg/ml. In some embodiments, an antibody disclosed herein is capable of neutralizing the cross-clade HIV isolates of the 56 cross-clade indicator virus panel with a median IC50 equal to or less than about 1 µg/ml. In some embodiments, an antibody disclosed herein is capable of neutralizing the cross-clade HIV isolates of the 56 cross- clade indicator virus panel with a median IC₅₀ equal to or less than about 2 µg/ml. In some embodiments, an antibody disclosed herein is capable of neutralizing the cross-clade HIV isolates of the 56 cross-clade indicator virus panel with a median IC50 equal to or less than about 1.5 µg/ml. In some embodiments, an antibody disclosed herein is capable of neutralizing the cross-clade HIV isolates of the 56 cross-clade indicator virus panel with a median IC50 equal to or less than about 1 µg/ml. In some embodiments, an antibody disclosed herein is capable of neutralizing at least about 90% cross-clade HIV isolates in the 56 cross-clade indicator virus panel with a median IC₅₀ equal to or less than about 1 µg/ml. In some embodiments, an antibody disclosed herein is capable of neutralizing at least about 80% cross-clade HIV isolates in the 56 cross-clade indicator virus panel with a median IC₅₀ equal to or less than about 1 µg/ml. In some embodiments, an antibody disclosed herein is capable of neutralizing at least about 90% cross-clade HIV isolates in the 56 cross-clade indicator virus panel with a median IC50 equal to or less than about 0.5 µg/ml. In some embodiments, an antibody disclosed herein is capable of neutralizing at least about 80% cross-clade HIV isolates in the 56 cross-clade indicator virus panel with a median IC50 equal to or less than about 0.5 µg/ml. In some embodiments, an antibody disclosed herein is capable of neutralizing the cross-clade HIV isolates of the 56 cross- clade indicator virus panel with a median IC₈₀ equal to or less than about 7 µg/ml, about 6 µg/ml, about 5 µg/ml, about 4 µg/ml, about 3 µg/ml, about 2 µg/ml, about 1 µg/ml, or about 0.5 µg/ml. In some embodiments, an antibody disclosed herein is capable of neutralizing the cross-clade HIV isolates of the 56 cross-clade indicator virus panel with a median IC₈₀ equal to or less than about 7 µg/ml. In some embodiments, an antibody disclosed herein is capable of neutralizing the cross-clade HIV isolates with a median IC80 equal to or less than about 6 µg/ml. In some embodiments, an antibody disclosed herein is capable of neutralizing the cross-clade HIV isolates of the 56 cross-clade indicator virus panel with a median IC80 equal to or less than about 5 µg/ml. In some embodiments, an antibody disclosed herein is capable of neutralizing the cross-clade HIV isolates of the 56 cross-clade indicator virus panel with a median IC₈₀ equal to or less than about 2 µg/ml. In some embodiments, an antibody disclosed herein is capable of neutralizing the cross-clade HIV isolates of the 56 cross-clade indicator virus panel with a median IC80 equal to or less than about 1 µg/ml. In another aspect, provided herein are antibodies that bind the same or an overlapping epitope of Env as an antibody described herein (e.g., eN49P7-FRv1-23, eN49P7-FRv1-65 or eN49P7-FRv1-85). In certain embodiments, the epitope of an antibody can be determined by, e.g., NMR spectroscopy, X-ray crystallography, negative- stain and cryo-EM (see, e.g., Lin M, et al., J Am Soc Mass Spectrom. 5: 961-971 (2018); Rantalainen et al., Cell Rep.23(11); 3249-3261 (2018); Torrents de la Peña A et al., PLoS Pathog.15;15(7):e1007920 (2019)), ELISA assays, hydrogen/deuterium exchange coupled with mass spectrometry (e.g., liquid chromatography electrospray mass spectrometry), array-based oligo-peptide scanning assays, and/or mutagenesis mapping (e.g., site-directed mutagenesis mapping). For X-ray crystallography, crystallization may be accomplished using any of the known methods in the art (e.g., Giegé R, et al., (1994) Acta Crystallogr D Biol Crystallogr 50(Pt 4): 339-350; McPherson A (1990) Eur J Biochem 189: 1-23; Chayen NE (1997) Structure 5: 1269-1274; McPherson A (1976) J Biol Chem 251: 6300-6303). Antibody:antigen crystals may be studied using well-known X-ray diffraction techniques and may be refined using computer software such as Phenix (Adams et al., Acta Crystallogr Biol Crystallogr D66, 213-221 (2010)) and BUSTER (Bricogne G (1993) Acta Crystallogr D Biol Crystallogr 49(Pt 1): 37-60; Bricogne G (1997) Meth. Enzymol.276A: 361-423, ed Carter CW; Roversi P et al., (2000) Acta Crystallogr. D Biol. Crystallogr.56(Pt 10): 1316- 1323). Mutagenesis mapping studies may be accomplished using any method known to one of skill in the art. See, e.g., Champe M et al., (1995) supra and Cunningham BC & Wells JA (1989) supra for a description of mutagenesis techniques, including alanine scanning mutagenesis techniques. In a specific embodiment, the epitope of an antibody is determined using alanine scanning mutagenesis studies. Usually, binding to the antigen is reduced or disrupted when a residue within the epitope is substituted to alanine. In some embodiments, the KD of binding to the antigen is increased by about 5-fold, 10-fold, 20- fold, 10-fold or more when a residue within the epitope is substituted for alanine. In some embodiments, binding affinity is determined by ELISA. In addition, antibodies that recognize and bind to the same or overlapping epitopes of Env can be identified using routine techniques such as an immunoassay, for example, by showing the ability of one antibody to block the binding of another antibody to a target antigen, i.e., a competitive binding assay. In some embodiments, an antibody described herein immunospecifically binds to the same epitope as that bound by eN49P7-FRv1-23, eN49P7-FRv1-65 or eN49P7- FRv1-85 antibody. In some embodiments, an antibody described herein immunospecifically binds to an epitope that overlaps the epitope bound by eN49P7-FRv1-23, eN49P7-FRv1-65 or eN49P7-FRv1-85. In some embodiments, an antibody described herein is capable of competing with eN49P7-FRv1-23, eN49P7-FRv1-65 or eN49P7-FRv1-85 for binding to HIV Env. In certain embodiments, the epitope of an antibody described herein is used as an immunogen to produce antibodies. In one aspect, provided herein are methods for producing an engineered variant of an antibody described herein. In some embodiments, a method for producing an engineered variant comprises directed-evolution and yeast display. Methods for producing an engineered antibody are known to those skilled in the art, for example, as described in WO2020023827, which is incorporated herein by reference in its entirety for all purposes. In some embodiments, an engineered antibody possesses one or more improved properties, for example, higher binding affinity to target antigen, higher binding affinity to target antigen at low pH, increased median neutralization IC₅₀ potency, and increased breadth of neutralization compared to the parent antibody. In some embodiments, a method of producing an engineered variant of a parent antibody comprises substituting one or more amino acid residues of the VH; and/or substituting one or more amino acid residues of the VL to create an engineered variant antibody, and producing the engineered variant antibody. In some embodiments, the parent antibody is an antibody described herein. In some embodiments, the parent antibody is eN49P7-FRv1-23, eN49P7-FRv1-65 or eN49P7-FRv1-85. In some embodiments, the method further comprises determining that the engineered variant antibody has improved properties, for example, by determining the engineered variant antibody's binding affinity to target antigen, binding affinity to target antigen at low pH, median neutralization IC₅₀ potency, or breadth of neutralization compared to the parent antibody. The affinity or avidity of an antibody for an antigen can be determined experimentally using any suitable method well-known in the art, e.g., flow cytometry, enzyme-linked immunoabsorbent assay (ELISA), biolayer interferometry (BLI) assay, radioimmunoassay (RIA), or kinetics (e.g., BIACORE™ analysis). Direct binding assays as well as competitive binding assay formats can be readily employed. (See, for example, Berzofsky, et al., "Antibody-Antigen Interactions," In Fundamental Immunology, Paul, W. E., Ed., Raven Press: New York, N.Y. (1984); Kuby, Janis Immunology, W. H. Freeman and Company: New York, N.Y. (1992); and methods described herein. The measured affinity of a particular antibody-antigen interaction can vary if measured under different conditions (e.g., salt concentration, pH, temperature). Thus, measurements of affinity and other antigen-binding parameters (e.g., KD or Kd, Kon, Koff) are made with standardized solutions of antibody and antigen, and a standardized buffer, as known in the art and such as the buffer described herein. In some embodiments, an antibody described herein is a monoclonal antibody. Monoclonal antibodies can be made using recombinant DNA methods, for example, as described in U.S. Patent 4,816,567. The polynucleotides encoding a monoclonal antibody can be amplified from a suitable source or chemically synthetized. The isolated polynucleotides encoding the heavy and light chains are then cloned into suitable expression vectors, which when transfected into host cells such as E. coli cells, simian COS cells, Chinese hamster ovary (CHO) cells, or myeloma cells that do not otherwise produce immunoglobulin protein, monoclonal antibodies are generated by the host cells. The polynucleotide(s) encoding a monoclonal antibody can be modified in a number of different manners using recombinant DNA technology to generate alternative antibodies. In some embodiments, the constant domains of the light and heavy chains can be substituted for a non-immunoglobulin polypeptide to generate a fusion antibody. In some embodiments, the constant regions are truncated or removed to generate the desired antibody fragment of a monoclonal antibody. Site-directed or high-density mutagenesis of the variable region can be used to optimize specificity, affinity, etc. of a monoclonal antibody. Methods for engineering antibodies can also be used and are well-known in the art. An engineered antibody can have one or more amino acid residues substituted, deleted or inserted. These sequence modifications can be used to reduce immunogenicity or reduce, enhance or modify binding, affinity, on-rate, off-rate, avidity, specificity, half-life, or any other suitable characteristic, as known in the art. Antibodies can also be engineered to eliminate development liabilities by altering or eliminating sequence elements targeted for post-translational modification including glycosylation sites, oxidation sites, or deamination sites. In general, the CDR residues are directly and most substantially involved in influencing antibody binding. Accordingly, part or all of the CDR sequences are maintained while the variable framework and constant regions can be engineered by introducing substitutions, insertions, or deletions. Antibodies disclosed herein can also optionally be engineered with retention of high affinity for the antigen and other favorable biological properties. To achieve this goal, engineered antibodies can be prepared by a process of analysis of the parental sequences and various conceptual engineered products using three-dimensional models of the parental and engineered sequences. Three-dimensional immunoglobulin models are commonly available and are familiar to those skilled in the art. Computer programs are available, which illustrate and display probable three-dimensional conformational structures of selected candidate immunoglobulin sequences. Inspection of these displays permits analysis of the likely role of the residues in the functioning of the candidate immunoglobulin sequence, i.e., the analysis of residues that influence the ability of the candidate immunoglobulin to bind its antigen. In this way, framework (FR) residues can be selected and combined from the consensus and import sequences so that the desired antibody characteristic, such as increased affinity for the target antigen(s), is achieved. In certain embodiments an antibody fragment is provided. Various techniques are known for the production of antibody fragments. Traditionally, these fragments are derived via proteolytic digestion of intact antibodies (for example Morimoto et al., 1993, Journal of Biochemical and Biophysical Methods 24:107-117; Brennan et al., 1985, Science, 229:81). In certain embodiments, antibody fragments are produced recombinantly. Fab, Fv, and scFv antibody fragments can all be expressed in and secreted from E. coli or other host cells, thus allowing the production of large amounts of these fragments. Such antibody fragments can also be isolated from antibody phage libraries. The antibody fragment can also be linear antibodies as described in U.S. Patent 5,641,870, for example, and can be monospecific or bispecific. Other techniques for the production of antibody fragments will be apparent to the skilled practitioner. In certain embodiments, the variable domains in both the heavy and light chains are altered by at least partial replacement of one or more CDRs and, if necessary, by partial framework region replacement and sequence changing. Although the CDRs can be derived from an antibody of the same class or even subclass as the antibody from which the framework regions are derived, it is envisaged that the CDRs may be derived from an antibody of different class and in certain embodiments from an antibody from a different species. It may not be necessary to replace all of the CDRs with the complete CDRs from the donor variable region to transfer the antigen-binding capacity of one variable domain to another. Rather, it may only be necessary to transfer those residues that are necessary to maintain the activity of the antigen-binding site. Given the explanations set forth in U.S. Pat. Nos. 5,585,089, 5,693,761 and 5,693,762, it will be well within the competence of those skilled in the art, either by carrying out routine experimentation or by trial and error testing to obtain a functional antibody with reduced immunogenicity. Alterations to the variable region notwithstanding, those skilled in the art will appreciate that the modified antibodies described herein will comprise antibodies (e.g., full-length antibodies or antigen-binding fragments thereof) in which at least a fraction of one or more of the constant region domains has been deleted or otherwise altered so as to provide desired biochemical characteristics such as increased serum half-life when compared with an antibody of approximately the same antigen-binding activity comprising a native or unaltered constant region. In some embodiments, the constant region of the modified antibodies will comprise a human constant region. Modifications to the constant region compatible with this invention comprise additions, deletions or substitutions of one or more amino acids in one or more domains. That is, the modified antibodies described herein can comprise alterations or modifications to one or more of the three heavy chain constant domains (CH1, CH2 or CH3) and/or to the light chain constant domain (CL). In some embodiments, modified constant regions wherein one or more domains are partially or entirely deleted are contemplated. In some embodiments, the modified antibodies will comprise domain deleted constructs or variants wherein the entire CH2 domain has been removed (ΔCH2 constructs). In some embodiments, the omitted constant region domain will be replaced by a short amino acid spacer (e.g., 10 residues) that provides some of the molecular flexibility typically imparted by the absent constant region. It will be noted that in certain embodiments, the modified antibodies can be engineered to fuse the C_H3 domain directly to the hinge region of the respective modified antibodies. In other constructs it may be desirable to provide a peptide spacer between the hinge region and the modified CH2 and/or CH3 domains. For example, compatible constructs could be expressed wherein the CH2 domain has been deleted and the remaining C_H3 domain (modified or unmodified) is joined to the hinge region with a 5-20 amino acid spacer. Such a spacer can be added, for instance, to ensure that the regulatory elements of the constant domain remain free and accessible or that the hinge region remains flexible. However, it should be noted that amino acid spacers can, in some cases, prove to be immunogenic and elicit an unwanted immune response against the construct. Accordingly, in certain embodiments, any spacer added to the construct will be relatively non- immunogenic, or even omitted altogether, so as to maintain the desired biochemical qualities of the modified antibodies. Besides the deletion of whole constant region domains, it will be appreciated that the antibodies described herein can be provided by the partial deletion or substitution of a few or even a single amino acid. For example, it may be desirable to simply delete that part of one or more constant region domains that control the effector function (e.g., complement C1q binding) to be modulated. Such partial deletions of the constant regions can improve selected characteristics of the antibody (serum half-life) while leaving other desirable functions associated with the subject constant region domain intact. Moreover, as alluded to above, the constant regions of the disclosed antibodies can be modified through the mutation or substitution of one or more amino acids that enhances the profile of the resulting construct. In this respect it may be possible to disrupt the activity provided by a conserved binding site (e.g., Fc binding) while substantially maintaining the configuration and immunogenic profile of the modified antibody. Certain embodiments can comprise the addition of one or more amino acids to the constant region to enhance desirable characteristics such as decreasing or increasing effector function or provide for more cytotoxin or carbohydrate attachment. In such embodiments, it can be desirable to insert or replicate specific sequences derived from selected constant region domains. In further embodiments, an antibody disclosed herein comprises a variant IgG Fc region (e.g., variant IgG1 Fc region) comprising the M428L and N434S substitutions to improve the recycling of the antibody via the antibody salvage pathway. See, e.g., Grevys, et al., J. Immunology, 194:5497-508 (2015). The half-life of an IgG is mediated by its pH-dependent binding to the neonatal receptor FcRn. In some embodiments, an antibody described herein comprises a variant Fc region that has been modified to enhance binding to FcRn (see, e.g., Petkova et al., Int. Immunol. 18: 1759-1769 (2006); Dall'Acqua et al., J. Immunol.169: 5171-5180 (2002); Oganesyan et al., Mol. Immunol. 46: 1750-1755 (2009); Dall'Acqua et al., J. Biol. Chem. 281: 23514-23524 (2006), Hinton et al., J. Immunol. 176: 346-356 (2006); Datta-Mannan et al., Drug Metab. Dispos. 35: 86-94 (2007); Datta-Mannan et al., J. Biol. Chem. 282: 1709-1717 (2007); WO 06/130834; Strohl, Curr. Opin. Biotechnol. 20: 685-691 (2009); and Yeung et al., J. Immunol. 182: 7663-7671 (2009), the contents of each of which is herein incorporated by reference in its entirety). In some embodiments, an antibody described herein comprises an Fc region comprising the amino acid sequence of SEQ ID NO: 90. In some embodiments, an antibody described herein comprises a variant Fc region, for example, a variant Fc region comprising the amino acid sequence of SEQ ID NO: 92-102 or 103. In some embodiments, an antibody described herein comprises a variant Fc region comprising the "LS" mutation (see, e.g., SEQ ID NO: 91). In some embodiments, an antibody described herein comprises a variant Fc region comprising the "YTE" mutation (see, e.g., SEQ ID NO: 92). In some embodiments, an antibody described herein comprises a variant Fc region comprising the "LALA" mutation (see, e.g., SEQ ID NO: 99). In some embodiments, an antibody described herein comprises a variant Fc region comprising the "DE" and "LS" mutations (see, e.g., SEQ ID NO: 100). In some embodiments, an antibody described herein comprises a variant Fc region comprising the "DE" and "YTE" mutations (see, e.g., SEQ ID NO: 101). In some embodiments, an antibody described herein comprises a variant Fc region comprising the "DLE" and "LS" mutations (see, e.g., SEQ ID NO: 102). In some embodiments, an antibody described herein comprises a variant Fc region comprising the "DLE" and "YTE" mutations (see, e.g., SEQ ID NO: 103). In some embodiments, an antibody described herein comprises a first variant Fc region comprising a "knob" mutation (see, e.g., SEQ ID NO: 93) and a second variant Fc region comprising a "hole" mutation (see, e.g., SEQ ID NO: 96). In some embodiments, an antibody described herein comprises a first variant Fc region comprising a "knob" mutation and an "LS" mutation (see, e.g., SEQ ID NO: 94) and a second variant Fc region comprising a "hole" mutation and an 'LS" mutation (see, e.g., SEQ ID NO: 97). In some embodiments, an antibody described herein comprises a first variant Fc region comprising a "knob" mutation and an "YTE" mutation (see, e.g., SEQ ID NO: 95) and a second variant Fc region comprising a "hole" mutation and an 'YTE" mutation (see, e.g., SEQ ID NO: 98). In some embodiments, an antibody described herein comprises a variant Fc region that has been modified to have a selective affinity for FcRn at pH 6.0, but not pH 7.4. By way of example, the variant Fc region contains one or more of the following modifications that increase half-life: IgG1-M252Y, S254T, T256E (see, e.g., SEQ ID NO: 92, 95, 97, 101 and 103); IgG1-T250Q, M428L; IgG1-M428L and N434S (the "LS" mutation) (see, e.g., SEQ ID NO: 91, 94, 97, 100 and 102); IgG1-H433K, N434Y; IgG1-N434A; and IgG1-T307A, E380A, N434A; wherein the numbering of the residues is that of the EU index of Kabat et al. (Kabat et al., Sequences of Proteins of Immunological Interest, 1991 Fifth edition, herein incorporated by reference). In some embodiments, an antibody described herein comprises a variant Fc region comprising the "LS" mutation (see, e.g., SEQ ID NO: 91). In some embodiments, an antibody described herein comprises a variant Fc region comprising the "YTE" mutation (see, e.g., SEQ ID NO: 92). In some embodiments, an antibody described herein comprises a first variant Fc region comprising a "knob" mutation and an "LS" mutation (see, e.g., SEQ ID NO: 94) and a second variant Fc region comprising a "hole" mutation and an 'LS" mutation (see, e.g., SEQ ID NO: 97). In some embodiments, an antibody described herein comprises a first variant Fc region comprising a "knob" mutation and an "YTE" mutation (see, e.g., SEQ ID NO: 95) and a second variant Fc region comprising a "hole" mutation and an 'YTE" mutation (see, e.g., SEQ ID NO: 98). In some embodiments, an antibody described herein comprises a variant Fc region that has been modified to reduce its effector functions. In some embodiments, the variant Fc region comprises the L234A, L235A hinge region substitutions (SEQ ID NO: 99), wherein the numbering of the residues is that of the EU index of Kabat et al. In some embodiments, an antibody described herein comprises a variant Fc region comprising the "LALA" mutation (see, e.g., SEQ ID NO: 99). In some embodiments, an antibody described herein comprises an Fc region having a carbohydrate structure that lacks fucose attached (directly or indirectly) to the Fc region or has a reduced level of fucosylation. In some embodiments, a fucosylation variant antibody has improved ADCC function. See, e.g., US Patent Publication Nos. US 2003/0157108; US 2004/0093621, each of which is incorporated by reference herein in its entirety. Examples of publications related to "defucosylated" or "fucose-deficient" antibody variants include: US 2003/0157108; WO 2000/61739; WO 2001/29246; US 2003/0115614; US 2002/0164328; US 2004/0093621; US 2004/0132140; US 2004/0110704; US 2004/0110282; US 2004/0109865; WO 2003/085119; WO 2003/084570; WO 2005/035586; WO 2005/035778; WO2005/053742; WO2002/031140; Okazaki et al. J. Mol. Biol.336:1239-1249 (2004); Yamane-Ohnuki et al. Biotech. Bioeng. 87: 614 (2004), each of which is incorporated by reference herein in its entirety. Examples of cell lines capable of producing defucosylated antibodies include Lec 13 CHO cells deficient in protein fucosylation (Ripka et al. Arch. Biochem. Biophys. 249:533-545 (1986); US Pat Appl No US 2003/0157108 A1; and WO 2004/056312), and knockout cell lines, such as alpha-1,6-fucosyltransferase gene, FUT8, knockout CHO cells (see, e.g., Yamane-Ohnuki et al. Biotech. Bioeng. 87: 614 (2004); Kanda, Y. et al., Biotechnol. Bioeng., 94:680-688 (2006); and WO2003/085107), each of which is incorporated by reference herein in its entirety. In some embodiments, an antibody described herein comprises bisected oligosaccharides, in which a biantennary oligosaccharide attached to the Fc region of the antibody is bisected by GlcNAc. In some embodiment, an antibody comprising bisected oligosaccharides has reduced fucosylation and/or improved ADCC function. See, e.g., WO 2003/011878; U.S. Pat. No. 6,602,684; and US 2005/0123546, each of which is incorporated by reference herein in its entirety. In some embodiment, an antibody described herein comprises at least one galactose residue in the oligosaccharide attached to the Fc region. Such antibody variants may have improved CDC function. See, e.g., in WO 1997/30087; WO 1998/58964; and WO 1999/22764, each of which is incorporated by reference herein in its entirety. In some embodiments, an antibody described herein comprises a variant Fc region comprising a combination of substitutions with increased binding to FcRn and Fc gamma RIIIa. The combinations increase antibody half-life and ADCC. For example, such combination include antibodies with the following amino acid substitution in the Fc region: (1) S239D/I332E and T250Q/M428L; (2) S239D/I332E and M428L/N434S; (3) S239D/I332E and N434A; (4) S239D/I332E and T307A/E380A/N434A; (5) S239D/I332E and M252Y/S254T/T256E; (6) S239D/A330L/I332E and 250Q/M428L; (7) S239D/A330L/I332E and M428L/N434S; (8) S239D/A330L/I332E and N434A; (9) S239D/A330L/I332E and T307A/E380A/N434A; or (10) S239D/A330L/I332E and M252Y/S254T/T256E, wherein the numbering of the residues is that of the EU index of Kabat et al. In some embodiments, an antibody described herein comprises a variant Fc region, for example, a variant Fc region comprising the amino acid sequence of SEQ ID NO: 100-102 or 103. In some embodiments, an antibody comprising the variant Fc region is directly cytotoxic to infected cells, or uses natural defenses such as complement, antibody dependent cellular cytotoxicity (ADCC), or phagocytosis by macrophages. The present invention further embraces variants and equivalents, which are substantially homologous to the chimeric, humanized and human antibodies, or antibody fragments thereof, set forth herein. These can contain, for example, conservative substitution mutations, i.e., the substitution of one or more amino acids by similar amino acids. For example, conservative substitution refers to the substitution of an amino acid with another within the same general class such as, for example, one acidic amino acid with another acidic amino acid, one basic amino acid with another basic amino acid or one neutral amino acid by another neutral amino acid. What is intended by a conservative amino acid substitution is well-known in the art. The polypeptides provided herein can be recombinant polypeptides, natural polypeptides, or synthetic polypeptides comprising an antibody, or fragment thereof. It will be recognized in the art that some amino acid sequences described herein can be varied without significant effect of the structure or function of the protein. Thus, the invention further includes variations of the polypeptides, which show substantial activity or which include regions of an antibody, or fragment thereof, against a human folate receptor protein. Such mutants include deletions, insertions, inversions, repeats, and type substitutions. The polypeptides and analogs can be further modified to contain additional chemical moieties not normally part of the protein. Those derivatized moieties can improve the solubility, the biological half-life or absorption of the protein. The moieties can also reduce or eliminate any desirable side effects of the proteins and the like. An overview for those moieties can be found in REMINGTON'S PHARMACEUTICAL SCIENCES, 21th ed., Mack Publishing Co., Easton, PA (2005). III. Polynucleotides In certain aspects, provided herein are polynucleotides comprising a nucleotide sequence or nucleotide sequences encoding an antibody described herein (e.g., a variable light chain and/or variable heavy chain region) or an antigen-binding fragment thereof and vectors, e.g., vectors comprising such polynucleotides. In some embodiments, the vectors can be used for recombinant expression of an antibody described herein in host cells (e.g., E. coli and mammalian cells). In some embodiments, the vectors can be used for administration of an antibody described herein to a patient in need thereof. In some embodiments, the antibody comprises eN49P7-FRv1-23. In some embodiments, the antibody comprises eN49P7-FRv1-65. In some embodiments, the antibody comprises eN49P7-FRv1-85. In some embodiments, the antibody comprises the Tris 27, Tris 28 or Tris 29 trispecific antibody. In one aspect, provided herein are isolated polynucleotides encoding the heavy chain variable region or heavy chain of an antibody described herein. In one aspect, provided herein are isolated polynucleotides encoding the light chain variable region or light chain of an antibody described herein. In one aspect, provided herein are isolated polynucleotides encoding the heavy chain variable region or heavy chain of an antibody described herein and the light chain variable region or light chain of an antibody described herein. In some embodiments, the polynucleotide encodes eN49P7-FRv1-23. In some embodiments, the polynucleotide encodes eN49P7-FRv1-65. In some embodiments, the polynucleotide encodes eN49P7-FRv1-85. In some embodiments, the polynucleotide encodes a VH or VL as shown in Table 1. In some embodiments, the polynucleotide encodes a polypeptide comprising an amino acid sequence shown in Table 2. In some embodiments, the polynucleotide encodes a polypeptide comprising an amino acid sequence shown in Table 3. In some embodiments, the polynucleotide encodes a polypeptide comprising an amino acid sequence shown in Table 3. In some embodiments, the polynucleotide encodes the Tris 27, Tris 28 or Tris 29 trispecific antibody. In some embodiments, the polynucleotide comprises the nucleotide sequences of SEQ ID NO: 77, 78, 80, 82, or 84. In some embodiments, an isolated polynucleotide described herein encodes an antibody described herein and comprises an mRNA. In some embodiments, the mRNA comprises at least one modified nucleotide. In some embodiments, a modified mRNA encoding an antibody disclosed herein is for administering to a subject to treat or prevent HIV infection. As used herein, an "isolated" polynucleotide or nucleic acid molecule is one, which is separated from other nucleic acid molecules, which are present in the natural source (e.g., in a mouse or a human) of the nucleic acid molecule. Moreover, an "isolated" nucleic acid molecule, such as a cDNA molecule, can be substantially free of other cellular material, or culture medium when produced by recombinant techniques, or substantially free of chemical precursors or other chemicals when chemically synthesized. For example, the language "substantially free" includes preparations of polynucleotide or nucleic acid molecule having less than about 15%, 10%, 5%, 2%, 1%, 0.5%, or 0.1% (in particular less than about 10%) of other material, e.g., cellular material, culture medium, other nucleic acid molecules, chemical precursors and/or other chemicals. In a specific embodiment, a nucleic acid molecule(s) encoding an antibody or fusion polypeptide described herein is isolated or purified. In particular aspects, provided herein are polynucleotides comprising nucleotide sequences encoding antibodies described herein, as well as antibodies that compete with such antibodies for binding to HIV, or which binds to the same epitope as that of such antibodies. In certain aspects, provided herein are polynucleotides comprising a nucleotide sequence encoding the light chain or heavy chain of an antibody described herein. The polynucleotides can comprise nucleotide sequences encoding a light chain comprising the VL of antibodies described herein (see, e.g., Table 1). The polynucleotides can comprise nucleotide sequences encoding a heavy chain comprising the VH of antibodies described herein (see, e.g., Table 1). In specific embodiments, a polynucleotide described herein encodes a VH domain shown in Table 1. In specific embodiments, a polynucleotide described herein encodes a VL domain shown in Table 1. In some embodiments, a polynucleotide described herein encodes eN49P7-FRv1-23. In some embodiments, a polynucleotide described herein encodes eN49P7-FRv1-65. In some embodiments, a polynucleotide described herein encodes eN49P7-FRv1-85. In some embodiments, the antibody is a chimeric antibody. In particular embodiments, provided herein are polynucleotides comprising a nucleotide sequence encoding an antibody comprising three VL chain CDRs, e.g., containing VL CDR1, VL CDR2, and VL CDR3 of any one of antibodies described herein (e.g., see Table 2). In specific embodiments, provided herein are polynucleotides comprising three VH chain CDRs, e.g., containing VH CDR1, VH CDR2, and VH CDR3 of any one of antibodies described herein (e.g., see Table 2). In specific embodiments, provided herein are polynucleotides comprising a nucleotide sequence encoding an anti- Env antibody comprising three VL CDRs, e.g., containing VL CDR1, VL CDR2, and VL CDR3 of any one of antibodies described herein (e.g., see Table 2) and three VH chain CDRs, e.g., containing VH CDR1, VH CDR2, and VH CDR3 of any one of antibodies described herein (e.g., see Table 2). In specific aspects, provided herein is a polynucleotide comprising a nucleotide sequence encoding an antibody comprising a light chain and a heavy chain, e.g., a separate light chain and heavy chain. With respect to the light chain, in a specific embodiment, a polynucleotide provided herein comprises a nucleotide sequence encoding a kappa light chain. In another specific embodiment, a polynucleotide provided herein comprises a nucleotide sequence encoding a lambda light chain. In yet another specific embodiment, a polynucleotide provided herein comprises a nucleotide sequence encoding an antibody described herein comprising a human kappa light chain or a human lambda light chain. In a particular embodiment, a polynucleotide provided herein comprises a nucleotide sequence encoding an antibody, which immunospecifically binds to Env, wherein the antibody comprises a light chain, and wherein the amino acid sequence of the VL domain can comprise the amino acid sequence set forth in Table 1, and wherein the constant region of the light chain comprises the amino acid sequence of a human kappa light chain constant region. In another particular embodiment, a polynucleotide provided herein comprises a nucleotide sequence encoding an antibody, which immunospecifically binds to Env, and comprises a light chain, wherein the amino acid sequence of the VL domain can comprise the amino acid sequence set forth in Table 1, and wherein the constant region of the light chain comprises the amino acid sequence of a human lambda light chain constant region. For example, human constant region sequences can be those described in U.S. Patent No. 5,693,780. In a particular embodiment, a polynucleotide provided herein comprises a nucleotide sequence encoding an antibody described herein, which immunospecifically binds to Env, wherein the antibody comprises a heavy chain, wherein the amino acid sequence of the VH domain can comprise the amino acid sequence set forth in Table 1, and wherein the constant region of the heavy chain comprises the amino acid sequence of a human alpha or gamma heavy chain constant region. In yet another specific embodiment, a polynucleotide provided herein comprises a nucleotide sequence encoding an antibody described herein, which immunospecifically binds Env, wherein the antibody comprises a VL domain and a VH domain comprising any amino acid sequences described herein, and wherein the constant regions comprise the amino acid sequences of the constant regions of a human IgA₁, human IgA₂, human IgG₁ (e.g., allotype 1, 17, or 3), human IgG2, or human IgG4. In yet another specific embodiment, a polynucleotide provided herein comprises a nucleotide sequences encoding an anti-Env antibody or a fragment thereof that are optimized, e.g., by codon/RNA optimization, replacement with heterologous signal sequences, and elimination of mRNA instability elements. Methods to generate optimized nucleic acids encoding an anti-Env antibody or a fragment thereof (e.g., light chain, heavy chain, VH domain, or VL domain) for recombinant expression by introducing codon changes and/or eliminating inhibitory regions in the mRNA can be carried out by adapting the optimization methods described in, e.g., U.S. Patent Nos. 5,965,726; 6,174,666; 6,291,664; 6,414,132; and 6,794,498, accordingly. For example, potential splice sites and instability elements (e.g., A/T or A/U rich elements) within the RNA can be mutated without altering the amino acids encoded by the nucleic acid sequences to increase stability of the RNA for recombinant expression. The alterations utilize the degeneracy of the genetic code, e.g., using an alternative codon for an identical amino acid. In some embodiments, it can be desirable to alter one or more codons to encode a conservative mutation, e.g., a similar amino acid with similar chemical structure and properties and/or function as the original amino acid. In certain embodiments, an optimized polynucleotide sequence encoding an anti- Env antibody described herein or a fragment thereof (e.g., VL domain or VH domain) can hybridize to an antisense (e.g., complementary) polynucleotide of an unoptimized polynucleotide sequence encoding an anti-Env antibody described herein or a fragment thereof (e.g., VL domain or VH domain). In specific embodiments, an optimized nucleotide sequence encoding an anti-Env antibody described herein or a fragment hybridizes under high stringency conditions to antisense polynucleotide of an unoptimized polynucleotide sequence encoding an anti-Env antibody described herein or a fragment thereof. In a specific embodiment, an optimized nucleotide sequence encoding an anti-Env antibody described herein or a fragment thereof hybridizes under high stringency, intermediate or lower stringency hybridization conditions to an antisense polynucleotide of an unoptimized nucleotide sequence encoding an anti-Env antibody described herein or a fragment thereof. Information regarding hybridization conditions has been described, see, e.g., U.S. Patent Application Publication No. US 2005/0048549 (e.g., paragraphs 72-73), which is incorporated herein by reference. The polynucleotides can be obtained, and the nucleotide sequence of the polynucleotides determined, by any method known in the art. Nucleotide sequences encoding antibodies described herein, and modified versions of these antibodies can be determined using methods well-known in the art, i.e., nucleotide codons known to encode particular amino acids are assembled in such a way to generate a nucleic acid that encodes the antibody. Such a polynucleotide encoding the antibody can be assembled from chemically synthesized oligonucleotides (e.g., as described in Kutmeier G et al., (1994), BioTechniques 17: 242-246), which, briefly, involves the synthesis of overlapping oligonucleotides containing portions of the sequence encoding the antibody, annealing and ligating of those oligonucleotides, and then amplification of the ligated oligonucleotides by PCR. Alternatively, a polynucleotide encoding an antibody or fragment thereof described herein can be generated from nucleic acid from a suitable source (e.g., PBMCs) using methods well-known in the art (e.g., PCR and other molecular cloning methods). For example, PCR amplification using synthetic primers hybridizable to the 3' and 5' ends of a known sequence can be performed using genomic DNA obtained from hybridoma cells producing the antibody of interest. Such PCR amplification methods can be used to obtain nucleic acids comprising the sequence encoding the light chain and/or heavy chain of an antibody. Such PCR amplification methods can be used to obtain nucleic acids comprising the sequence encoding the variable light chain region and/or the variable heavy chain region of an antibody. The amplified nucleic acids can be cloned into vectors for expression in host cells and for further cloning, for example, to generate chimeric and humanized antibodies. If a clone containing a nucleic acid encoding a particular antibody or fragment thereof is not available, but the sequence of the antibody molecule or fragment thereof is known, a nucleic acid encoding the immunoglobulin or fragment can be chemically synthesized or obtained from a suitable source (e.g., an antibody cDNA library or a cDNA library generated from, or nucleic acid, preferably poly A+ RNA, isolated from, any tissue or cells expressing the antibody, such as hybridoma cells selected to express an antibody described herein) by PCR amplification using synthetic primers hybridizable to the 3' and 5' ends of the sequence or by cloning using an oligonucleotide probe specific for the particular gene sequence to identify, e.g., a cDNA clone from a cDNA library that encodes the antibody. Amplified nucleic acids generated by PCR can then be cloned into replicable cloning vectors using any method well-known in the art. DNA encoding anti-Env antibodies described herein can be readily isolated and sequenced using conventional procedures (e.g., by using oligonucleotide probes that are capable of binding specifically to genes encoding the heavy and light chains of the anti- Env antibodies). PBMCs can serve as a source of such DNA. Once isolated, the DNA can be placed into expression vectors, which are then transfected into host cells such as E. coli cells, simian COS cells, Chinese hamster ovary (CHO) cells (e.g., CHO cells from the CHO GS System™ (Lonza)), or myeloma cells that do not otherwise produce immunoglobulin protein, to obtain the synthesis of anti-Env antibodies in the recombinant host cells. The DNA also can be modified, for example, by substituting the coding sequence for human heavy and light chain constant domains with a coding sequence for a non- immunoglobulin polypeptide, or by covalently joining to the immunoglobulin coding sequence all or part of the coding sequence for a non-immunoglobulin polypeptide. Also provided are polynucleotides that hybridize under high stringency, intermediate or lower stringency hybridization conditions to polynucleotides that encode an antibody described herein. In specific embodiments, polynucleotides described herein hybridize under high stringency, intermediate or lower stringency hybridization conditions to polynucleotides encoding a VH domain and/or VL domain provided herein. Hybridization conditions have been described in the art and are known to one of skill in the art. For example, hybridization under stringent conditions can involve hybridization to filter-bound DNA in 6x sodium chloride/sodium citrate (SSC) at about 45°C followed by one or more washes in 0.2xSSC/0.1% SDS at about 50-65°C; hybridization under highly stringent conditions can involve hybridization to filter-bound nucleic acid in 6xSSC at about 45°C followed by one or more washes in 0.1xSSC/0.2% SDS at about 68°C. Hybridization under other stringent hybridization conditions are known to those of skill in the art and have been described, see, for example, Ausubel FM et al., eds., (1989) Current Protocols in Molecular Biology, Vol. I, Green Publishing Associates, Inc. and John Wiley & Sons, Inc., New York at pages 6.3.1-6.3.6 and 2.10.3. IV. Vectors, Cells, and Methods of Producing a Broadly Neutralizing Agent In certain aspects, provided herein are cells (e.g., host cells) expressing (e.g., recombinantly) antibodies described herein, which specifically bind to Env and related polynucleotides and expression vectors. Provided herein are vectors (e.g., expression vectors) comprising polynucleotides comprising nucleotide sequences encoding anti-Env antibodies or a fragment thereof described herein. In some embodiments, the vectors can be used for recombinant expression of an antibody described herein in host cells (e.g., mammalian cells). In some embodiments, the vectors can be used for administration of an antibody described herein to a patient in need thereof. Also provided herein are host cells comprising such vectors for recombinantly expressing anti-Env antibodies described herein. In a particular aspect, provided herein are methods for producing an antibody described herein, comprising expressing such antibody in a host cell. In some embodiments, the antibody comprises eN49P7-FRv1-23. In some embodiments, the antibody comprises eN49P7-FRv1-65. In some embodiments, the antibody comprises eN49P7-FRv1-85. In some embodiments, the antibody comprises the Tris 27, Tris 28 or Tris 29 trispecific antibody. In certain aspects, provided herein is an isolated vector comprising a polynucleotide described herein. In some embodiments, the vector is a viral vector. In certain aspects, provided herein is a recombinant virus comprising a polynucleotide described herein. In some embodiments, the recombinant virus encodes an antibody described herein. In some embodiments, the recombinant virus encodes a bispecific antibody described herein. In some embodiments, the recombinant virus is a replication defective virus. Suitable replication defective viral vectors are known to those skilled in the art, for example, as disclosed in U.S. Pat. Nos. 7198784, 9408905, 9862931, 8067156, U.S. Pat. Appl. Pub. Nos. 20150291935, 20120220492, 20180291351, and 20170175137, each of which is incorporated herein by reference in its entirety. In some embodiments, the recombinant virus is a retrovirus or retroviral vector, for example, a lentivirus or lentiviral vector. In some embodiments, the recombinant virus is an adenovirus or adenoviral vector, HSV or HSV vector, or influenza virus or viral vector. In some embodiments, the recombinant virus is an adeno-associated virus (AAV). In some embodiments, the recombinant virus is for administration to a subject to prevent or treat HIV infection. In some embodiments, the recombinant virus is an adeno-associated virus (AAV) for administration to a subject to prevent or treat HIV infection. Recombinant AAV particles encoding an antibody that binds to HIV Env and methods for producing thereof are known to one skilled in the art, for example, as disclosed in US Patent 8,865,881 and US20190031740, each of which is incorporated by reference herein in its entirety for all purposes. See also, Lin and Balazs, Retrovirology 15:66 (2018) and van den Berg et al., Molecular Therapy: Methods & Clinical Development 14:100-112 (2019), each of which is incorporated by reference herein in its entirety for all purposes. In some embodiments, the antibody comprises eN49P7-FRv1-23. In some embodiments, the antibody comprises eN49P7-FRv1-65. In some embodiments, the antibody comprises eN49P7-FRv1-85. In some embodiments, the antibody comprises the Tris 27, Tris 28 or Tris 29 trispecific antibody. In certain aspects, provided herein is a host cell comprising a polynucleotide described herein, or a vector described herein. In some embodiments, the vector encodes an antibody described herein. In some embodiments, a vector described herein comprises a first vector encoding a VH described herein and a second vector encoding a VL described herein. In some embodiments, a vector described herein comprises a first nucleotide sequence encoding a VH described herein and a second nucleotide sequence encoding a VL described herein. In some embodiments, the antibody comprises eN49P7-FRv1-23. In some embodiments, the antibody comprises eN49P7-FRv1-65. In some embodiments, the antibody comprises eN49P7-FRv1-85. In some embodiments, the vector encodes a trispecific antibody described herein. In some embodiments, a vector described herein comprises a first, second and third vector encoding the first, second and third polypeptide chain of a trisepcific antibody described herein. In some embodiments, a vector described herein comprises a first, second, and third nucleotide sequence encoding he first, second and third polypeptide chain of a trisepcific antibody described herein. In some embodiments, the antibody comprises the Tris 27, Tris 28 or Tris 29 trispecific antibody. In some embodiments, the host cell is selected from the group consisting of E. coli, Pseudomonas, Bacillus, Streptomyces, yeast, CHO, YB/20, NS0, PER-C6, HEK-293T, NIH-3T3, Helga, BHK, Hep G2, SP2/0, R1.1, B-W, L-M, COS 1, COS 7, BSC1, BSC40, BMT10 cell, plant cell, insect cell, and human cell in tissue culture. In some embodiments, the host cell is CHO. In certain aspects, provided herein is a method of producing an antibody that binds to HIV comprising culturing a host cell described herein so that the polynucleotide is expressed and the antibody is produced. In some embodiments, the method further comprises recovering the antibody. The isolated polypeptides, i.e., anti-HIV Env antibodies described herein can be produced by any suitable method known in the art. Such methods range from direct protein synthetic methods to constructing a DNA sequence encoding isolated polypeptide sequences and expressing those sequences in a suitable transformed host. In some embodiments, a DNA sequence is constructed using recombinant technology by isolating or synthesizing a DNA sequence encoding a wild-type protein of interest. Optionally, the sequence can be mutagenized by site-specific mutagenesis to provide functional analogs thereof. See, e.g. Zoeller et al., Proc. Nat'l. Acad. Sci. USA 81:5662-5066 (1984) and U.S. Pat. No. 4,588,585. Methods known in the art for purifying antibodies and other proteins also include, for example, those described in U.S. Patent Publication Nos. 2008/0312425, 2008/0177048, and 2009/0187005, each of which is hereby incorporated by reference herein in its entirety. V. Pharmaceutical Compositions Compositions comprising the antibodies or antigen-binding fragments described herein (e.g., eN49P7-FRv1-23, eN49P7-FRv1-65 or eN49P7-FRv1-85) are also provided. Further provided herein are compositions comprising a polynucleotide or polynucleotides encoding the antibodies or antigen-binding fragments described herein. In some embodiments, the polynucleotide comprises mRNA. In some embodiments, the composition is a pharmaceutical composition. In some embodiments, the antibody comprises eN49P7-FRv1-23. In some embodiments, the antibody comprises eN49P7- FRv1-65. In some embodiments, the antibody comprises eN49P7-FRv1-85. In some embodiments, the antibody comprises the Tris 27, Tris 28 or Tris 29 trispecific antibody. In some embodiments, the composition is a lyophilized composition. In some embodiments, the composition is formulated for topical administration, and in certain embodiments the composition is formulated for vaginal or rectal administration. In certain aspects, provided herein is a pharmaceutical composition comprising an antibody described herein (e.g., eN49P7-FRv1-23, eN49P7-FRv1-65 or eN49P7-FRv1-85) and a pharmaceutically acceptable excipient. In some embodiments, the antibody is an intact antibody. In some embodiments, the antibody is an antigen-binding antibody fragment. In some embodiments, the composition is formulated for topical administration, and in certain embodiments the composition is formulated for vaginal or rectal administration. In some embodiments, the antibody comprises eN49P7-FRv1-23. In some embodiments, the antibody comprises eN49P7-FRv1-65. In some embodiments, the antibody comprises eN49P7-FRv1-85. In some embodiments, the antibody comprises the Tris 27, Tris 28 or Tris 29 trispecific antibody. In another embodiment, the disclosure provides a pharmaceutical composition comprising an antibody described herein (e.g., eN49P7-FRv1-23, eN49P7-FRv1-65 or eN49P7-FRv1-85). Such compositions are intended for prevention and treatment of HIV infection. In some embodiments, the antibody comprises eN49P7-FRv1-23. In some embodiments, the antibody comprises eN49P7-FRv1-65. In some embodiments, the antibody comprises eN49P7-FRv1-85. In some embodiments, the antibody comprises the Tris 27, Tris 28 or Tris 29 trispecific antibody. In further embodiments of the present disclosure, a composition comprising the antibody described herein can additionally be combined with other compositions for the treatment of HIV infection or the prevention of HIV transmission. In some embodiments, an antibody described herein may be administered within a pharmaceutically acceptable diluent, carrier, or excipient, in unit dose form. Conventional pharmaceutical practice may be employed to provide suitable formulations or compositions to administer to individuals being treated for HIV infection. In some embodiments, the administration is prophylactic. Any appropriate route of administration may be employed, for example, administration may be parenteral, intravenous, intra-arterial, subcutaneous, intramuscular, intraperitoneal, intranasal, aerosol, suppository, oral administration, vaginal, or anal. The pharmaceutical compositions described herein are prepared in a manner known per se, for example, by means of conventional dissolving, lyophilizing, mixing, granulating or confectioning processes. The pharmaceutical compositions may be formulated according to conventional pharmaceutical practice (see for example, in Remington: The Science and Practice of Pharmacy (21st ed.), ed. A.R. Gennaro, 2005, Lippincott Williams & Wilkins, Philadelphia, PA, and Encyclopedia of Pharmaceutical Technology, eds. J. Swarbrick and J. C. Boylan, 2013, Marcel Dekker, New York, NY). The injection compositions are prepared in customary manner under sterile conditions; the same applies also to introducing the compositions into ampoules or vials and sealing the containers. Pharmaceutical compositions according to the invention may be, for example, in unit dose form, such as in the form of ampoules, vials, suppositories, tablets, pills, or capsules. The formulations can be administered to human individuals in therapeutically or prophylactic effective amounts (e.g., amounts which prevent, eliminate, or reduce a pathological condition) to provide therapy for a disease or condition. The preferred dosage of therapeutic agent to be administered is likely to depend on such variables as the type and extent of the disorder, the overall health status of the particular patient, the formulation of the compound excipients, and its route of administration. In certain embodiments, the compositions described herein can be formulated for topical administration, and in certain embodiments the composition is formulated for vaginal or rectal administration. The composition may be formulated as a gel, or formulated as a topical cream, ointment, lotion or foam formulation. Useful formulations are known in the art, for example, as disclosed in U.S. Patent Appl. Pub. No. 20130022619, which is incorporated by reference herein in its entirety for all purposes. In certain embodiments, the composition may further comprise a pharmaceutically acceptable excipient, a lubricant, or an antiviral agent. The topical formulations of the present invention can be used to prevent HIV infection in a human, or to inhibit transmission of the HIV virus from an infected human to another human. The topical formulations of the present invention can inhibit the growth or replication of HIV. The topical formulations are useful in the prophylactic treatment of humans who are at risk for HIV infection. The topical formulations also can be used to treat objects or materials, such as contraceptive devices (for example condoms or intrauterine devices), medical equipment, supplies, or fluids, including biological fluids, such as blood, blood products, and tissues, to prevent or inhibit viral infection of a human. Such topical formulations also are useful to prevent transmission, such as sexual transmission of viral infections, e.g., HIV, which is the primary way in which HIV is transmitted globally. The methods of prevention or inhibition or retardation of transmission of viral infection, e.g., HIV infection, in accordance with the present invention, comprise vaginal, rectal, penile or other topical treatment with an antiviral effective amount of a topical preparation of the present invention, alone or in combination with another antiviral compound as described herein. In some embodiments, the composition is in the form of a cream, lotion, gel, or foam that is applied to the affected skin or epithelial cavity, and preferably spread over the entire skin or epithelial surface which is at risk of contact with bodily fluids. Such formulations, which are suitable for vaginal or rectal administration, may be present as aqueous or oily suspensions, solutions or emulsions (liquid formulations) containing in addition to the active ingredient, such carriers as are known in the art to be appropriate. These formulations are useful to protect not only against sexual transmission of HIV, but also to prevent infection of a baby during passage through the birth canal. Thus the vaginal administration can take place prior to sexual intercourse, during sexual intercourse, and immediately prior to childbirth. As a vaginal formulation, the active ingredient may be used in conjunction with a spermicide and may be employed with a condom, diaphragm, sponge or other contraceptive device. Examples of suitable spermicides include nonylphenoxypolyoxyethylene glycol (nonoxynol 9), benzethonium chloride, and chlorindanol. Suitably, the pH of the composition is 4.5 to 8.5. Vaginal compositions preferably have a pH of 4.5 to 6, most preferably about 5. Vaginal formulations include suppositories (for example, gel-covered creams), tablets and films. The suppositories can be administered by insertion with an applicator using methods well-known in the art. Vaginal formulations further include vaginal ring devices formulated for sustained release. See, e.g., Morrow et al., Eur J Pharm Biopharm. 77:3-10 (2011), Zhao et al., Antimicrob Agents Chemother. 61:pii: e02465-16 (2017). Buccal formulations include creams, ointments, gels, tablets or films that comprise ingredients that are safe when administered via the mouth cavity. Buccal formulations can also comprise a taste-masking or flavoring agent. The present compositions may be associated with a contraceptive device or article, such as a vaginal ring device, an intrauterine device (IUD), vaginal diaphragm, vaginal sponge, pessary, condom, etc. In some embodiments, the compositions described herein are used in conjunction with condoms, to enhance the risk-reducing effectiveness of condoms and provide maximum protection for users. The composition can either be coated onto condoms during manufacture, and enclosed within conventional watertight plastic or foil packages that contain one condom per package, or it can be manually applied by a user to either the inside or the outside of a condom, immediately before use. As used herein, "condom" refers to a barrier device, which is used to provide a watertight physical barrier between male and female genitalia during sexual intercourse, and which is removed after intercourse. This term includes conventional condoms that cover the penis; it also includes so-called "female condoms", which are inserted into the vaginal cavity prior to intercourse. In another embodiment, a composition described herein is in the form of an intra- vaginal pill, an intra-rectal pill, or a suppository. The suppository or pill should be inserted into the vaginal or rectal cavity in a manner that permits the suppository or pill, as it dissolves or erodes, to coat the vaginal or rectal walls with a prophylactic layer of an antibody described herein. In certain embodiments, the composition may further comprise a pharmaceutically acceptable excipient, a lubricant, or an antiviral agent. Compositions used in the methods of this invention may also comprise other active agents, such as another agent to prevent HIV infection, and agents that protect individuals from conception and other sexually transmitted diseases. Thus, in another embodiment the compositions used in this invention further comprise a second anti-HIV agent, a virucide effective against viral infections other than HIV, and/or a spermicide. The compositions used in this invention may also contain a lubricant that facilitates application of the composition to the desired areas of skin and epithelial tissue, and reduces friction during sexual intercourse. In the case of a pill or suppository, the lubricant can be applied to the exterior of the dosage form to facilitate insertion. In the cream or ointment embodiments of the present invention, the topical formulation comprises one or more lubricants. The gels and foams of the present invention optionally can include one or more lubricants. Non-limiting examples of useful lubricants include cetyl esters wax, hydrogenated vegetable oil, magnesium stearate, methyl stearate, mineral oil, polyoxyethylene- polyoxypropylene copolymer, polyethylene glycol, polyvinyl alcohol, sodium lauryl sulfate, white wax, or mixtures of two or more of the above. The gel formulations of the present invention comprise one or more gelling agents. Non-limiting examples of useful gelling agents include carboxylic acid polymers including acrylic acid polymers crosslinked with cross links such as allyl ethers of sucrose (e.g. carbomer brand thickeners), cetostearyl alcohol, hydroxymethyl cellulose, polyoxyethylene-polyoxypropylene copolymer, sodium carboxymethylcellulose, polyvinyl pyrrolidone, or mixtures of two or more thereof. VI. Therapeutic Uses and Methods In one aspect, provided herein is a method of treating HIV or inhibiting transmission of HIV. In some embodiments, the method of inhibiting transmission of HIV comprises administering to a subject in need thereof an effective amount of an antibody described herein (e.g., eN49P7-FRv1-23, eN49P7-FRv1-65 or eN49P7-FRv1-85), a pharmaceutical composition described herein, an isolated polynucleotide described herein, or a recombinant virus (e.g., recombinant AAV) described herein. In some embodiments, the method of inhibiting transmission of HIV comprises administering to a subject in need thereof an effective amount of an antibody (e.g., a bispecific antibody) described herein. In some embodiments, the method of inhibiting transmission of HIV comprises administering to a subject in need thereof an effective amount of a recombinant AAV encoding an antibody (e.g., a bispecific antibody) described herein. In some embodiments, the method of inhibiting transmission of HIV comprises administering to a subject in need thereof an effective amount of an antibody described herein (e.g., eN49P7-FRv1-23, eN49P7-FRv1-65 or eN49P7-FRv1-85). In some embodiments, the subject has been exposed to HIV. In some embodiments, the subject is at risk of being exposed to HIV. In some embodiments, the subject at risk of being exposed to HIV is a health care worker, a sexual partner of an HIV infected individual, or a sex worker. In some embodiments, the subject that has been exposed to HIV or is at risk of being exposed to HIV is a newborn. In some embodiments, the antibody comprises eN49P7-FRv1-23. In some embodiments, the antibody comprises eN49P7-FRv1-65. In some embodiments, the antibody comprises eN49P7-FRv1-85. In some embodiments, the antibody comprises the Tris 27, Tris 28 or Tris 29 trispecific antibody. In one aspect, provided herein is a method of reducing the risk of a subject becoming infected with HIV comprising administering to the subject in need thereof an effective amount of an antibody (e.g., bispecific antibody) described herein (e.g., eN49P7- FRv1-23, eN49P7-FRv1-65 or eN49P7-FRv1-85), a pharmaceutical composition described herein, an isolated polynucleotide described herein, or a recombinant virus described herein. In some embodiments, the method comprises administering to a subject in need thereof an effective amount of an antibody (e.g., a bispecific antibody) described herein. In some embodiments, the method comprises administering to a subject in need thereof an effective amount of a recombinant AAV encoding an antibody (e.g., a bispecific antibody) described herein. In some embodiments, the subject has been exposed to HIV. In some embodiments, the subject is at risk of being exposed to HIV. In some embodiments, the subject at risk of being exposed to HIV is a health care worker, a sexual partner of an HIV infected individual, or a sex worker. In some embodiments, the subject that has been exposed to HIV or is at risk of being exposed to HIV is a newborn. In one aspect, provided herein is an antibody (e.g., eN49P7-FRv1-23, eN49P7-FRv1-65 or eN49P7-FRv1-85), a pharmaceutical composition, an isolated polynucleotide, or a recombinant virus for reducing the risk of a subject becoming infected with HIV. In some embodiments, the antibody comprises eN49P7-FRv1-23. In some embodiments, the antibody comprises eN49P7-FRv1-65. In some embodiments, the antibody comprises eN49P7-FRv1-85. In some embodiments, the antibody comprises the Tris 27, Tris 28 or Tris 29 trispecific antibody. In one aspect, provided herein is a method for passively immunizing a subject comprising administering to the subject in need thereof an effective amount of an antibody described herein (e.g., eN49P7-FRv1-23, eN49P7-FRv1-65 or eN49P7-FRv1-85), a pharmaceutical composition described herein, an isolated polynucleotide described herein, or a recombinant virus described herein. In some embodiments, the method comprises administering to a subject in need thereof an effective amount of an antibody (e.g., a bispecific antibody) described herein. In some embodiments, the method comprises administering to a subject in need thereof an effective amount of a recombinant AAV encoding an antibody (e.g., a bispecific antibody) described herein. In some embodiments, the subject has been exposed to HIV. In some embodiments, the subject is at risk of being exposed to HIV. In some embodiments, the subject at risk of being exposed to HIV is a health care worker, a sexual partner of an HIV infected individual, or a sex worker. In some embodiments, the subject that has been exposed to HIV or is at risk of being exposed to HIV is a newborn. In one aspect, provided herein is an antibody (e.g., eN49P7-FRv1-23, eN49P7-FRv1-65 or eN49P7-FRv1-85), a pharmaceutical composition, an isolated polynucleotide, or a recombinant virus for passively immunizing a subject. In some embodiments, the antibody comprises eN49P7-FRv1-23. In some embodiments, the antibody comprises eN49P7-FRv1-65. In some embodiments, the antibody comprises eN49P7-FRv1-85. In some embodiments, the antibody comprises the Tris 27, Tris 28 or Tris 29 trispecific antibody. Further provided herein is a method of neutralizing an HIV virus comprising contacting the virus with an effective amount of an antibody described herein (e.g., eN49P7-FRv1-23, eN49P7-FRv1-65 or eN49P7-FRv1-85). In some embodiments, the virus is comprised by a composition, for example, a fluid, including a biological fluid, such as blood or blood product. In certain embodiments, the method comprises adding an antibody described herein to a composition comprising HIV in a sufficient amount or concentration to neutralize the HIV. In some embodiments, the antibody comprises eN49P7-FRv1-23. In some embodiments, the antibody comprises eN49P7-FRv1-65. In some embodiments, the antibody comprises eN49P7-FRv1-85. In some embodiments, the antibody comprises the Tris 27, Tris 28 or Tris 29 trispecific antibody. Further provided herein is a method of reducing viral load comprising administering to a subject in need thereof an effective amount of an antibody (e.g., bispecific antibody) described herein (e.g., eN49P7-FRv1-23, eN49P7-FRv1-65 or eN49P7-FRv1-85), a pharmaceutical composition described herein, an isolated polynucleotide described herein, or a recombinant virus described herein. In some embodiments, the method comprises administering to a subject in need thereof an effective amount of an antibody (e.g., a bispecific antibody) described herein. In some embodiments, the method comprises administering to a subject in need thereof an effective amount of a recombinant AAV encoding an antibody (e.g., a bispecific antibody) described herein. In some embodiments, the antibody comprises eN49P7-FRv1-23. In some embodiments, the antibody comprises eN49P7-FRv1-65. In some embodiments, the antibody comprises eN49P7-FRv1-85. In some embodiments, the antibody comprises the Tris 27, Tris 28 or Tris 29 trispecific antibody. In some embodiments of a method described herein, the antibody can be a chimeric antibody, engineered antibody, recombinant antibody, or a monoclonal antibody described herein. In some embodiments, the antibody is a full antibody, an Fab fragment, or an F(ab')2 fragment described herein. In a specific embodiment, the antibody is an engineered monoclonal antibody described herein. In a specific embodiment, the antibody is a recombinant monoclonal antibody described herein. In a specific embodiment, the antibody is a chimeric monoclonal antibody described herein. In a specific embodiment, the antibody is an Fab described herein. In a specific embodiment, the antibody is a F(ab')₂ fragment described herein. In some embodiments, a method of preventing HIV infection provided herein comprises administering to a subject in need thereof a therapeutically sufficient amount of an antibody described herein (e.g., eN49P7-FRv1-23, eN49P7-FRv1-65 or eN49P7-FRv1- 85), a pharmaceutical composition described herein, an isolated polynucleotide described herein, or a recombinant virus described herein. In some embodiments, the antibody comprises eN49P7-FRv1-23. In some embodiments, the antibody comprises eN49P7- FRv1-65. In some embodiments, the antibody comprises eN49P7-FRv1-85. In some embodiments, the antibody comprises the Tris 27, Tris 28 or Tris 29 trispecific antibody. In some embodiments, a method of treating HIV/AIDS provided herein comprises administering to a subject in need thereof a therapeutically sufficient amount of an antibody described herein (e.g., eN49P7-FRv1-23, eN49P7-FRv1-65 or eN49P7-FRv1-85), a pharmaceutical composition described herein, an isolated polynucleotide described herein, or a recombinant virus described herein. In some embodiments, a method of treating HIV/AIDS comprises administering an antibody described herein. In some embodiments, a method of treating HIV/AIDS comprises administering a pharmaceutical composition described herein. In some embodiments, a method of treating HIV/AIDS comprises administering an isolated polynucleotide described herein. In some embodiments, a method of treating HIV/AIDS comprises administering a recombinant virus described herein. In one aspect, provided herein is an antibody, a pharmaceutical composition, an isolated polynucleotide, or a recombinant virus for treating HIV/AIDS. In some embodiments, the antibody comprises eN49P7-FRv1-23. In some embodiments, the antibody comprises eN49P7-FRv1-65. In some embodiments, the antibody comprises eN49P7-FRv1-85. In some embodiments, the antibody comprises the Tris 27, Tris 28 or Tris 29 trispecific antibody. In some embodiments, the administering to the subject is by at least one mode selected from oral, parenteral, subcutaneous, intramuscular, intravenous, vaginal, rectal, buccal, sublingual, and transdermal In some embodiments, a method of treatment described herein further comprises administering at least one additional therapeutic agent. In some embodiments, the additional therapeutic agent comprises an antiretroviral therapy (ART) agent, a reservoir activator, an immunomodulator, a second antibody, or a second and third antibody. In some embodiments, the additional therapeutic agent comprises a second antibody. In some embodiments, the additional therapeutic agent comprises a second and third antibody. In some embodiments, the additional therapeutic agent comprises a second and optionally third antibody, which is an anti-HIV antibody. In some embodiments, the additional therapeutic agent comprises a second and optionally third antibody, which is an anti-HIV Env antibody. In some embodiments, the additional therapeutic agent comprises a second and optionally third anti-HIV Env antibody, which binds to an HIV Env epitope region different from the HIV Env epitope region bound by an antibody disclosed herein. In some embodiments, the additional therapeutic agent comprises a second and optionally third anti-HIV Env antibody, which binds to the CD4 binding site (CD4bs), V2 apex, N332/V3 base supersite, silent face, gp120-gp41 interface or membrane-proximal external region (MPER). In some embodiments, the additional therapeutic agent comprises a second and optionally third anti-HIV Env antibody, which binds to the V2 apex, N332/V3 base supersite, silent face, gp120-gp41 interface or membrane-proximal external region (MPER). In some embodiments, the additional therapeutic agent comprises a second anti- HIV Env antibody, which binds to the CD4 binding site (CD4bs) epitope region. In some embodiments, the additional therapeutic agent comprises a second anti-HIV Env antibody, which binds to the V2 apex epitope region. In some embodiments, the additional therapeutic agent comprises a second anti-HIV Env antibody, which binds to the N332/V3 base supersite epitope region. In some embodiments, the additional therapeutic agent comprises a second anti-HIV Env antibody, which binds to the gp120-gp41 interface epitope region. In some embodiments, the additional therapeutic agent comprises a second anti-HIV Env antibody, which binds to the silent face epitope region. In some embodiments, the additional therapeutic agent comprises a second anti-HIV Env antibody, which binds to the membrane-proximal external region (MPER). In certain embodiments, the subject is at risk for exposure to HIV. In some embodiments, the subject is infected with HIV. In some embodiments, the subject is diagnosed with AIDS. In certain embodiments, the subject at risk for exposure to HIV is a health care worker. In certain embodiments, the subject at risk for exposure to HIV is a sex worker. In certain embodiments, the subject at risk for exposure to HIV is a sexual partner of an HIV infected individual. In certain embodiments, the subject at risk for exposure to HIV is a newborn. The invention also features methods of blocking HIV infection in a subject (e.g., a human) at risk of HIV transmission. For example, in one aspect, the subject may be a fetus of an HIV-infected pregnant female and the method includes administering to the HIV- infected pregnant female an antibody described herein (e.g., eN49P7-FRv1-23, eN49P7- FRv1-65 or eN49P7-FRv1-85), thereby blocking the HIV infection in the fetus. In other instances, the subject is a newborn having an HIV-infected mother, a subject at risk of HIV transmission following a needle stick injury, or a subject at risk of HIV transmission following a sexual exposure to an HIV-infected individual. In some embodiments, the antibody comprises eN49P7-FRv1-23. In some embodiments, the antibody comprises eN49P7-FRv1-65. In some embodiments, the antibody comprises eN49P7-FRv1-85. In some embodiments, the antibody comprises the Tris 27, Tris 28 or Tris 29 trispecific antibody. In instances when the subject is a newborn having an HIV-infected mother, the newborn can be administered an antibody described herein (e.g., eN49P7-FRv1-23, eN49P7-FRv1-65 or eN49P7-FRv1-85) peripartum and/or postpartum, for example, prior to, during, and/or following breastfeeding from the HIV-infected mother, in order to block an HIV infection in the newborn. In some embodiments, the antibody comprises eN49P7- FRv1-23. In some embodiments, the antibody comprises eN49P7-FRv1-65. In some embodiments, the antibody comprises eN49P7-FRv1-85. In some embodiments, the antibody comprises the Tris 27, Tris 28 or Tris 29 trispecific antibody. In instances when the subject is at risk of HIV transmission following a sexual exposure to an HIV-infected individual, the subject can be administered an antibody described herein (e.g., eN49P7-FRv1-23, eN49P7-FRv1-65 or eN49P7-FRv1-85) following the sexual exposure in order to block an HIV infection in the subject. In some embodiments, the antibody comprises eN49P7-FRv1-23. In some embodiments, the antibody comprises eN49P7-FRv1-65. In some embodiments, the antibody comprises eN49P7-FRv1-85. In some embodiments, the antibody comprises the Tris 27, Tris 28 or Tris 29 trispecific antibody. In some embodiments, an antibody described herein can be used as a microbicides to prevent mucosal HIV acquisition. In some embodiments, an antibody described herein is used to prevent vaginal or rectal acquisition of HIV. In some embodiments, an antibody described herein can be used as a microbicides to reduce the likelihood of mucosal HIV acquisition. In some embodiments, an antibody described herein is used to reduce the likelihood of vaginal or rectal acquisition of HIV. In any of the methods described above, further administration of ART and/or an immunomodulator and/or a second antibody is contemplated. For example, the ART and/or immunomodulator and/or a second antibody can be administered in conjunction with, prior to, concurrently with, subsequent to, or within the context of a treatment regimen that includes administration of an antibody described herein. An antibody described herein, or a pharmaceutical composition described herein can be delivered to a subject by a variety of routes, such as oral, parenteral, subcutaneous, intravenous, intradermal, transdermal, intranasal, vaginal, or anal. In some embodiments, the antibody or pharmaceutical composition is administered intravenously, vaginally, or anally. The amount of an antibody described herein, or a pharmaceutical composition described herein, which will be effective in the treatment and/or prevention of a condition will depend on the nature of the disease, and can be determined by standard clinical techniques. The precise dose to be employed in a pharmaceutical composition will also depend on the route of administration, and the seriousness of the disease, and should be decided according to the judgment of the practitioner and each subject's circumstances. For example, effective doses may also vary depending upon means of administration, target site, physiological state of the patient (including age, body weight and health), whether the patient is human or an animal, other medications administered, or whether treatment is prophylactic or therapeutic. Usually, the patient is a human but non-human mammals including transgenic mammals can also be treated. Treatment dosages are optimally titrated to optimize safety and efficacy. In certain embodiments, an in vitro assay is employed to help identify optimal dosage ranges. Effective doses may be extrapolated from dose response curves derived from in vitro or animal model test systems. Detection & Diagnostic Uses An antibody described herein can be used to detect HIV and/or assay HIV levels in a biological sample using classical immunohistological methods known to those of skill in the art, including immunoassays, such as the enzyme linked immunosorbent assay (ELISA), immunoprecipitation, or Western blotting. An antibody described herein can also be used as an imaging agent, for example, a tissue-penetrating imaging agent. In some embodiments, an antibody described herein is conjugated with a detectable label. Suitable assay labels are known in the art and include enzyme labels, such as, glucose oxidase; radioisotopes, such as iodine (¹²⁵I, ¹²¹I), carbon (¹⁴C), sulfur (³⁵S), tritium (³H), indium (¹²¹In), and technetium (⁹⁹Tc); luminescent labels, such as luminol; and fluorescent labels, such as fluorescein and rhodamine, and biotin. Such labels can be used to label an antibody or fusion polypeptide described herein. Alternatively, a second antibody that recognizes an antibody described herein can be labeled and used in combination with the antibody described herein to detect HIV levels. As used herein, the term "biological sample" refers to any biological sample obtained from a subject, cell line, tissue, or other source potentially comprising HIV. Methods for obtaining tissue biopsies and body fluids from animals (e.g., humans) are well- known in the art. In another embodiment, an antibody described herein can be used to detect levels of HIV, which levels can then be linked to certain disease symptoms. An antibody described herein may carry a detectable or functional label. An antibody described herein can carry a fluorescence label. Exemplary fluorescence labels include, for example, reactive and conjugated probes, e.g., Aminocoumarin, Fluorescein and Texas red, Alexa Fluor dyes, Cy dyes and DyLight dyes. An antibody described herein can carry a radioactive label, such as the isotopes ³H, ¹⁴C, ³²P, ³⁵S, ³⁶Cl, ⁵¹Cr, ⁵⁷Co, ⁵⁸Co, ⁵⁹Fe, ⁶⁷Cu, ⁹⁰Y, ⁹⁹Tc, ¹¹¹In, ¹¹⁷Lu, ¹²¹I, ¹²⁴I, ¹²⁵I, ¹³¹I, ¹⁹⁸Au, ²¹¹At, ²¹³Bi, ²²⁵Ac and ¹⁸⁶Re. When be utilized to identify and quantitate the specific binding of an antibody described herein to HIV. In the instance where the label is an enzyme, detection may be accomplished by any of the presently utilized colorimetric, spectrophotometric, fluorospectrophotometric, amperometric or gasometric techniques as known in the art. This can be achieved by contacting a sample or a control sample with an antibody described herein under conditions that allow for the formation of a complex between the antibody and HIV. Any complexes formed between the antibody and HIV are detected and compared in the sample and the control. An antibody described herein can also be used to purify HIV via immunoaffinity purification. In some aspects, provided herein are methods for in vitro detecting HIV in a sample, comprising contacting said sample with an antibody described herein. In some aspects, provided herein is the use of an antibody described herein, for in vitro detecting HIV in a sample. In one aspect, provided herein is an antibody or pharmaceutical composition described herein for use in the detection of HIV in a subject. In one aspect, provided herein is an antibody or pharmaceutical composition described herein for use as a diagnostic. In one preferred embodiment, the antibody comprises a detectable label. In some embodiments, the subject is a human. In some embodiments, the method of detecting HIV in a sample comprises contacting the sample with an antibody described herein. In some embodiments, the present disclosure provides methods of purifying HIV from a sample. In some embodiments, the method of purifying HIV from a sample comprises contacting the sample with an antibody described herein under conditions that allow the antibody to bind to HIV. In some embodiments, the antibody comprises a tag, for example, hexa-histidine tag or FLAG-tag to facilitate the purification of HIV. VII. Kits Provided herein are kits comprising one or more antibodies described herein (e.g., eN49P7-FRv1-23, eN49P7-FRv1-65 or eN49P7-FRv1-85). In some embodiments, a pharmaceutical pack or kit described herein comprises one or more containers filled with one or more of the ingredients of the pharmaceutical compositions described herein, such as one or more antibodies described herein. In some embodiments, a kit contains an antibody described herein or a pharmaceutical composition described herein, and a second prophylactic or therapeutic agent used in the treatment or prevention of HIV. In some embodiments, the second agent is an antiretroviral agent. In some embodiments, the second agent is a reservoir activator. In some embodiments, the second agent is an immunomodulator. In some embodiments, the second agent is one or more anti-HIV antibody. In some embodiments, the second agent is one or more anti-HIV Env antibody that binds to an HIV Env epitope region different from the HIV Env epitope region bound by an antibody disclosed herein (e.g., eN49P7-FRv1-23, eN49P7-FRv1-65 or eN49P7- FRv1-85). In some embodiments, the second agent is one or more anti-HIV Env antibody that binds to the CD4 binding site (CD4bs), V2 apex, N332/V3 base supersite, silent face, gp120-gp41 interface or membrane-proximal external region (MPER). In some embodiments, the second agent is one or more anti-HIV Env antibody that binds to the V2 apex, N332/V3 base supersite, silent face, gp120-gp41 interface or membrane-proximal external region (MPER). In some embodiments, a kit contains an antibody described herein or a pharmaceutical composition described herein, and a reagent used in the detection of HIV. In some embodiments, the detection reagent comprises DNA primers for the detection of HIV. Optionally associated with such container(s) can be a notice in the form prescribed by a governmental agency regulating the manufacture, use or sale of pharmaceuticals or biological products, which notice reflects approval by the agency of manufacture, use or sale for human administration. In some embodiments, the antibody comprises eN49P7-FRv1-23. In some embodiments, the antibody comprises eN49P7- FRv1-65. In some embodiments, the antibody comprises eN49P7-FRv1-85. In some embodiments, the antibody comprises the Tris 27, Tris 28 or Tris 29 trispecific antibody. In some embodiments, a kit described herein comprises an antibody described herein or a pharmaceutical composition described herein and a) a detection reagent, b) an HIV antigen, c) a notice that reflects approval for use or sale for human administration, or d) any combination thereof. Embodiments of the present disclosure can be further defined by reference to the following non-limiting examples, which describe in detail preparation of certain antibodies of the present disclosure and methods for using antibodies of the present disclosure. It will be apparent to those skilled in the art that many modifications, both to materials and methods, can be practiced without departing from the scope of the present disclosure. All documents, patent, and patent applications cited herein are hereby incorporated by reference, and may be employed in the practice described herein. EXAMPLES Example 1. In vitro affinity maturation of the HIV-1 bnAb N49P7-FR3 for increased neutralization breadth and potency. HIV-1 broadly neutralizing antibodies (bnAbs) have been powerful tools to inform HIV vaccine design and there is growing interest in using them for prophylactic and/or therapeutic indications [1]. The Antibody Mediated Prevention (AMP) trials found that prophylactic administration of VRC01, a CD4bs-targeting bnAb, provided protection against strains of HIV-1 that were sensitive to VRC01 neutralization. This demonstrated the potential for bnAb-mediated prevention; however, it highlighted the need for bnAbs with improved neutralization potency [2]. N49P7 is a VRC01-class bnAb that displays near pan coverage across a 117-pseudovirus global panel of HIV-1 isolates [3]. While N49P7 neutralizes HIV-1 more potently than VRC01, data from the AMP study suggests that N49P7 lacks the requisite potency to be useful for prophylactic indications. Described here is work to engineer a variant of N49P7 with improved neutralization breadth and potency. Antibody optimization workflow: A site-saturation mutagenesis scanning library, containing barcoded NNK codons sampling all amino acids (excluding cysteine) at all positions – one at a time, was constructed for VH and VL of N49P7-FR3 (SEQ ID NO: 1 and 5, respectively; Liu et al., "Rational Engraftment of Quaternary-Interactive Acidic Loops for Anti-HIV-1 Antibody Improvement." J Virol 95:10.1128/jvi.00159-21 (2021)). The library was displayed on the surface of Saccharomyces cerevisiae YVH10 cells as Fab fragments fused to a synthetic mucin-like domain and a GPI anchor. The N49P7-FR3 site-saturation libraries were screened for improved binding to 6 diverse gp120s in parallel. The antibody-encoding plasmid was recovered from the enriched cells as well as an unselected control population and deep sequence analyzed. The frequency of amino acids from the enriched dataset was normalized against the unselected dataset to develop a sequence/function profile for all single mutations within the antibody variable domain. A combinatorial library (>2 x 10⁶ variants) was then constructed that sampled all possible combinations of either the original amino acid or the favorable (most enriched and structurally important) amino acids identified in the mutagenesis screening. This combinatorial library was displayed on yeast and screened against 12 HIV gp120s in parallel to identify variants with improved binding affinity. The combinatorial library was screened with a total of five selections: three sorts to identify variants with improved binding to gp120 interspersed with two sorts to deplete variants with high binding to polyspecificity reagent (removing sticky antibodies). Antibody-encoding DNA from the enriched cells was deep sequence analyzed to identify antibodies that had improved binding affinity across all 12 gp120s. Selected variants were produced as IgG and tested for neutralization and biochemical properties. Optimization of VH to enhance potency: After selections, the 24 most frequent VH combinatorial library variants were produced as IgG. 4 variants were not polyreactive with CHO-SMP (ELISA). Three of them (VHv1, VHv10, and VHv13) displayed several-fold improved potency and breadth against 14 HIV-1 pseudoviruses from a 12- and 6-virus global panels. Table 5. HIV-1 pseudovirus cross-clade small global panel N49P7 N49P7- VHv1 VHv4 VHv10 VHv13 FR3 o u a e y, ese e a ce a a s a e uce y e co pa e o he parental N49P7-FR3, showed a delayed SEC retention time (tR), and precipitated in PBS after purification, thus requiring further design iterations to correct the biochemical behavior. Table 6. Biochemical properties. Precipitation observed after antibody elutionand buffer exchange into PBS. SEC Column: TSKgel SuperSW mAb HTP (Tosoh Bioscinece) length – 15 cm. Antibody Expi293F titer Precipitation SECtR [m /L] [min] This was accomplished by combining additional rounds of mutagenesis scanning with chain shuffling to screen for variants that retained both the favorable neutralization and biochemical profile. Optimization of VL to correct biochemical behavior: N49P7-FR3 VHv10, which exhibited the best developability profile of all top three VH variants, was selected as the constant VH when screening a VL combinatorial library. After selections, the 21 most frequent VL combinatorial library variants were produced as IgG. None of them showed polyreactivity with CHO-SMP, insulin, and ssDNA (ELISA). All VL variants still had a delayed SEC tR, however, 17 had a single, monodispersed peak. The top three VL variants had similar neutralization potencies and improved thermal stability (Tm). Next, previously engineered top VH variants were paired with one of the top new VL variants, VLv3. The combination VHv1 with VLv3 retained the gains in neutralization potency previously observed compared to the parental N49P7-FR3. Table 7. HIV-1 pseudovirus cross-clade Seaman global panel. N49P7- VH-WT/ VHv1/ VHv10/ VHv13/ FR3 VLv3 VLv3 VLv3 VLv3 The overall biochemical behavior of VHv1/VLv3 showed improvements compared to VHv1 paired with the parental light chain, however, the production yield remained low and SEC tR was still delayed, requiring additional corrections. Table 8. Biochemical properties. Precipitation after elution, low pH hold(1h at pH 3.0), and buffer exchange. SEC Column: TSKgel SuperSW mAb HR (Tosoh Bioscinece) length – 15 cm. Antibody Expi293F titer Precipitation SECt_R Tm ° Re-optimization of VH to remove remaining liabilities: A final round of heavy chain optimization was performed using VHv1/VLv3 as the starting bnAb. After selections, the 96 most frequent VHv1 combinatorial library variants were produced as IgG and paired with VLv3. 95 variants were not polyreactive with CHO-SMP (ELISA) and 10 variants had SEC tR within the range of a panel of clinical antibodies [5]. Among them, three VHv1 variants (VHv1-23, VHv1-65, and VHv1-85) showed no reactivity with HEp- 2 cells, relatively high production yield, and improved thermal stability (Tm) compared to the parental N49P7-FR3. eN49P7-FRv1-23 showed relatively high production yield, no reactivity with CHO-SMP in PSR-ELISA, optimal SEC retention time (SEC tR) within the range of a panel of clinical antibodies, and improved thermal stability (Tm) compared to the parental N49P7-FR. Table 9. Biochemical properties. (1) CHO-SMP (Chinese hamster ovary soluble membrane proteins) was used as a poly-specificity reagent (PSR) in ELISA (2) SEC column: TSKgel SuperSW mAb HR (Tosoh Bioscience), length - 30 cm (3) FDA-approved reference antibody (4) Polyreactive antibody used as control in PSR-ELISA (5) FDA- approved antibodies used as controls in SEC (6) Precipitation after elution, low pH hold(1h at pH 3.0), and buffer exchange. Antibody Expi293F Polyreactivity Precipitation SECt_R Tm tit r with CHO- (6) (2) [°C] 4E10 (4) 2.79 Golimumab (5) 9.1 y across HIV-1 pseudoviruses from the Seaman global panel (Figure 1) and from the VRC01 AMP trials (Figures 2 and 3). eN49P7-FR v1-23 had neutralization breadth improved 5- and 2- fold (IC80 ≤0.1 µg/mL), and median potency increased 36- and 5-fold compared to VRC01 and the parental N49P7-FR bnAb, respectively, against 149 HIV-1 pseudoviruses selected from the Seaman global panel and VRC01 AMP trials. Table 10. HIV-1 pseudovirus cross-clade Seaman global panel (Figure 1). IC₈₀ [ug/mL] HIV-1 pseudovirus Clade N49P7- eN49P7- eN49P7- eN49P7- 5 Ce703010054_2A2 C 0.669 0.354 0.082 0.071 0.078 246F C1G C 1.907 0.038 0.040 0.157 0.019 Table 11. Pseudoviruses derived from AMP trial placebo group clade B HIV-1 (Figure 2). IC₈₀ [µg/mL] 7- 5 H704_2767_070sN B 3.217 2.711 >50 >50 >50 H704_2788_060eN_04 B 1.719 0.121 0.019 0.019 0.025 6 H704_1528_240_RE_pblib_001_s B 2.006 0.046 0.016 0.032 0.019 H704_2684_181_RE_pblib006_s B 0.091 0.018 0.007 0.010 0.009 3 re 3). IC₈₀ [µg/mL] HIV-1 pseudovirus Clade VRC01 N49P7- eN49P7- eN49P7- eN49P7- 5 V703_2372_170_RE_con_s C 3.8890 0.074 0.012 0.020 0.013 Upon in FR v1-23 with the LS mutation inserted in the Fc region had a serum half-life comparable to that of VRC01 with the LS mutation and slightly increased compared to VRC01 without the LS mutation. Table 13. Pharmacokinetics Antibody Half-life in hFcRn mice [days] eN49P7-FRv1-23, a variant of N49P7-FR with several-fold improved neutralization breadth and potency compared to VRC01 and the parental bnAb against a large panel of HIV-1 pseudoviruses representing globally circulating strains was generated. eN49P7-FRv1-23 neutralized 92% of 149 HIV-1 pseudoviruses at IC80 ≤0.1 µg/mL. The variant of eN49P7-FRv1-23, containing the LS mutation in Fc, had a mouse serum half- life comparable to that of VRC01 LS. Based on the results of the VRC01 Antibody Mediated Prevention (AMP) trials, eN49P7-FR v1-23 should provide protection from the acquisition of the in vitro neutralized viruses, including 95% of the tested VRC01 AMP trial viruses, with prevention efficacy exceeding 90% (Corey et al., "Two Randomized Trials of Neutralizing Antibodies to Prevent HIV-1 Acquisition." N Engl J Med. 384(11):1003-1014 (2021)). In contrast, VRC01 provided protection against 30% of HIV- 1 strains present at the trial sites. This makes the engineered bnAb eN49P7-FR v1-23 a promising clinical candidate for future AMP trials and/or therapeutic regimens. It can be used in combination with other potent bnAbs to confer extremely broad and potent protection or to lower the risk of emerging viral escape mutant strains during therapy. References: _{[1] Griffith SA, McCoy LE. 2021. To bnAb or Not to bnAb: Defining Broadly Neutralising} Antibodies Against HIV-1. Front Immunol. 12:708227. _{[2] Corey L, Gilbert PB, Juraska M, Montefiori DC, et al. 2021. Two Randomized Trials} of Neutralizing Antibodies to Prevent HIV-1 Acquisition. N Engl J Med. 384(11):1003- 1014. _{[3] Sajadi MM, Dashti A, Rikhtegaran Tehrani Z, Tolbert WD, et al. 2018. Identification} of Near-Pan-neutralizing Antibodies against HIV-1 by Deconvolution of Plasma Humoral Responses. Cell 173(7):1783-1795.e14. _{[4] Liu Q, Zhang P, Miao H, Lin Y, et al. 2021. Rational Engraftment of Quaternary-} Interactive Acidic Loops for Anti-HIV-1 Antibody Improvement. J Virol. 95(12):e00159- 21. _{[5] Jain T, Sun T, Durand S, Hall A, et al. 2017. Biophysical properties of the clinical-stage} antibody landscape. Proc Natl Acad Sci U S A. 114(5):944-949. Example 2. Trispecific anti-HIV Env bnAbs Trispecific antibodies depicted in Figure 4 were produced as described in WO 2024/192203, which is incorporated by reference herein in its entirety for all purposes. HIV-1 pseudovirus neutralization assays were used to assess the trispecific antibodies as described in WO 2024/192203. The result of the assays are shown in the Tables below and in Figures 5-8.

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F 42 4 ^e 1 ^e _P 0_P ^{] a} _l G _{s (} 53 02 02 80 37 30 31 _{01 002 0003005 001 00}R9vG0 81 31 33 37 28 00 63 17 89 88 20 81 30 57 94 34 59 11 2 P vD _F 71 T9 - _{+ +}M ⁱ _gu F 0 .₀00 0 0 0 0 0 00 0 0 0 0 0 0 0 00 0 0 0 0 0 0 0R ^e _N 1 14 ^e 421 ^e _P 0_P ^re G ₆ 0^. ₀6^. ₀0^. ₀0^. ₀0^. ₀ ^. ₀ ^. ₀ ^. ₀ ^. ₀ ^. ₀ ^. ₀ ^. ₀ ^. ₀ ^. ₀ ^. ₀ ^. ₀ ^. ₁ ^. ₀ ^. ₀ ^. ₁ ^. ₀ ^. ₀ ^. ₀ ^. ₀ ^. ₀v19vG0vD ⁾. 5 ^{05 94}1 31 71 77 31 13 72 32 57 83 43 82 38 40 50 91 05 12 01 61 31 0 ^- ₂ P1 T9 37 M - _{+ +} 00 0 0 0 0 0 0 T .₀0^. ₀ ^. ₀ ^. ₀ ^. ₀ ^. ₀ ^. ₀ ^. ₂0 .₁0 .₁2 .₃0 .₇0 .₁0 .₀0 .₀0 .₁0 .₀0 .₇0 .₀0 .₄0 .₆0 .₀0 . 0 . 0 . 0 . ^{r 9}2 61 96 50 51 31 22 71 31 24 58 48 09 31 24 96 34 71 17 36 96₁ 48₁ 13₁ 70₁ 60 i_S 2 ^-2 000000 _T .₀ ^. ₀ ^. ₀ ^. ₀ ^. ₀ ^. ₀0 .₀0 .₀0 .₀0 .₀0 .₆0 .₄0 .₁0 .₀0 .₀0 .₀0 .₀0 .₂0 .₀0 . 0 . 0 . 0 . 0 . 0 . 0 . ^ri 0106010676220618280₄7₆0₀3₁5₀3₀2₀6 _S 8^{35 35 0895 695 7 1 342 1 9402 7 65 1 -} ₂ 7 00 0 0 _T .₀ ^. ₀ ^. ₀ ^. ₀0 .₀0 .₀0 .₀0 .₁0 .₁0 .₀1 .₁0 .₄0 .₁0 .₀0 .₀0 .₁0 .₀0 . 0 . 1 . 0 . 0 . 0 . 0 . 0 . 0 . ^ri 12090108093346102₃1₀1₀2₅5₀2₁2_{000 S} 1 ^{5 6341 7 8005 5 437 7 631 5 089}3 52 56 8 ^- ₂ 8 0 _T .₀0 .₀0 .₀0 .₀0 .₀0 .₀0 .₀0 .₁0 .₀0 .₀1 .₀0 .₃0 .₁0 .₀0 . 0 . 0 . 0 . 0 . 0 . 0 . 0 . 0 . 0 . 0 . 0 . ^ri 01080108693947₀1₀9₀3₂6₀0₄4₇3_{01 000 S} 9^{7 67 5 098397 07 37 42 995 7}4 58 03 63 47 7 ^- ₂ 9 H H H H 70707070 s_{_}3^s _{_} ^c _R D2F E 5 ¹ _ e₉B 7 s C C C C >5 > > > 0505050 > 0 5 > 05 > 050^. ₀0 4 0 .₀00 0 4 ^. ₀ ^. ₅ 133 ^. ₂ 6152 29 7 ^{7 6} 0 .₀0 4 ^. ₀0 .₀0 .₀ 73 10 83 7 0 .₀0 6 ^. ₀0 .₀0 .₀ 93 10 94 4 0 .₀0 4 ^. ₀00 2 ^. ₀ ^. ₀ 9²1 14 6 0 .₀0 5 ^. ₀0 3^. ₄0 .₀ 9⁶1 40 4 0 .₀0 6 ^. ₀0 32 ^. ₀0 81 ^. ₀ 10 4 1 .₁00 0 4 ^. ₇ ^. ₀ ^. ₀ 42 95 31 4 0 .₅0 9 ^. ₅0 .₀0 .₀ 16 20 91 0 1 .₁2 4 ^. ₅00 3^. ₀ ^. ₀ 6²1 51 1 0 .₆10 4 ^. ₁6^. ₀0 0 ^. ₀ 7 ^{5 8}1 5 Table 16. Neutralization results for a select group of eight HIV-1 pseudoviruses (Figure 7). IC₈₀ [µg/mL] ePGDM S- 7 3_{2 22 13 61 75 08 13} 23 Table 17. Neutralization potency of TriS-27 against HIV-1 panel from VRC01 AMP trials (Figure 8). IC₈₀ [µg/mL] ePGDM S- 7₀ 15 6_{5 18 70 66} 20 15 4₉ 24 9_{0 16 09 13 41 32 43} H704_3008_040EsN B >50 0.003 0.116 0.004 0.035 H704_0513_150_eN01T B >50 >50 0.405 0.369 3.719 32 34 53 23 38 64 70 21 27 22 63 61 78 55 65 41 40 85 18 72 61 38 58 26 39 03 02 42 63 50 78 06 57 35 25 16 75 29 14 74 19 48 12 44 V703_0309_100_RE_pblib002_s C 0.015 0.021 0.055 0.006 0.016 H703_0322_130s_M1I C 7.336 0.004 0.057 0.003 0.014 10 11 09 18 32 17 35 12 21 13 09 25 44 53 04 05 02 24 94 33 33 31 47 09 30 18 04 45 Table 16 and Figure 7 presents data demonstrating the neutralization breadth and potency of TriS-27, a trispecific antibody, in comparison to its parental monoclonal antibodies administered individually or in combination, against a panel of HIV-1 pseudoviruses. The selected subset of eight pseudoviruses, which were largely resistant to ePGDM1400v9 or ePGT121v1 and moderately sensitive to eN49P7-FRv1-23, exhibited significantly enhanced neutralization by TriS-27 relative to the parental antibodies. These findings indicate a synergistic effect achieved through the combination of the parental components into a trispecific format. Although previous studies have reported increased neutralization breadth with bi- and trispecific antibody formats (Padte et al., 2018, Retrovirology 15, 60, DOI: 10.1186/s12977-018-0439-9; Xu et al., 2017, Science 358, 85-90, DOI: 10.1126/science.aan8630), the reported gains often did not correlate with improved potency relative to the parental monospecific antibodies. Strategies aimed at enhancing potency, such as increasing valency via flexible linker-connected scFv domains in trispecific antibodies (Steinhardt et al., 2018, Nat Commun 9, 877, DOI: 10.1038/s41467- 018-03335-4) or incorporating extended hinge regions in bispecific antibodies (Bournazos et al., 2016, Cell 165(7), 1609-1620, DOI: 10.1016/j.cell.2016.04.050) have shown promise. However, the data presented here is one of the few reported instances of a clear synergistic enhancement of potency in a trispecific antibody, highlighting that rational molecular design and optimal domain pairing can yield functionality beyond the additive properties of individual antibody components. Table 17 and Figure 8 demonstrate the neutralization breadth and potency of TriS-27 in comparison to its parental monoclonal antibodies administered individually or in combination, against the HIV-1 panel from VRC01 AMP trials, representing circulating viral strains. TriS-27 exhibited pan-neutralizing activity against all pseudoviruses with median IC80 of 0.041 µg/mL. The exceptional breadth of TriS-27 surpassed that of any of the best-in-class monoclonal bnAbs targeting diverse HIV epitopes, including engineered bnAbs with enhanced potency (Figure 9). TriS-27 maintained the broadest viral coverage even at IC80 <0.1 µg/mL, neutralizing 89% pseudoviruses at IC80 <0.3 µg/mL (this IC80 threshold, indicated by a vertical dotted line in Figure 9, correlates with prevention efficacy exceeding 80%, according to VRC01 AMP trials). While the invention has been described in connection with what is presently considered to be the most practical and preferred embodiments, it is to be understood that the invention is not to be limited to the disclosed embodiments, but on the contrary, is intended to cover various modifications and equivalent arrangements included within the spirit and scope of the appended claims. All publications, patents, patent applications, internet sites, and accession numbers/database sequences including both polynucleotide and polypeptide sequences cited herein are hereby incorporated by reference herein in their entirety for all purposes to the same extent as if each individual publication, patent, patent application, internet site, or accession number/database sequence were specifically and individually indicated to be so incorporated by reference.

Claims

CLAIMS What is claimed is: 1. An isolated monoclonal antibody that is capable of binding HIV Env and comprises a heavy chain variable region (VH) comprising a VH CDR1, VH CDR2, and VH CDR3 and a light chain variable region (VL) comprising a VL CDR1, VL CDR2, and VL CDR3, wherein the VH CDR1, VH CDR2, VH CDR3, VL CDR1, VL CDR2, and VL CDR3 comprise the amino acid sequence of the eN49P7-FRv1-23, eN49P7-FRv1-65 or eN49P7- FRv1-85 VH CDR1, VH CDR2, VH CDR3, VL CDR1, VL CDR2, and VL CDR3, respectively.

2. The isolated monoclonal antibody of claim 1, wherein the VH comprises an amino acid sequence that is at least about 90%, 95%, 97%, 98%, 99% or 100% identical to the eN49P7- FRv1-23 VH, eN49P7-FRv1-65 VH or eN49P7-FRv1-85 VH..

3. The isolated monoclonal antibody of claim 1 or 2, wherein the VL comprises an amino acid sequence that is at least about 90%, 95%, 97%, 98%, 99% or 100% identical to eN49P7-FRv1-23 VL, eN49P7-FRv1-65 VL or eN49P7-FRv1-85 VL.

4. The isolated monoclonal antibody of any one of claims 1 to 3, wherein the VH comprises the eN49P7-FRv1-23 VH, eN49P7-FRv1-65 VH or eN49P7-FRv1-85 VH and the VL comprises the eN49P7-FRv1-23 VL, eN49P7-FRv1-65 VL or eN49P7-FRv1-85 VL.

5. The monoclonal antibody of any one of claims 1 to 4, further comprising a heavy and/or light chain constant region.

6. The monoclonal antibody of any one of claims 1 to 4, further comprising a human heavy and/or light chain constant region.

7. The monoclonal antibody of claim 5 or claim 6, wherein the heavy chain constant region is selected from the group consisting of a human immunoglobulin IgG₁, IgG₂, IgG₃, IgG₄ constant region.

8. The monoclonal antibody of any one of claims 5 to 7, wherein the heavy chain constant region comprises a native amino acid sequence.

9. The monoclonal antibody of any one of claims 5 to 7, wherein the heavy chain constant region comprises a non-native variant amino acid sequence.

10. The monoclonal antibody of any one of claims 1 to 9, wherein the antibody is a recombinant antibody, a chimeric antibody, a human antibody, an antibody fragment, a bispecific antibody, or a trispecific antibody.

11. The monoclonal antibody of claim 10, wherein the antibody is an antigen binding fragment comprising a single-chain Fv (scFv), Fab fragment, F(ab’)₂ fragment, or an isolated VH domain.

12. The monoclonal antibody of claim 10, wherein the antibody is a bispecific antibody.

13. The monoclonal antibody of claim 10, wherein the antibody is a trispecific antibody.

14. The monoclonal antibody of claim 13, which is a trispecific antibody comprising (i) a first scFv linked to a first Fc domain, (ii) an antibody heavy chain comprising a second Fc domain, and (iii) second scFv domain linked to an antibody light chain, wherein the first scFv linked to a first Fc domain, the antibody heavy chain comprising the second Fc domain, and the second scFv domain linked to the antibody light chain comprise an amino acid sequence having at least 80%, at least 85%, at least 90%, at least 95%, at least 97% or 100% identity to SEQ ID NOs: 75, 76, and 79, respectively, SEQ ID NOs: 75, 76, and 81, respectively, or SEQ ID NOs: 75, 76, and 83, respectively.

15. A pharmaceutical composition comprising the antibody or antigen-binding fragment thereof of any one of claims 1 to 14 and a pharmaceutically acceptable excipient.

16. An isolated polynucleotide encoding the antibody or antigen-binding fragment thereof of any one of claims 1 to 14.

17. The isolated polynucleotide of claim 16, which is a DNA.

18. The isolated polynucleotide of claim 16, which is an mRNA.

19. The isolated polynucleotide of claim 18, wherein the mRNA comprises a modified nucleotide.

20. An isolated vector comprising the polynucleotide of claim 16.

21. The isolated vector of claim 20, wherein the vector is a viral vector.

22. A recombinant virus comprising the polynucleotide of claim 16.

23. The recombinant virus of claim 22, which is a recombinant adeno-associated virus (AAV).

24. A host cell comprising the polynucleotide of claim 16 or the vector of claim 20.

25. A method of producing the antibody or antigen-binding fragment thereof of any one of claims 1 to 14 comprising culturing the host cell of claim 24 so that the antibody or antigen- binding fragment thereof is expressed and the antibody or antigen-binding fragment thereof is produced.

26. A method of neutralizing an HIV virus comprising contacting the virus with a sufficient amount of the antibody or antigen-binding fragment thereof of any one of claims 1 to 14.

27. A method of reducing the likelihood of HIV infection in a subject exposed to HIV comprising administering to the subject a therapeutically sufficient amount of the antibody or antigen-binding fragment thereof of any one of claims 1 to 14.

28. A method of treating HIV/AIDS comprising administering to a subject in need thereof a therapeutically sufficient amount of the antibody or antigen-binding fragment thereof of any one of claims 1 to 14.

29. A method of reducing viral load comprising administering to a subject in need thereof a therapeutically sufficient amount of the antibody or antigen-binding fragment thereof of any one of claims 1 to 14.

30. The method of any one of claims 27 to 29, further comprising administering at least one additional therapeutic agent.

31. A method for detecting HIV in a sample comprising contacting the sample with the antibody of any one of claims 1 to 14.

32. A method of producing an engineered variant of an antibody of any one of claims 1 to 11 comprising (a) substituting one or more amino acid residues of the VH; and/or substituting one or more amino acid residues of the VL to create an engineered variant antibody, and (b) producing the engineered variant antibody.

33. The method of claim 32 wherein the antibody is eN49P7-FRv1-23, eN49P7-FRv1-65 or eN49P7-FRv1-85.