JP2004515243A - サイレント抗cd28抗体およびその使用 - Google Patents
サイレント抗cd28抗体およびその使用 Download PDFInfo
- Publication number
- JP2004515243A JP2004515243A JP2002549291A JP2002549291A JP2004515243A JP 2004515243 A JP2004515243 A JP 2004515243A JP 2002549291 A JP2002549291 A JP 2002549291A JP 2002549291 A JP2002549291 A JP 2002549291A JP 2004515243 A JP2004515243 A JP 2004515243A
- Authority
- JP
- Japan
- Prior art keywords
- antibody
- cells
- seq
- mouse
- igg3
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Withdrawn
Links
- 238000000034 method Methods 0.000 claims abstract description 53
- 210000001744 T-lymphocyte Anatomy 0.000 claims abstract description 28
- 238000004519 manufacturing process Methods 0.000 claims abstract description 18
- 230000001506 immunosuppresive effect Effects 0.000 claims abstract description 8
- 210000000056 organ Anatomy 0.000 claims abstract description 8
- 230000001939 inductive effect Effects 0.000 claims abstract description 6
- 210000004027 cell Anatomy 0.000 claims description 147
- 101000914514 Homo sapiens T-cell-specific surface glycoprotein CD28 Proteins 0.000 claims description 56
- 102100027213 T-cell-specific surface glycoprotein CD28 Human genes 0.000 claims description 56
- 239000013604 expression vector Substances 0.000 claims description 28
- 125000003275 alpha amino acid group Chemical group 0.000 claims description 24
- 108091033319 polynucleotide Proteins 0.000 claims description 17
- 102000040430 polynucleotide Human genes 0.000 claims description 17
- 239000002157 polynucleotide Substances 0.000 claims description 17
- 239000012634 fragment Substances 0.000 claims description 15
- 239000008194 pharmaceutical composition Substances 0.000 claims description 6
- 238000012258 culturing Methods 0.000 claims description 5
- 102000001706 Immunoglobulin Fab Fragments Human genes 0.000 claims description 4
- 108010054477 Immunoglobulin Fab Fragments Proteins 0.000 claims description 4
- 239000003018 immunosuppressive agent Substances 0.000 claims description 4
- FWMNVWWHGCHHJJ-SKKKGAJSSA-N 4-amino-1-[(2r)-6-amino-2-[[(2r)-2-[[(2r)-2-[[(2r)-2-amino-3-phenylpropanoyl]amino]-3-phenylpropanoyl]amino]-4-methylpentanoyl]amino]hexanoyl]piperidine-4-carboxylic acid Chemical compound C([C@H](C(=O)N[C@H](CC(C)C)C(=O)N[C@H](CCCCN)C(=O)N1CCC(N)(CC1)C(O)=O)NC(=O)[C@H](N)CC=1C=CC=CC=1)C1=CC=CC=C1 FWMNVWWHGCHHJJ-SKKKGAJSSA-N 0.000 claims 4
- 229960003444 immunosuppressant agent Drugs 0.000 claims 3
- 230000001861 immunosuppressant effect Effects 0.000 claims 3
- 230000002297 mitogenic effect Effects 0.000 abstract description 11
- 238000002054 transplantation Methods 0.000 abstract description 9
- 239000000203 mixture Substances 0.000 abstract description 6
- 206010062016 Immunosuppression Diseases 0.000 abstract description 3
- 108090000623 proteins and genes Proteins 0.000 description 51
- 241000699666 Mus <mouse, genus> Species 0.000 description 49
- 230000027455 binding Effects 0.000 description 32
- 238000002474 experimental method Methods 0.000 description 26
- 235000018102 proteins Nutrition 0.000 description 25
- 102000004169 proteins and genes Human genes 0.000 description 25
- 239000002609 medium Substances 0.000 description 23
- 108700024394 Exon Proteins 0.000 description 21
- MHMNJMPURVTYEJ-UHFFFAOYSA-N fluorescein-5-isothiocyanate Chemical compound O1C(=O)C2=CC(N=C=S)=CC=C2C21C1=CC=C(O)C=C1OC1=CC(O)=CC=C21 MHMNJMPURVTYEJ-UHFFFAOYSA-N 0.000 description 18
- 238000003752 polymerase chain reaction Methods 0.000 description 18
- 238000000684 flow cytometry Methods 0.000 description 17
- 238000002965 ELISA Methods 0.000 description 16
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 16
- 241000283707 Capra Species 0.000 description 14
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 14
- 238000012360 testing method Methods 0.000 description 14
- 239000013598 vector Substances 0.000 description 14
- 238000004458 analytical method Methods 0.000 description 13
- 239000002299 complementary DNA Substances 0.000 description 13
- 210000004408 hybridoma Anatomy 0.000 description 13
- 238000003998 size exclusion chromatography high performance liquid chromatography Methods 0.000 description 12
- 241000699800 Cricetinae Species 0.000 description 11
- 230000002829 reductive effect Effects 0.000 description 11
- 241000699670 Mus sp. Species 0.000 description 10
- 241000283074 Equus asinus Species 0.000 description 9
- 241001465754 Metazoa Species 0.000 description 9
- 235000001014 amino acid Nutrition 0.000 description 9
- 238000003556 assay Methods 0.000 description 9
- 238000010367 cloning Methods 0.000 description 9
- 239000013612 plasmid Substances 0.000 description 9
- 102000008203 CTLA-4 Antigen Human genes 0.000 description 8
- 108010021064 CTLA-4 Antigen Proteins 0.000 description 8
- 229940045513 CTLA4 antagonist Drugs 0.000 description 8
- 229940024606 amino acid Drugs 0.000 description 8
- 150000001413 amino acids Chemical class 0.000 description 8
- 238000004128 high performance liquid chromatography Methods 0.000 description 8
- 239000002773 nucleotide Substances 0.000 description 8
- 125000003729 nucleotide group Chemical group 0.000 description 8
- 239000011780 sodium chloride Substances 0.000 description 8
- 108010076504 Protein Sorting Signals Proteins 0.000 description 7
- 230000006044 T cell activation Effects 0.000 description 7
- 210000000612 antigen-presenting cell Anatomy 0.000 description 7
- 239000003153 chemical reaction reagent Substances 0.000 description 7
- 230000000694 effects Effects 0.000 description 7
- 238000011534 incubation Methods 0.000 description 7
- 239000000047 product Substances 0.000 description 7
- 238000012163 sequencing technique Methods 0.000 description 7
- 230000001052 transient effect Effects 0.000 description 7
- 102000017420 CD3 protein, epsilon/gamma/delta subunit Human genes 0.000 description 6
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 6
- WCUXLLCKKVVCTQ-UHFFFAOYSA-M Potassium chloride Chemical compound [Cl-].[K+] WCUXLLCKKVVCTQ-UHFFFAOYSA-M 0.000 description 6
- 206010052779 Transplant rejections Diseases 0.000 description 6
- 239000000427 antigen Substances 0.000 description 6
- 108091007433 antigens Proteins 0.000 description 6
- 102000036639 antigens Human genes 0.000 description 6
- 239000000872 buffer Substances 0.000 description 6
- 230000001419 dependent effect Effects 0.000 description 6
- 238000001943 fluorescence-activated cell sorting Methods 0.000 description 6
- 239000000499 gel Substances 0.000 description 6
- 238000002347 injection Methods 0.000 description 6
- 239000007924 injection Substances 0.000 description 6
- 230000003993 interaction Effects 0.000 description 6
- 239000003550 marker Substances 0.000 description 6
- 239000000243 solution Substances 0.000 description 6
- 238000006467 substitution reaction Methods 0.000 description 6
- LWIHDJKSTIGBAC-UHFFFAOYSA-K tripotassium phosphate Chemical compound [K+].[K+].[K+].[O-]P([O-])([O-])=O LWIHDJKSTIGBAC-UHFFFAOYSA-K 0.000 description 6
- 102000010910 CD28 Antigens Human genes 0.000 description 5
- 108010062433 CD28 Antigens Proteins 0.000 description 5
- 108020004414 DNA Proteins 0.000 description 5
- 108010087819 Fc receptors Proteins 0.000 description 5
- 102000009109 Fc receptors Human genes 0.000 description 5
- 229960002685 biotin Drugs 0.000 description 5
- 239000011616 biotin Substances 0.000 description 5
- 238000006243 chemical reaction Methods 0.000 description 5
- 230000000295 complement effect Effects 0.000 description 5
- 229940079593 drug Drugs 0.000 description 5
- 239000003814 drug Substances 0.000 description 5
- 239000013613 expression plasmid Substances 0.000 description 5
- 238000007799 mixed lymphocyte reaction assay Methods 0.000 description 5
- 230000035772 mutation Effects 0.000 description 5
- 230000009871 nonspecific binding Effects 0.000 description 5
- 238000002360 preparation method Methods 0.000 description 5
- 102000005962 receptors Human genes 0.000 description 5
- 108020003175 receptors Proteins 0.000 description 5
- 239000012679 serum free medium Substances 0.000 description 5
- 238000010561 standard procedure Methods 0.000 description 5
- 230000004083 survival effect Effects 0.000 description 5
- 238000013518 transcription Methods 0.000 description 5
- 230000035897 transcription Effects 0.000 description 5
- 238000003146 transient transfection Methods 0.000 description 5
- 102100032937 CD40 ligand Human genes 0.000 description 4
- 241000282693 Cercopithecidae Species 0.000 description 4
- 108020004635 Complementary DNA Proteins 0.000 description 4
- 241000699679 Cricetulus migratorius Species 0.000 description 4
- 206010035226 Plasma cell myeloma Diseases 0.000 description 4
- 230000006052 T cell proliferation Effects 0.000 description 4
- 108091008874 T cell receptors Proteins 0.000 description 4
- 102000016266 T-Cell Antigen Receptors Human genes 0.000 description 4
- IQFYYKKMVGJFEH-XLPZGREQSA-N Thymidine Chemical compound O=C1NC(=O)C(C)=CN1[C@@H]1O[C@H](CO)[C@@H](O)C1 IQFYYKKMVGJFEH-XLPZGREQSA-N 0.000 description 4
- 238000001042 affinity chromatography Methods 0.000 description 4
- 206010003246 arthritis Diseases 0.000 description 4
- 238000005119 centrifugation Methods 0.000 description 4
- 238000005516 engineering process Methods 0.000 description 4
- 238000010353 genetic engineering Methods 0.000 description 4
- 210000004602 germ cell Anatomy 0.000 description 4
- 230000003053 immunization Effects 0.000 description 4
- 238000002649 immunization Methods 0.000 description 4
- 210000003292 kidney cell Anatomy 0.000 description 4
- 201000000050 myeloid neoplasm Diseases 0.000 description 4
- 210000003819 peripheral blood mononuclear cell Anatomy 0.000 description 4
- 108090000765 processed proteins & peptides Proteins 0.000 description 4
- 238000012545 processing Methods 0.000 description 4
- 238000001742 protein purification Methods 0.000 description 4
- 238000013207 serial dilution Methods 0.000 description 4
- 238000003153 stable transfection Methods 0.000 description 4
- 230000000638 stimulation Effects 0.000 description 4
- 235000000346 sugar Nutrition 0.000 description 4
- 239000006228 supernatant Substances 0.000 description 4
- 210000001519 tissue Anatomy 0.000 description 4
- 108091032973 (ribonucleotides)n+m Proteins 0.000 description 3
- NHBKXEKEPDILRR-UHFFFAOYSA-N 2,3-bis(butanoylsulfanyl)propyl butanoate Chemical compound CCCC(=O)OCC(SC(=O)CCC)CSC(=O)CCC NHBKXEKEPDILRR-UHFFFAOYSA-N 0.000 description 3
- 241000283690 Bos taurus Species 0.000 description 3
- 108700031361 Brachyury Proteins 0.000 description 3
- PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 3
- 239000004471 Glycine Substances 0.000 description 3
- 241000701024 Human betaherpesvirus 5 Species 0.000 description 3
- 241001529936 Murinae Species 0.000 description 3
- 108091028043 Nucleic acid sequence Proteins 0.000 description 3
- 239000012980 RPMI-1640 medium Substances 0.000 description 3
- 229920002684 Sepharose Polymers 0.000 description 3
- 241000700605 Viruses Species 0.000 description 3
- 238000002835 absorbance Methods 0.000 description 3
- 230000004913 activation Effects 0.000 description 3
- 239000000654 additive Substances 0.000 description 3
- CKLJMWTZIZZHCS-REOHCLBHSA-N aspartic acid group Chemical group N[C@@H](CC(=O)O)C(=O)O CKLJMWTZIZZHCS-REOHCLBHSA-N 0.000 description 3
- 230000003833 cell viability Effects 0.000 description 3
- 238000004587 chromatography analysis Methods 0.000 description 3
- 238000004040 coloring Methods 0.000 description 3
- 238000005094 computer simulation Methods 0.000 description 3
- 238000010276 construction Methods 0.000 description 3
- 239000003623 enhancer Substances 0.000 description 3
- 125000000404 glutamine group Chemical group N[C@@H](CCC(N)=O)C(=O)* 0.000 description 3
- 101150106093 gpt gene Proteins 0.000 description 3
- 239000001963 growth medium Substances 0.000 description 3
- 230000006058 immune tolerance Effects 0.000 description 3
- 238000000338 in vitro Methods 0.000 description 3
- 230000002401 inhibitory effect Effects 0.000 description 3
- 230000005764 inhibitory process Effects 0.000 description 3
- 238000002955 isolation Methods 0.000 description 3
- 239000003446 ligand Substances 0.000 description 3
- 239000007788 liquid Substances 0.000 description 3
- 238000005259 measurement Methods 0.000 description 3
- 239000002245 particle Substances 0.000 description 3
- 239000011148 porous material Substances 0.000 description 3
- 239000001103 potassium chloride Substances 0.000 description 3
- 235000011164 potassium chloride Nutrition 0.000 description 3
- 229910000160 potassium phosphate Inorganic materials 0.000 description 3
- 235000011009 potassium phosphates Nutrition 0.000 description 3
- 239000000843 powder Substances 0.000 description 3
- 239000012460 protein solution Substances 0.000 description 3
- ZAHRKKWIAAJSAO-UHFFFAOYSA-N rapamycin Natural products COCC(O)C(=C/C(C)C(=O)CC(OC(=O)C1CCCCN1C(=O)C(=O)C2(O)OC(CC(OC)C(=CC=CC=CC(C)CC(C)C(=O)C)C)CCC2C)C(C)CC3CCC(O)C(C3)OC)C ZAHRKKWIAAJSAO-UHFFFAOYSA-N 0.000 description 3
- 230000002441 reversible effect Effects 0.000 description 3
- 238000000926 separation method Methods 0.000 description 3
- 229960002930 sirolimus Drugs 0.000 description 3
- QFJCIRLUMZQUOT-HPLJOQBZSA-N sirolimus Chemical compound C1C[C@@H](O)[C@H](OC)C[C@@H]1C[C@@H](C)[C@H]1OC(=O)[C@@H]2CCCCN2C(=O)C(=O)[C@](O)(O2)[C@H](C)CC[C@H]2C[C@H](OC)/C(C)=C/C=C/C=C/[C@@H](C)C[C@@H](C)C(=O)[C@H](OC)[C@H](O)/C(C)=C/[C@@H](C)C(=O)C1 QFJCIRLUMZQUOT-HPLJOQBZSA-N 0.000 description 3
- 210000004989 spleen cell Anatomy 0.000 description 3
- 238000010186 staining Methods 0.000 description 3
- 238000003860 storage Methods 0.000 description 3
- 229940104230 thymidine Drugs 0.000 description 3
- 238000005406 washing Methods 0.000 description 3
- NFGXHKASABOEEW-UHFFFAOYSA-N 1-methylethyl 11-methoxy-3,7,11-trimethyl-2,4-dodecadienoate Chemical compound COC(C)(C)CCCC(C)CC=CC(C)=CC(=O)OC(C)C NFGXHKASABOEEW-UHFFFAOYSA-N 0.000 description 2
- XKRFYHLGVUSROY-UHFFFAOYSA-N Argon Chemical compound [Ar] XKRFYHLGVUSROY-UHFFFAOYSA-N 0.000 description 2
- DWRXFEITVBNRMK-UHFFFAOYSA-N Beta-D-1-Arabinofuranosylthymine Natural products O=C1NC(=O)C(C)=CN1C1C(O)C(O)C(CO)O1 DWRXFEITVBNRMK-UHFFFAOYSA-N 0.000 description 2
- 238000011735 C3H mouse Methods 0.000 description 2
- 108020004705 Codon Proteins 0.000 description 2
- 102000003712 Complement factor B Human genes 0.000 description 2
- 108090000056 Complement factor B Proteins 0.000 description 2
- 101150074155 DHFR gene Proteins 0.000 description 2
- 108010017826 DNA Polymerase I Proteins 0.000 description 2
- 102000004594 DNA Polymerase I Human genes 0.000 description 2
- 108010024212 E-Selectin Proteins 0.000 description 2
- 102100023471 E-selectin Human genes 0.000 description 2
- 241000588724 Escherichia coli Species 0.000 description 2
- 108090000270 Ficain Proteins 0.000 description 2
- 108090000288 Glycoproteins Proteins 0.000 description 2
- 102000003886 Glycoproteins Human genes 0.000 description 2
- ZRALSGWEFCBTJO-UHFFFAOYSA-N Guanidine Chemical compound NC(N)=N ZRALSGWEFCBTJO-UHFFFAOYSA-N 0.000 description 2
- 101000840258 Homo sapiens Immunoglobulin J chain Proteins 0.000 description 2
- 108060003951 Immunoglobulin Proteins 0.000 description 2
- 102000010789 Interleukin-2 Receptors Human genes 0.000 description 2
- 108010038453 Interleukin-2 Receptors Proteins 0.000 description 2
- XUJNEKJLAYXESH-REOHCLBHSA-N L-Cysteine Chemical compound SC[C@H](N)C(O)=O XUJNEKJLAYXESH-REOHCLBHSA-N 0.000 description 2
- 108700018351 Major Histocompatibility Complex Proteins 0.000 description 2
- 241000699673 Mesocricetus auratus Species 0.000 description 2
- 101000966481 Mus musculus Dihydrofolate reductase Proteins 0.000 description 2
- 101710135898 Myc proto-oncogene protein Proteins 0.000 description 2
- 102100038895 Myc proto-oncogene protein Human genes 0.000 description 2
- 108091034117 Oligonucleotide Proteins 0.000 description 2
- 108010035766 P-Selectin Proteins 0.000 description 2
- 102100023472 P-selectin Human genes 0.000 description 2
- 229920001213 Polysorbate 20 Polymers 0.000 description 2
- 239000004365 Protease Substances 0.000 description 2
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 description 2
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 description 2
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 2
- 108010029180 Sialic Acid Binding Ig-like Lectin 3 Proteins 0.000 description 2
- 102000001555 Sialic Acid Binding Ig-like Lectin 3 Human genes 0.000 description 2
- 101710150448 Transcriptional regulator Myc Proteins 0.000 description 2
- 108010027570 Xanthine phosphoribosyltransferase Proteins 0.000 description 2
- JLCPHMBAVCMARE-UHFFFAOYSA-N [3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-hydroxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methyl [5-(6-aminopurin-9-yl)-2-(hydroxymethyl)oxolan-3-yl] hydrogen phosphate Polymers Cc1cn(C2CC(OP(O)(=O)OCC3OC(CC3OP(O)(=O)OCC3OC(CC3O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c3nc(N)[nH]c4=O)C(COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3CO)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cc(C)c(=O)[nH]c3=O)n3cc(C)c(=O)[nH]c3=O)n3ccc(N)nc3=O)n3cc(C)c(=O)[nH]c3=O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)O2)c(=O)[nH]c1=O JLCPHMBAVCMARE-UHFFFAOYSA-N 0.000 description 2
- 230000003321 amplification Effects 0.000 description 2
- 210000004102 animal cell Anatomy 0.000 description 2
- 210000003719 b-lymphocyte Anatomy 0.000 description 2
- IQFYYKKMVGJFEH-UHFFFAOYSA-N beta-L-thymidine Natural products O=C1NC(=O)C(C)=CN1C1OC(CO)C(O)C1 IQFYYKKMVGJFEH-UHFFFAOYSA-N 0.000 description 2
- 230000005540 biological transmission Effects 0.000 description 2
- 230000000903 blocking effect Effects 0.000 description 2
- 238000012512 characterization method Methods 0.000 description 2
- 238000007385 chemical modification Methods 0.000 description 2
- 239000003795 chemical substances by application Substances 0.000 description 2
- 230000002860 competitive effect Effects 0.000 description 2
- 239000012228 culture supernatant Substances 0.000 description 2
- 229960002433 cysteine Drugs 0.000 description 2
- 238000013461 design Methods 0.000 description 2
- 238000011161 development Methods 0.000 description 2
- DOIRQSBPFJWKBE-UHFFFAOYSA-N dibutyl phthalate Chemical compound CCCCOC(=O)C1=CC=CC=C1C(=O)OCCCC DOIRQSBPFJWKBE-UHFFFAOYSA-N 0.000 description 2
- 238000010790 dilution Methods 0.000 description 2
- 239000012895 dilution Substances 0.000 description 2
- 238000004520 electroporation Methods 0.000 description 2
- 238000010828 elution Methods 0.000 description 2
- POTUGHMKJGOKRI-UHFFFAOYSA-N ficin Chemical compound FI=CI=N POTUGHMKJGOKRI-UHFFFAOYSA-N 0.000 description 2
- 235000019836 ficin Nutrition 0.000 description 2
- 239000012737 fresh medium Substances 0.000 description 2
- 238000002523 gelfiltration Methods 0.000 description 2
- 239000011544 gradient gel Substances 0.000 description 2
- 230000008105 immune reaction Effects 0.000 description 2
- 230000028993 immune response Effects 0.000 description 2
- 238000003125 immunofluorescent labeling Methods 0.000 description 2
- 102000018358 immunoglobulin Human genes 0.000 description 2
- 238000007918 intramuscular administration Methods 0.000 description 2
- 238000001990 intravenous administration Methods 0.000 description 2
- 239000000463 material Substances 0.000 description 2
- 239000000178 monomer Substances 0.000 description 2
- 230000000263 nonmitogenic effect Effects 0.000 description 2
- 238000003199 nucleic acid amplification method Methods 0.000 description 2
- 150000007523 nucleic acids Chemical group 0.000 description 2
- 230000037361 pathway Effects 0.000 description 2
- 239000013600 plasmid vector Substances 0.000 description 2
- 239000000256 polyoxyethylene sorbitan monolaurate Substances 0.000 description 2
- 235000010486 polyoxyethylene sorbitan monolaurate Nutrition 0.000 description 2
- 210000002966 serum Anatomy 0.000 description 2
- 239000007787 solid Substances 0.000 description 2
- 230000004936 stimulating effect Effects 0.000 description 2
- 238000007920 subcutaneous administration Methods 0.000 description 2
- 239000000126 substance Substances 0.000 description 2
- 230000020382 suppression by virus of host antigen processing and presentation of peptide antigen via MHC class I Effects 0.000 description 2
- 230000001225 therapeutic effect Effects 0.000 description 2
- 238000004448 titration Methods 0.000 description 2
- 238000001890 transfection Methods 0.000 description 2
- 230000009261 transgenic effect Effects 0.000 description 2
- 230000014616 translation Effects 0.000 description 2
- 238000005199 ultracentrifugation Methods 0.000 description 2
- 239000013603 viral vector Substances 0.000 description 2
- DGVVWUTYPXICAM-UHFFFAOYSA-N β‐Mercaptoethanol Chemical compound OCCS DGVVWUTYPXICAM-UHFFFAOYSA-N 0.000 description 2
- 102000040650 (ribonucleotides)n+m Human genes 0.000 description 1
- OWEGMIWEEQEYGQ-UHFFFAOYSA-N 100676-05-9 Natural products OC1C(O)C(O)C(CO)OC1OCC1C(O)C(O)C(O)C(OC2C(OC(O)C(O)C2O)CO)O1 OWEGMIWEEQEYGQ-UHFFFAOYSA-N 0.000 description 1
- QKNYBSVHEMOAJP-UHFFFAOYSA-N 2-amino-2-(hydroxymethyl)propane-1,3-diol;hydron;chloride Chemical compound Cl.OCC(N)(CO)CO QKNYBSVHEMOAJP-UHFFFAOYSA-N 0.000 description 1
- ODHCTXKNWHHXJC-VKHMYHEASA-N 5-oxo-L-proline Chemical compound OC(=O)[C@@H]1CCC(=O)N1 ODHCTXKNWHHXJC-VKHMYHEASA-N 0.000 description 1
- 208000030507 AIDS Diseases 0.000 description 1
- 108700028369 Alleles Proteins 0.000 description 1
- 108090000915 Aminopeptidases Proteins 0.000 description 1
- 102000004400 Aminopeptidases Human genes 0.000 description 1
- 241000203069 Archaea Species 0.000 description 1
- 240000003291 Armoracia rusticana Species 0.000 description 1
- 235000011330 Armoracia rusticana Nutrition 0.000 description 1
- 208000023275 Autoimmune disease Diseases 0.000 description 1
- 241000894006 Bacteria Species 0.000 description 1
- 101000852101 Bombyx mori DNA topoisomerase 2 Proteins 0.000 description 1
- 102000001902 CC Chemokines Human genes 0.000 description 1
- 108010040471 CC Chemokines Proteins 0.000 description 1
- GDOPTJXRTPNYNR-UHFFFAOYSA-N CC1CCCC1 Chemical compound CC1CCCC1 GDOPTJXRTPNYNR-UHFFFAOYSA-N 0.000 description 1
- 108010029697 CD40 Ligand Proteins 0.000 description 1
- 101150013553 CD40 gene Proteins 0.000 description 1
- 102000008186 Collagen Human genes 0.000 description 1
- 108010035532 Collagen Proteins 0.000 description 1
- 108091035707 Consensus sequence Proteins 0.000 description 1
- 229930105110 Cyclosporin A Natural products 0.000 description 1
- PMATZTZNYRCHOR-CGLBZJNRSA-N Cyclosporin A Chemical compound CC[C@@H]1NC(=O)[C@H]([C@H](O)[C@H](C)C\C=C\C)N(C)C(=O)[C@H](C(C)C)N(C)C(=O)[C@H](CC(C)C)N(C)C(=O)[C@H](CC(C)C)N(C)C(=O)[C@@H](C)NC(=O)[C@H](C)NC(=O)[C@H](CC(C)C)N(C)C(=O)[C@H](C(C)C)NC(=O)[C@H](CC(C)C)N(C)C(=O)CN(C)C1=O PMATZTZNYRCHOR-CGLBZJNRSA-N 0.000 description 1
- 108010036949 Cyclosporine Proteins 0.000 description 1
- 102000053602 DNA Human genes 0.000 description 1
- 206010012438 Dermatitis atopic Diseases 0.000 description 1
- KCXVZYZYPLLWCC-UHFFFAOYSA-N EDTA Chemical compound OC(=O)CN(CC(O)=O)CCN(CC(O)=O)CC(O)=O KCXVZYZYPLLWCC-UHFFFAOYSA-N 0.000 description 1
- 238000008157 ELISA kit Methods 0.000 description 1
- 208000009386 Experimental Arthritis Diseases 0.000 description 1
- 206010015866 Extravasation Diseases 0.000 description 1
- 102100026973 Heat shock protein 75 kDa, mitochondrial Human genes 0.000 description 1
- 241000282412 Homo Species 0.000 description 1
- 101000935587 Homo sapiens Flavin reductase (NADPH) Proteins 0.000 description 1
- 101000914484 Homo sapiens T-lymphocyte activation antigen CD80 Proteins 0.000 description 1
- 102000008100 Human Serum Albumin Human genes 0.000 description 1
- 108091006905 Human Serum Albumin Proteins 0.000 description 1
- 206010061218 Inflammation Diseases 0.000 description 1
- 108090001090 Lectins Proteins 0.000 description 1
- 102000004856 Lectins Human genes 0.000 description 1
- 239000012097 Lipofectamine 2000 Substances 0.000 description 1
- GUBGYTABKSRVRQ-PICCSMPSSA-N Maltose Natural products O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CO)O[C@@H]1O[C@@H]1[C@@H](CO)OC(O)[C@H](O)[C@H]1O GUBGYTABKSRVRQ-PICCSMPSSA-N 0.000 description 1
- 241000124008 Mammalia Species 0.000 description 1
- 101100370002 Mus musculus Tnfsf14 gene Proteins 0.000 description 1
- CHJJGSNFBQVOTG-UHFFFAOYSA-N N-methyl-guanidine Natural products CNC(N)=N CHJJGSNFBQVOTG-UHFFFAOYSA-N 0.000 description 1
- 206010028980 Neoplasm Diseases 0.000 description 1
- ODHCTXKNWHHXJC-GSVOUGTGSA-N Pyroglutamic acid Natural products OC(=O)[C@H]1CCC(=O)N1 ODHCTXKNWHHXJC-GSVOUGTGSA-N 0.000 description 1
- 108090000919 Pyroglutamyl-Peptidase I Proteins 0.000 description 1
- 241000283984 Rodentia Species 0.000 description 1
- PMZURENOXWZQFD-UHFFFAOYSA-L Sodium Sulfate Chemical compound [Na+].[Na+].[O-]S([O-])(=O)=O PMZURENOXWZQFD-UHFFFAOYSA-L 0.000 description 1
- 102100027222 T-lymphocyte activation antigen CD80 Human genes 0.000 description 1
- QJJXYPPXXYFBGM-LFZNUXCKSA-N Tacrolimus Chemical compound C1C[C@@H](O)[C@H](OC)C[C@@H]1\C=C(/C)[C@@H]1[C@H](C)[C@@H](O)CC(=O)[C@H](CC=C)/C=C(C)/C[C@H](C)C[C@H](OC)[C@H]([C@H](C[C@H]2C)OC)O[C@@]2(O)C(=O)C(=O)N2CCCC[C@H]2C(=O)O1 QJJXYPPXXYFBGM-LFZNUXCKSA-N 0.000 description 1
- 108010006785 Taq Polymerase Proteins 0.000 description 1
- 101710204707 Transforming growth factor-beta receptor-associated protein 1 Proteins 0.000 description 1
- 102100040245 Tumor necrosis factor receptor superfamily member 5 Human genes 0.000 description 1
- 206010067584 Type 1 diabetes mellitus Diseases 0.000 description 1
- 230000001594 aberrant effect Effects 0.000 description 1
- ODHCTXKNWHHXJC-UHFFFAOYSA-N acide pyroglutamique Natural products OC(=O)C1CCC(=O)N1 ODHCTXKNWHHXJC-UHFFFAOYSA-N 0.000 description 1
- 230000003213 activating effect Effects 0.000 description 1
- 238000005377 adsorption chromatography Methods 0.000 description 1
- 239000000556 agonist Substances 0.000 description 1
- 230000001270 agonistic effect Effects 0.000 description 1
- 230000000961 alloantigen Effects 0.000 description 1
- 230000000735 allogeneic effect Effects 0.000 description 1
- 125000000539 amino acid group Chemical group 0.000 description 1
- BFNBIHQBYMNNAN-UHFFFAOYSA-N ammonium sulfate Chemical compound N.N.OS(O)(=O)=O BFNBIHQBYMNNAN-UHFFFAOYSA-N 0.000 description 1
- 229910052921 ammonium sulfate Inorganic materials 0.000 description 1
- 235000011130 ammonium sulphate Nutrition 0.000 description 1
- 230000003042 antagnostic effect Effects 0.000 description 1
- 239000003242 anti bacterial agent Substances 0.000 description 1
- 230000003172 anti-dna Effects 0.000 description 1
- 229940088710 antibiotic agent Drugs 0.000 description 1
- 230000000890 antigenic effect Effects 0.000 description 1
- 230000006907 apoptotic process Effects 0.000 description 1
- 229910052786 argon Inorganic materials 0.000 description 1
- 208000006673 asthma Diseases 0.000 description 1
- 201000008937 atopic dermatitis Diseases 0.000 description 1
- OHDRQQURAXLVGJ-HLVWOLMTSA-N azane;(2e)-3-ethyl-2-[(e)-(3-ethyl-6-sulfo-1,3-benzothiazol-2-ylidene)hydrazinylidene]-1,3-benzothiazole-6-sulfonic acid Chemical compound [NH4+].[NH4+].S/1C2=CC(S([O-])(=O)=O)=CC=C2N(CC)C\1=N/N=C1/SC2=CC(S([O-])(=O)=O)=CC=C2N1CC OHDRQQURAXLVGJ-HLVWOLMTSA-N 0.000 description 1
- 230000001580 bacterial effect Effects 0.000 description 1
- 239000012148 binding buffer Substances 0.000 description 1
- 230000004071 biological effect Effects 0.000 description 1
- 230000015572 biosynthetic process Effects 0.000 description 1
- 210000004369 blood Anatomy 0.000 description 1
- 239000008280 blood Substances 0.000 description 1
- 238000009835 boiling Methods 0.000 description 1
- 210000001185 bone marrow Anatomy 0.000 description 1
- 210000002798 bone marrow cell Anatomy 0.000 description 1
- 238000010322 bone marrow transplantation Methods 0.000 description 1
- 201000011510 cancer Diseases 0.000 description 1
- 239000002775 capsule Substances 0.000 description 1
- 150000001720 carbohydrates Chemical class 0.000 description 1
- 235000014633 carbohydrates Nutrition 0.000 description 1
- 230000015556 catabolic process Effects 0.000 description 1
- 230000001413 cellular effect Effects 0.000 description 1
- 229960001265 ciclosporin Drugs 0.000 description 1
- 229920001436 collagen Polymers 0.000 description 1
- 150000001875 compounds Chemical class 0.000 description 1
- 238000004590 computer program Methods 0.000 description 1
- 238000007796 conventional method Methods 0.000 description 1
- 210000004087 cornea Anatomy 0.000 description 1
- 230000000139 costimulatory effect Effects 0.000 description 1
- 235000018417 cysteine Nutrition 0.000 description 1
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 1
- 230000003247 decreasing effect Effects 0.000 description 1
- 230000002950 deficient Effects 0.000 description 1
- 238000006731 degradation reaction Methods 0.000 description 1
- 238000000502 dialysis Methods 0.000 description 1
- 239000003085 diluting agent Substances 0.000 description 1
- SWSQBOPZIKWTGO-UHFFFAOYSA-N dimethylaminoamidine Natural products CN(C)C(N)=N SWSQBOPZIKWTGO-UHFFFAOYSA-N 0.000 description 1
- 201000010099 disease Diseases 0.000 description 1
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 1
- 238000004090 dissolution Methods 0.000 description 1
- 238000009826 distribution Methods 0.000 description 1
- 239000003651 drinking water Substances 0.000 description 1
- 235000020188 drinking water Nutrition 0.000 description 1
- 238000001962 electrophoresis Methods 0.000 description 1
- 239000000839 emulsion Substances 0.000 description 1
- 239000008393 encapsulating agent Substances 0.000 description 1
- 210000003527 eukaryotic cell Anatomy 0.000 description 1
- 230000001747 exhibiting effect Effects 0.000 description 1
- 238000000605 extraction Methods 0.000 description 1
- 230000036251 extravasation Effects 0.000 description 1
- 239000003889 eye drop Substances 0.000 description 1
- 229940012356 eye drops Drugs 0.000 description 1
- 239000003885 eye ointment Substances 0.000 description 1
- 239000007850 fluorescent dye Substances 0.000 description 1
- 231100000221 frame shift mutation induction Toxicity 0.000 description 1
- 230000037433 frameshift Effects 0.000 description 1
- 230000006870 function Effects 0.000 description 1
- 230000002538 fungal effect Effects 0.000 description 1
- 108020001507 fusion proteins Proteins 0.000 description 1
- 102000037865 fusion proteins Human genes 0.000 description 1
- 238000005227 gel permeation chromatography Methods 0.000 description 1
- ZDXPYRJPNDTMRX-UHFFFAOYSA-N glutamine Natural products OC(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-N 0.000 description 1
- 230000013595 glycosylation Effects 0.000 description 1
- 238000006206 glycosylation reaction Methods 0.000 description 1
- 208000024908 graft versus host disease Diseases 0.000 description 1
- 239000008187 granular material Substances 0.000 description 1
- 210000002216 heart Anatomy 0.000 description 1
- -1 human serum albumin Chemical compound 0.000 description 1
- 230000002209 hydrophobic effect Effects 0.000 description 1
- 208000026278 immune system disease Diseases 0.000 description 1
- 230000016784 immunoglobulin production Effects 0.000 description 1
- 230000000091 immunopotentiator Effects 0.000 description 1
- 229940125721 immunosuppressive agent Drugs 0.000 description 1
- 239000007943 implant Substances 0.000 description 1
- 230000001976 improved effect Effects 0.000 description 1
- 238000010348 incorporation Methods 0.000 description 1
- 230000006698 induction Effects 0.000 description 1
- 208000015181 infectious disease Diseases 0.000 description 1
- 230000004054 inflammatory process Effects 0.000 description 1
- 238000001802 infusion Methods 0.000 description 1
- 239000003112 inhibitor Substances 0.000 description 1
- 230000010354 integration Effects 0.000 description 1
- 238000010255 intramuscular injection Methods 0.000 description 1
- 239000007927 intramuscular injection Substances 0.000 description 1
- 238000007912 intraperitoneal administration Methods 0.000 description 1
- 238000010253 intravenous injection Methods 0.000 description 1
- JDNTWHVOXJZDSN-UHFFFAOYSA-N iodoacetic acid Chemical compound OC(=O)CI JDNTWHVOXJZDSN-UHFFFAOYSA-N 0.000 description 1
- 238000004255 ion exchange chromatography Methods 0.000 description 1
- 210000003734 kidney Anatomy 0.000 description 1
- 239000002523 lectin Substances 0.000 description 1
- 230000023404 leukocyte cell-cell adhesion Effects 0.000 description 1
- 239000002502 liposome Substances 0.000 description 1
- 210000004185 liver Anatomy 0.000 description 1
- 210000004072 lung Anatomy 0.000 description 1
- 210000004698 lymphocyte Anatomy 0.000 description 1
- 239000008176 lyophilized powder Substances 0.000 description 1
- 210000004962 mammalian cell Anatomy 0.000 description 1
- 238000013507 mapping Methods 0.000 description 1
- 201000006512 mast cell neoplasm Diseases 0.000 description 1
- 208000006971 mastocytoma Diseases 0.000 description 1
- 230000001404 mediated effect Effects 0.000 description 1
- 238000012986 modification Methods 0.000 description 1
- 230000004048 modification Effects 0.000 description 1
- 238000010369 molecular cloning Methods 0.000 description 1
- 238000000329 molecular dynamics simulation Methods 0.000 description 1
- 238000012544 monitoring process Methods 0.000 description 1
- 210000001616 monocyte Anatomy 0.000 description 1
- 201000006417 multiple sclerosis Diseases 0.000 description 1
- 210000003205 muscle Anatomy 0.000 description 1
- 206010028417 myasthenia gravis Diseases 0.000 description 1
- 230000010807 negative regulation of binding Effects 0.000 description 1
- 210000005036 nerve Anatomy 0.000 description 1
- 102000039446 nucleic acids Human genes 0.000 description 1
- 108020004707 nucleic acids Proteins 0.000 description 1
- 229920001778 nylon Polymers 0.000 description 1
- 239000002674 ointment Substances 0.000 description 1
- 239000004006 olive oil Substances 0.000 description 1
- 235000008390 olive oil Nutrition 0.000 description 1
- 230000003287 optical effect Effects 0.000 description 1
- 230000003204 osmotic effect Effects 0.000 description 1
- 229940046781 other immunosuppressants in atc Drugs 0.000 description 1
- 210000000496 pancreas Anatomy 0.000 description 1
- 229950008882 polysorbate Drugs 0.000 description 1
- 229920000136 polysorbate Polymers 0.000 description 1
- 230000003389 potentiating effect Effects 0.000 description 1
- 238000001556 precipitation Methods 0.000 description 1
- 229940072288 prograf Drugs 0.000 description 1
- 230000035755 proliferation Effects 0.000 description 1
- 230000002035 prolonged effect Effects 0.000 description 1
- 238000000164 protein isolation Methods 0.000 description 1
- 238000003259 recombinant expression Methods 0.000 description 1
- 230000006798 recombination Effects 0.000 description 1
- 238000005215 recombination Methods 0.000 description 1
- 238000001953 recrystallisation Methods 0.000 description 1
- 230000009467 reduction Effects 0.000 description 1
- 230000010076 replication Effects 0.000 description 1
- QEVHRUUCFGRFIF-MDEJGZGSSA-N reserpine Chemical compound O([C@H]1[C@@H]([C@H]([C@H]2C[C@@H]3C4=C(C5=CC=C(OC)C=C5N4)CCN3C[C@H]2C1)C(=O)OC)OC)C(=O)C1=CC(OC)=C(OC)C(OC)=C1 QEVHRUUCFGRFIF-MDEJGZGSSA-N 0.000 description 1
- 108091008146 restriction endonucleases Proteins 0.000 description 1
- 206010039073 rheumatoid arthritis Diseases 0.000 description 1
- 238000005185 salting out Methods 0.000 description 1
- 150000003839 salts Chemical class 0.000 description 1
- 238000012772 sequence design Methods 0.000 description 1
- 230000008054 signal transmission Effects 0.000 description 1
- 238000001542 size-exclusion chromatography Methods 0.000 description 1
- 210000003491 skin Anatomy 0.000 description 1
- 210000000813 small intestine Anatomy 0.000 description 1
- 239000001488 sodium phosphate Substances 0.000 description 1
- 229910000162 sodium phosphate Inorganic materials 0.000 description 1
- 229910052938 sodium sulfate Inorganic materials 0.000 description 1
- 235000011152 sodium sulphate Nutrition 0.000 description 1
- 239000002904 solvent Substances 0.000 description 1
- 230000009870 specific binding Effects 0.000 description 1
- 239000007921 spray Substances 0.000 description 1
- 239000003381 stabilizer Substances 0.000 description 1
- 238000007619 statistical method Methods 0.000 description 1
- 238000010254 subcutaneous injection Methods 0.000 description 1
- 239000007929 subcutaneous injection Substances 0.000 description 1
- 239000000758 substrate Substances 0.000 description 1
- 150000008163 sugars Chemical class 0.000 description 1
- 239000000829 suppository Substances 0.000 description 1
- 239000004094 surface-active agent Substances 0.000 description 1
- 238000001356 surgical procedure Methods 0.000 description 1
- 239000000725 suspension Substances 0.000 description 1
- 230000002459 sustained effect Effects 0.000 description 1
- 208000024891 symptom Diseases 0.000 description 1
- 201000000596 systemic lupus erythematosus Diseases 0.000 description 1
- 239000003826 tablet Substances 0.000 description 1
- 210000000115 thoracic cavity Anatomy 0.000 description 1
- 230000005030 transcription termination Effects 0.000 description 1
- 238000013519 translation Methods 0.000 description 1
- RYFMWSXOAZQYPI-UHFFFAOYSA-K trisodium phosphate Chemical compound [Na+].[Na+].[Na+].[O-]P([O-])([O-])=O RYFMWSXOAZQYPI-UHFFFAOYSA-K 0.000 description 1
- 238000000108 ultra-filtration Methods 0.000 description 1
- 230000003612 virological effect Effects 0.000 description 1
- 239000011534 wash buffer Substances 0.000 description 1
Images
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/18—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans
- C07K16/28—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/18—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans
- C07K16/28—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants
- C07K16/2803—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants against the immunoglobulin superfamily
- C07K16/2818—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants against the immunoglobulin superfamily against CD28 or CD152
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P37/00—Drugs for immunological or allergic disorders
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P37/00—Drugs for immunological or allergic disorders
- A61P37/02—Immunomodulators
- A61P37/06—Immunosuppressants, e.g. drugs for graft rejection
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P41/00—Drugs used in surgical methods, e.g. surgery adjuvants for preventing adhesion or for vitreum substitution
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P43/00—Drugs for specific purposes, not provided for in groups A61P1/00-A61P41/00
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K39/00—Medicinal preparations containing antigens or antibodies
- A61K2039/505—Medicinal preparations containing antigens or antibodies comprising antibodies
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/20—Immunoglobulins specific features characterized by taxonomic origin
- C07K2317/24—Immunoglobulins specific features characterized by taxonomic origin containing regions, domains or residues from different species, e.g. chimeric, humanized or veneered
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/50—Immunoglobulins specific features characterized by immunoglobulin fragments
- C07K2317/54—F(ab')2
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/50—Immunoglobulins specific features characterized by immunoglobulin fragments
- C07K2317/55—Fab or Fab'
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/50—Immunoglobulins specific features characterized by immunoglobulin fragments
- C07K2317/56—Immunoglobulins specific features characterized by immunoglobulin fragments variable (Fv) region, i.e. VH and/or VL
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
Landscapes
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Immunology (AREA)
- Organic Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Medicinal Chemistry (AREA)
- Life Sciences & Earth Sciences (AREA)
- Engineering & Computer Science (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Public Health (AREA)
- Pharmacology & Pharmacy (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Animal Behavior & Ethology (AREA)
- General Chemical & Material Sciences (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Veterinary Medicine (AREA)
- Biophysics (AREA)
- Biochemistry (AREA)
- Genetics & Genomics (AREA)
- Molecular Biology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Transplantation (AREA)
- Surgery (AREA)
- Peptides Or Proteins (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
- Medicines Containing Material From Animals Or Micro-Organisms (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US25515500P | 2000-12-14 | 2000-12-14 | |
| PCT/US2001/047955 WO2002047721A1 (en) | 2000-12-14 | 2001-12-14 | Silensed anti-cd28 antibodies and use thereof |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| JP2004515243A true JP2004515243A (ja) | 2004-05-27 |
Family
ID=22967074
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP2002549291A Withdrawn JP2004515243A (ja) | 2000-12-14 | 2001-12-14 | サイレント抗cd28抗体およびその使用 |
Country Status (18)
| Country | Link |
|---|---|
| EP (1) | EP1341553A4 (es) |
| JP (1) | JP2004515243A (es) |
| KR (1) | KR20040020866A (es) |
| CN (1) | CN1272345C (es) |
| AR (1) | AR031924A1 (es) |
| AU (2) | AU2608602A (es) |
| BR (1) | BR0116686A (es) |
| CA (1) | CA2432736A1 (es) |
| CZ (1) | CZ20031909A3 (es) |
| HU (1) | HUP0400697A3 (es) |
| IL (1) | IL156262A0 (es) |
| MX (1) | MXPA03005327A (es) |
| NO (1) | NO20032542L (es) |
| NZ (1) | NZ526569A (es) |
| PL (1) | PL363239A1 (es) |
| RU (1) | RU2261723C2 (es) |
| WO (1) | WO2002047721A1 (es) |
| ZA (1) | ZA200305384B (es) |
Cited By (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2013519389A (ja) * | 2010-02-18 | 2013-05-30 | エフィミュヌ | 抗cd28ヒト化抗体 |
Families Citing this family (24)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US7531168B2 (en) | 2001-02-16 | 2009-05-12 | Genetics Institute Llc | Method for downmodulating immune response in type I diabetes |
| US20080095774A1 (en) * | 2001-02-16 | 2008-04-24 | Wyeth | Agents and Methods for Specifically Blocking CD28-Mediated Signaling |
| ES2776657T3 (es) | 2005-06-14 | 2020-07-31 | Amgen Inc | Formulaciones de proteínas autotamponantes |
| FR2951176A1 (fr) * | 2009-10-09 | 2011-04-15 | Tcl Pharma | Ligands monovalents du recepteur cd28 humain |
| WO2018075818A1 (en) | 2016-10-21 | 2018-04-26 | Amgen Inc. | Pharmaceutical formulations and methods of making the same |
| CN112638375A (zh) | 2018-06-15 | 2021-04-09 | 旗舰创业创新五公司 | 通过后细胞信号传导因子的调节来增加免疫活性 |
| JP2022525332A (ja) * | 2019-03-14 | 2022-05-12 | ビオンド バイオロジクス リミテッド | 免疫抑制の方法 |
| MA55805A (fr) | 2019-05-03 | 2022-03-09 | Flagship Pioneering Innovations V Inc | Métodes de modulation de l'activité immunitaire |
| EP4076434A1 (en) | 2019-12-17 | 2022-10-26 | Flagship Pioneering Innovations V, Inc. | Combination anti-cancer therapies with inducers of iron-dependent cellular disassembly |
| CN116096906A (zh) | 2020-06-29 | 2023-05-09 | 旗舰创业创新五公司 | 工程化以促进萨诺传递的病毒及其在治疗癌症中的用途 |
| IL300666A (en) | 2020-08-19 | 2023-04-01 | Xencor Inc | ANTI–CD28 COMPOSITIONS |
| US20220325287A1 (en) | 2021-03-31 | 2022-10-13 | Flagship Pioneering Innovations V, Inc. | Thanotransmission polypeptides and their use in treating cancer |
| JP2024525475A (ja) | 2021-06-29 | 2024-07-12 | フラグシップ パイオニアリング イノベーションズ ブイ,インコーポレーテッド | タノトランスミッションを促進するように操作された免疫細胞及びその使用 |
| KR20240161977A (ko) | 2022-02-23 | 2024-11-13 | 젠코어 인코포레이티드 | 항-CD28 x 항-PSMA 항체 |
| WO2024040194A1 (en) | 2022-08-17 | 2024-02-22 | Capstan Therapeutics, Inc. | Conditioning for in vivo immune cell engineering |
| EP4598946A1 (en) | 2022-10-05 | 2025-08-13 | Flagship Pioneering Innovations V, Inc. | Nucleic acid molecules encoding trif and additionalpolypeptides and their use in treating cancer |
| WO2024148336A1 (en) * | 2023-01-06 | 2024-07-11 | Igm Biosciences, Inc. | T cell costimulatory multimeric binding molecules and uses thereof |
| US20240269251A1 (en) | 2023-01-09 | 2024-08-15 | Flagship Pioneering Innovations V, Inc. | Genetic switches and their use in treating cancer |
| US12311033B2 (en) | 2023-05-31 | 2025-05-27 | Capstan Therapeutics, Inc. | Lipid nanoparticle formulations and compositions |
| US20250127728A1 (en) | 2023-10-05 | 2025-04-24 | Capstan Therapeutics, Inc. | Constrained Ionizable Cationic Lipids and Lipid Nanoparticles |
| WO2025076113A1 (en) | 2023-10-05 | 2025-04-10 | Capstan Therapeutics, Inc. | Ionizable cationic lipids with conserved spacing and lipid nanoparticles |
| US20250302763A1 (en) | 2024-02-22 | 2025-10-02 | Capstan Therapeutics, Inc. | Immune engineering amplification |
| WO2025217454A2 (en) | 2024-04-11 | 2025-10-16 | Capstan Therapeutics, Inc. | Ionizable cationic lipids and lipid nanoparticles |
| WO2025217452A1 (en) | 2024-04-11 | 2025-10-16 | Capstan Therapeutics, Inc. | Constrained ionizable cationic lipids and lipid nanoparticles |
Family Cites Families (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US6641809B1 (en) * | 1990-03-26 | 2003-11-04 | Bristol-Myers Squibb Company | Method of regulating cellular processes mediated by B7 and CD28 |
-
2001
- 2001-12-14 RU RU2003121231/15A patent/RU2261723C2/ru not_active IP Right Cessation
- 2001-12-14 CZ CZ20031909A patent/CZ20031909A3/cs unknown
- 2001-12-14 HU HU0400697A patent/HUP0400697A3/hu unknown
- 2001-12-14 BR BR0116686-7A patent/BR0116686A/pt not_active IP Right Cessation
- 2001-12-14 AU AU2608602A patent/AU2608602A/xx active Pending
- 2001-12-14 AR ARP010105828A patent/AR031924A1/es unknown
- 2001-12-14 JP JP2002549291A patent/JP2004515243A/ja not_active Withdrawn
- 2001-12-14 IL IL15626201A patent/IL156262A0/xx unknown
- 2001-12-14 NZ NZ526569A patent/NZ526569A/en unknown
- 2001-12-14 CN CNB018226361A patent/CN1272345C/zh not_active Expired - Fee Related
- 2001-12-14 WO PCT/US2001/047955 patent/WO2002047721A1/en not_active Ceased
- 2001-12-14 EP EP01995504A patent/EP1341553A4/en not_active Withdrawn
- 2001-12-14 MX MXPA03005327A patent/MXPA03005327A/es unknown
- 2001-12-14 KR KR10-2003-7007798A patent/KR20040020866A/ko not_active Ceased
- 2001-12-14 CA CA002432736A patent/CA2432736A1/en not_active Abandoned
- 2001-12-14 AU AU2002226086A patent/AU2002226086C1/en not_active Ceased
- 2001-12-14 PL PL01363239A patent/PL363239A1/xx not_active Application Discontinuation
-
2003
- 2003-06-05 NO NO20032542A patent/NO20032542L/no not_active Application Discontinuation
- 2003-07-11 ZA ZA200305384A patent/ZA200305384B/en unknown
Cited By (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2013519389A (ja) * | 2010-02-18 | 2013-05-30 | エフィミュヌ | 抗cd28ヒト化抗体 |
Also Published As
| Publication number | Publication date |
|---|---|
| CZ20031909A3 (cs) | 2003-11-12 |
| EP1341553A1 (en) | 2003-09-10 |
| HUP0400697A2 (hu) | 2004-06-28 |
| RU2261723C2 (ru) | 2005-10-10 |
| CN1272345C (zh) | 2006-08-30 |
| CN1489473A (zh) | 2004-04-14 |
| NO20032542D0 (no) | 2003-06-05 |
| ZA200305384B (en) | 2004-10-11 |
| HUP0400697A3 (en) | 2007-05-02 |
| CA2432736A1 (en) | 2002-06-20 |
| BR0116686A (pt) | 2003-12-30 |
| AR031924A1 (es) | 2003-10-08 |
| NO20032542L (no) | 2003-08-07 |
| AU2608602A (en) | 2002-06-24 |
| MXPA03005327A (es) | 2004-12-03 |
| RU2003121231A (ru) | 2005-02-10 |
| WO2002047721A1 (en) | 2002-06-20 |
| EP1341553A4 (en) | 2004-07-28 |
| AU2002226086C1 (en) | 2006-03-09 |
| PL363239A1 (en) | 2004-11-15 |
| IL156262A0 (en) | 2004-01-04 |
| AU2002226086B2 (en) | 2005-08-25 |
| KR20040020866A (ko) | 2004-03-09 |
| NZ526569A (en) | 2005-07-29 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| JP2004515243A (ja) | サイレント抗cd28抗体およびその使用 | |
| TWI708787B (zh) | Pd-1促效劑抗體及其用途 | |
| JP6621778B2 (ja) | IL7受容体のα鎖に対する抗体‐薬剤候補物質の製造におけるこれらの使用 | |
| KR100191152B1 (ko) | Cd4 특이적 재조합 항체 | |
| EP1654286B1 (en) | Humanized anti-cd4 antibody with immunosuppressive properties | |
| AU2002226086A1 (en) | Silensed anti-CD28 antibodies and use thereof | |
| EP0617126A2 (en) | Polypeptide capable of inhibiting the binding bewteen human IL-6 and its receptor | |
| KR20170057298A (ko) | Cd19에 특이적인 항체 및 키메라 항원 수용체 | |
| AU2020286444B2 (en) | PD-1 agonist and method of using same | |
| JP2002540764A (ja) | B7分子と反応するヒト化免疫グロブリンおよびそれを用いた治療方法 | |
| JP7278623B2 (ja) | 抗cd27抗体およびその使用 | |
| US20040116675A1 (en) | Silenced anti-cd28 antibodies and use thereof | |
| EP4406970A1 (en) | Monoclonal antibody targeting tigit | |
| US20240269276A1 (en) | Specific binding protein targeting pd-l1 and cd73 | |
| CN116854820B (zh) | Pd-1非阻断性清除抗体及其用途 | |
| HK1088337B (en) | Humanized anti-cd4 antibody with immunosuppressive properties |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| A621 | Written request for application examination |
Free format text: JAPANESE INTERMEDIATE CODE: A621 Effective date: 20041124 |
|
| RD01 | Notification of change of attorney |
Free format text: JAPANESE INTERMEDIATE CODE: A7421 Effective date: 20050225 |
|
| A521 | Request for written amendment filed |
Free format text: JAPANESE INTERMEDIATE CODE: A523 Effective date: 20050324 |
|
| A711 | Notification of change in applicant |
Free format text: JAPANESE INTERMEDIATE CODE: A712 Effective date: 20050520 |
|
| A761 | Written withdrawal of application |
Free format text: JAPANESE INTERMEDIATE CODE: A761 Effective date: 20061102 |