CA2096159C - Peptides that induce antibodies which neutralize genetically divergent hiv-1 isolates - Google Patents
Peptides that induce antibodies which neutralize genetically divergent hiv-1 isolates Download PDFInfo
- Publication number
- CA2096159C CA2096159C CA002096159A CA2096159A CA2096159C CA 2096159 C CA2096159 C CA 2096159C CA 002096159 A CA002096159 A CA 002096159A CA 2096159 A CA2096159 A CA 2096159A CA 2096159 C CA2096159 C CA 2096159C
- Authority
- CA
- Canada
- Prior art keywords
- seq
- peptide
- hiv
- type
- antibody
- 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.)
- Expired - Lifetime
Links
- 108090000765 processed proteins & peptides Proteins 0.000 title claims abstract description 122
- 102000004196 processed proteins & peptides Human genes 0.000 title claims abstract description 53
- 241000713772 Human immunodeficiency virus 1 Species 0.000 claims abstract description 71
- 230000003472 neutralizing effect Effects 0.000 claims abstract description 30
- 241000700605 Viruses Species 0.000 claims abstract description 16
- 230000004927 fusion Effects 0.000 claims abstract description 12
- 239000002671 adjuvant Substances 0.000 claims abstract description 11
- 230000028993 immune response Effects 0.000 claims description 13
- 241000712461 unidentified influenza virus Species 0.000 claims description 13
- 230000000890 antigenic effect Effects 0.000 claims description 9
- 229940033332 HIV-1 vaccine Drugs 0.000 claims description 6
- 102000017727 Immunoglobulin Variable Region Human genes 0.000 claims description 5
- 108010067060 Immunoglobulin Variable Region Proteins 0.000 claims description 5
- 108010067390 Viral Proteins Proteins 0.000 claims description 5
- 239000002773 nucleotide Substances 0.000 claims description 3
- 125000003729 nucleotide group Chemical group 0.000 claims description 3
- 102000005720 Glutathione transferase Human genes 0.000 claims description 2
- 108010070675 Glutathione transferase Proteins 0.000 claims description 2
- 108010006232 Neuraminidase Proteins 0.000 claims description 2
- 238000002347 injection Methods 0.000 claims description 2
- 239000007924 injection Substances 0.000 claims description 2
- 102000001706 Immunoglobulin Fab Fragments Human genes 0.000 claims 2
- 108010054477 Immunoglobulin Fab Fragments Proteins 0.000 claims 2
- 102000008394 Immunoglobulin Fragments Human genes 0.000 claims 1
- 108010021625 Immunoglobulin Fragments Proteins 0.000 claims 1
- 241000124008 Mammalia Species 0.000 claims 1
- 102000005348 Neuraminidase Human genes 0.000 claims 1
- 230000002068 genetic effect Effects 0.000 claims 1
- 230000003993 interaction Effects 0.000 claims 1
- 239000000126 substance Substances 0.000 claims 1
- 208000015181 infectious disease Diseases 0.000 abstract description 9
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 abstract description 4
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 abstract description 4
- 210000004027 cell Anatomy 0.000 description 100
- 208000031886 HIV Infections Diseases 0.000 description 66
- 238000000034 method Methods 0.000 description 58
- 210000003463 organelle Anatomy 0.000 description 49
- 108020001507 fusion proteins Proteins 0.000 description 48
- 210000001519 tissue Anatomy 0.000 description 48
- 102000054766 genetic haplotypes Human genes 0.000 description 46
- 108091033319 polynucleotide Proteins 0.000 description 38
- 102000040430 polynucleotide Human genes 0.000 description 38
- 239000002157 polynucleotide Substances 0.000 description 38
- 241000724791 Filamentous phage Species 0.000 description 32
- 150000001413 amino acids Chemical group 0.000 description 31
- 235000001014 amino acid Nutrition 0.000 description 26
- 239000012634 fragment Substances 0.000 description 26
- 102000039446 nucleic acids Human genes 0.000 description 24
- 108020004707 nucleic acids Proteins 0.000 description 24
- 150000007523 nucleic acids Chemical class 0.000 description 24
- 108090000623 proteins and genes Proteins 0.000 description 22
- 230000003053 immunization Effects 0.000 description 18
- 241000699670 Mus sp. Species 0.000 description 16
- 108010092854 aspartyllysine Proteins 0.000 description 16
- 238000002649 immunization Methods 0.000 description 16
- 239000000185 hemagglutinin Substances 0.000 description 13
- ZQNCUVODKOBSSO-XEGUGMAKSA-N Glu-Trp-Ala Chemical compound [H]N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC1=CNC2=C1C=CC=C2)C(=O)N[C@@H](C)C(O)=O ZQNCUVODKOBSSO-XEGUGMAKSA-N 0.000 description 11
- 101710154606 Hemagglutinin Proteins 0.000 description 10
- 101710093908 Outer capsid protein VP4 Proteins 0.000 description 10
- 101710135467 Outer capsid protein sigma-1 Proteins 0.000 description 10
- 101710176177 Protein A56 Proteins 0.000 description 10
- 241000588724 Escherichia coli Species 0.000 description 8
- RVKIPWVMZANZLI-UHFFFAOYSA-N H-Lys-Trp-OH Natural products C1=CC=C2C(CC(NC(=O)C(N)CCCCN)C(O)=O)=CNC2=C1 RVKIPWVMZANZLI-UHFFFAOYSA-N 0.000 description 8
- 239000000427 antigen Substances 0.000 description 8
- 102000036639 antigens Human genes 0.000 description 8
- 108091007433 antigens Proteins 0.000 description 8
- 101800001690 Transmembrane protein gp41 Proteins 0.000 description 7
- 102000037865 fusion proteins Human genes 0.000 description 7
- 230000002163 immunogen Effects 0.000 description 7
- 238000010561 standard procedure Methods 0.000 description 7
- RLFSBAPJTYKSLG-WHFBIAKZSA-N Gly-Ala-Asp Chemical compound NCC(=O)N[C@@H](C)C(=O)N[C@@H](CC(O)=O)C(O)=O RLFSBAPJTYKSLG-WHFBIAKZSA-N 0.000 description 6
- 239000002953 phosphate buffered saline Substances 0.000 description 6
- 208000030507 AIDS Diseases 0.000 description 5
- PJBVXVBTTFZPHJ-GUBZILKMSA-N Glu-Leu-Asp Chemical compound CC(C)C[C@@H](C(=O)N[C@@H](CC(=O)O)C(=O)O)NC(=O)[C@H](CCC(=O)O)N PJBVXVBTTFZPHJ-GUBZILKMSA-N 0.000 description 5
- 241000725303 Human immunodeficiency virus Species 0.000 description 5
- CNXOBMMOYZPPGS-NUTKFTJISA-N Lys-Trp-Ala Chemical compound [H]N[C@@H](CCCCN)C(=O)N[C@@H](CC1=CNC2=C1C=CC=C2)C(=O)N[C@@H](C)C(O)=O CNXOBMMOYZPPGS-NUTKFTJISA-N 0.000 description 5
- 238000000338 in vitro Methods 0.000 description 5
- 206010022000 influenza Diseases 0.000 description 5
- 102000004169 proteins and genes Human genes 0.000 description 5
- 241000710198 Foot-and-mouth disease virus Species 0.000 description 4
- 241000712431 Influenza A virus Species 0.000 description 4
- 201000010099 disease Diseases 0.000 description 4
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 4
- BPHPUYQFMNQIOC-NXRLNHOXSA-N isopropyl beta-D-thiogalactopyranoside Chemical compound CC(C)S[C@@H]1O[C@H](CO)[C@H](O)[C@H](O)[C@H]1O BPHPUYQFMNQIOC-NXRLNHOXSA-N 0.000 description 4
- 238000006386 neutralization reaction Methods 0.000 description 4
- 235000018102 proteins Nutrition 0.000 description 4
- 102100027723 Endogenous retrovirus group K member 6 Rec protein Human genes 0.000 description 3
- 101710121417 Envelope glycoprotein Proteins 0.000 description 3
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 3
- MYGQXVYRZMKRDB-SRVKXCTJSA-N Leu-Asp-Lys Chemical compound CC(C)C[C@H](N)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@H](C(O)=O)CCCCN MYGQXVYRZMKRDB-SRVKXCTJSA-N 0.000 description 3
- 108091034117 Oligonucleotide Proteins 0.000 description 3
- 208000037581 Persistent Infection Diseases 0.000 description 3
- 230000006044 T cell activation Effects 0.000 description 3
- 241000700618 Vaccinia virus Species 0.000 description 3
- 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 3
- 230000002238 attenuated effect Effects 0.000 description 3
- 230000008901 benefit Effects 0.000 description 3
- 230000015572 biosynthetic process Effects 0.000 description 3
- 238000005119 centrifugation Methods 0.000 description 3
- 238000010367 cloning Methods 0.000 description 3
- 230000000694 effects Effects 0.000 description 3
- RWSXRVCMGQZWBV-WDSKDSINSA-N glutathione Chemical compound OC(=O)[C@@H](N)CCC(=O)N[C@@H](CS)C(=O)NCC(O)=O RWSXRVCMGQZWBV-WDSKDSINSA-N 0.000 description 3
- 229960003180 glutathione Drugs 0.000 description 3
- 235000003969 glutathione Nutrition 0.000 description 3
- 230000001900 immune effect Effects 0.000 description 3
- 239000013612 plasmid Substances 0.000 description 3
- 229920001184 polypeptide Polymers 0.000 description 3
- 230000001681 protective effect Effects 0.000 description 3
- 230000009257 reactivity Effects 0.000 description 3
- 238000002255 vaccination Methods 0.000 description 3
- 229960005486 vaccine Drugs 0.000 description 3
- 230000003612 virological effect Effects 0.000 description 3
- 238000005406 washing Methods 0.000 description 3
- 206010001513 AIDS related complex Diseases 0.000 description 2
- ZXRQJQCXPSMNMR-XIRDDKMYSA-N Asp-Lys-Trp Chemical compound C1=CC=C2C(=C1)C(=CN2)C[C@@H](C(=O)O)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CC(=O)O)N ZXRQJQCXPSMNMR-XIRDDKMYSA-N 0.000 description 2
- 241000991587 Enterovirus C Species 0.000 description 2
- 206010061598 Immunodeficiency Diseases 0.000 description 2
- 208000029462 Immunodeficiency disease Diseases 0.000 description 2
- 241000283973 Oryctolagus cuniculus Species 0.000 description 2
- 229920002684 Sepharose Polymers 0.000 description 2
- 230000024932 T cell mediated immunity Effects 0.000 description 2
- 125000000539 amino acid group Chemical group 0.000 description 2
- 230000005875 antibody response Effects 0.000 description 2
- 238000003556 assay Methods 0.000 description 2
- AIYUHDOJVYHVIT-UHFFFAOYSA-M caesium chloride Chemical compound [Cl-].[Cs+] AIYUHDOJVYHVIT-UHFFFAOYSA-M 0.000 description 2
- 230000001413 cellular effect Effects 0.000 description 2
- 238000011161 development Methods 0.000 description 2
- 238000010828 elution Methods 0.000 description 2
- 238000002474 experimental method Methods 0.000 description 2
- 230000028996 humoral immune response Effects 0.000 description 2
- 230000008105 immune reaction Effects 0.000 description 2
- 230000007813 immunodeficiency Effects 0.000 description 2
- 208000033065 inborn errors of immunity Diseases 0.000 description 2
- 238000004519 manufacturing process Methods 0.000 description 2
- 230000001404 mediated effect Effects 0.000 description 2
- 238000002703 mutagenesis Methods 0.000 description 2
- 231100000350 mutagenesis Toxicity 0.000 description 2
- 244000052769 pathogen Species 0.000 description 2
- 238000012510 peptide mapping method Methods 0.000 description 2
- 230000001566 pro-viral effect Effects 0.000 description 2
- 102000005962 receptors Human genes 0.000 description 2
- 108020003175 receptors Proteins 0.000 description 2
- 238000005215 recombination Methods 0.000 description 2
- 230000006798 recombination Effects 0.000 description 2
- 230000010076 replication Effects 0.000 description 2
- AVWQQPYHYQKEIZ-UHFFFAOYSA-K trisodium;2-dodecylbenzenesulfonate;3-dodecylbenzenesulfonate;4-dodecylbenzenesulfonate Chemical compound [Na+].[Na+].[Na+].CCCCCCCCCCCCC1=CC=C(S([O-])(=O)=O)C=C1.CCCCCCCCCCCCC1=CC=CC(S([O-])(=O)=O)=C1.CCCCCCCCCCCCC1=CC=CC=C1S([O-])(=O)=O AVWQQPYHYQKEIZ-UHFFFAOYSA-K 0.000 description 2
- 241001430294 unidentified retrovirus Species 0.000 description 2
- 239000013598 vector Substances 0.000 description 2
- 210000002845 virion Anatomy 0.000 description 2
- 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 description 1
- -1 AMINO Chemical class 0.000 description 1
- LSLIRHLIUDVNBN-CIUDSAMLSA-N Ala-Asp-Lys Chemical compound C[C@H](N)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@H](C(O)=O)CCCCN LSLIRHLIUDVNBN-CIUDSAMLSA-N 0.000 description 1
- DAEFQZCYZKRTLR-ZLUOBGJFSA-N Ala-Cys-Asp Chemical compound [H]N[C@@H](C)C(=O)N[C@@H](CS)C(=O)N[C@@H](CC(O)=O)C(O)=O DAEFQZCYZKRTLR-ZLUOBGJFSA-N 0.000 description 1
- GRPHQEMIFDPKOE-HGNGGELXSA-N Ala-His-Glu Chemical compound [H]N[C@@H](C)C(=O)N[C@@H](CC1=CNC=N1)C(=O)N[C@@H](CCC(O)=O)C(O)=O GRPHQEMIFDPKOE-HGNGGELXSA-N 0.000 description 1
- BFMIRJBURUXDRG-DLOVCJGASA-N Ala-Phe-Asp Chemical compound OC(=O)C[C@@H](C(O)=O)NC(=O)[C@@H](NC(=O)[C@@H](N)C)CC1=CC=CC=C1 BFMIRJBURUXDRG-DLOVCJGASA-N 0.000 description 1
- HOVPGJUNRLMIOZ-CIUDSAMLSA-N Ala-Ser-Leu Chemical compound CC(C)C[C@@H](C(O)=O)NC(=O)[C@H](CO)NC(=O)[C@H](C)N HOVPGJUNRLMIOZ-CIUDSAMLSA-N 0.000 description 1
- YCTIYBUTCKNOTI-UWJYBYFXSA-N Ala-Tyr-Asp Chemical compound C[C@@H](C(=O)N[C@@H](CC1=CC=C(C=C1)O)C(=O)N[C@@H](CC(=O)O)C(=O)O)N YCTIYBUTCKNOTI-UWJYBYFXSA-N 0.000 description 1
- 108090000656 Annexin A6 Proteins 0.000 description 1
- 102100034278 Annexin A6 Human genes 0.000 description 1
- 108010032595 Antibody Binding Sites Proteins 0.000 description 1
- 101100421130 Arabidopsis thaliana SEI3 gene Proteins 0.000 description 1
- SQKPKIJVWHAWNF-DCAQKATOSA-N Arg-Asp-Lys Chemical compound [H]N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CCCCN)C(O)=O SQKPKIJVWHAWNF-DCAQKATOSA-N 0.000 description 1
- 208000002109 Argyria Diseases 0.000 description 1
- OAMLVOVXNKILLQ-BQBZGAKWSA-N Asp-Lys Chemical compound NCCCC[C@@H](C(O)=O)NC(=O)[C@@H](N)CC(O)=O OAMLVOVXNKILLQ-BQBZGAKWSA-N 0.000 description 1
- 208000034048 Asymptomatic disease Diseases 0.000 description 1
- 102100022717 Atypical chemokine receptor 1 Human genes 0.000 description 1
- 238000011725 BALB/c mouse Methods 0.000 description 1
- 241000894006 Bacteria Species 0.000 description 1
- 101100436100 Caenorhabditis elegans asp-6 gene Proteins 0.000 description 1
- 101150109517 Camlg gene Proteins 0.000 description 1
- 108020004705 Codon Proteins 0.000 description 1
- 201000000077 Cysticercosis Diseases 0.000 description 1
- 108010054576 Deoxyribonuclease EcoRI Proteins 0.000 description 1
- 206010061818 Disease progression Diseases 0.000 description 1
- 238000002965 ELISA Methods 0.000 description 1
- 241000702371 Enterobacteria phage f1 Species 0.000 description 1
- 101900345593 Escherichia coli Alkaline phosphatase Proteins 0.000 description 1
- 208000007212 Foot-and-Mouth Disease Diseases 0.000 description 1
- QBLMTCRYYTVUQY-GUBZILKMSA-N Gln-Leu-Asp Chemical compound [H]N[C@@H](CCC(N)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(O)=O)C(O)=O QBLMTCRYYTVUQY-GUBZILKMSA-N 0.000 description 1
- RBSKVTZUFMIWFU-XEGUGMAKSA-N Gln-Trp-Ala Chemical compound [H]N[C@@H](CCC(N)=O)C(=O)N[C@@H](CC1=CNC2=C1C=CC=C2)C(=O)N[C@@H](C)C(O)=O RBSKVTZUFMIWFU-XEGUGMAKSA-N 0.000 description 1
- VMKCPNBBPGGQBJ-GUBZILKMSA-N Glu-Leu-Asn Chemical compound CC(C)C[C@@H](C(=O)N[C@@H](CC(=O)N)C(=O)O)NC(=O)[C@H](CCC(=O)O)N VMKCPNBBPGGQBJ-GUBZILKMSA-N 0.000 description 1
- CLODWIOAKCSBAN-BQBZGAKWSA-N Gly-Arg-Asp Chemical compound NC(N)=NCCC[C@H](NC(=O)CN)C(=O)N[C@@H](CC(O)=O)C(O)=O CLODWIOAKCSBAN-BQBZGAKWSA-N 0.000 description 1
- YTSVAIMKVLZUDU-YUMQZZPRSA-N Gly-Leu-Asp Chemical compound [H]NCC(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(O)=O)C(O)=O YTSVAIMKVLZUDU-YUMQZZPRSA-N 0.000 description 1
- WDXLKVQATNEAJQ-BQBZGAKWSA-N Gly-Pro-Asp Chemical compound NCC(=O)N1CCC[C@H]1C(=O)N[C@@H](CC(O)=O)C(O)=O WDXLKVQATNEAJQ-BQBZGAKWSA-N 0.000 description 1
- 239000004471 Glycine Substances 0.000 description 1
- 101000678879 Homo sapiens Atypical chemokine receptor 1 Proteins 0.000 description 1
- 101001082397 Human adenovirus B serotype 3 Hexon-associated protein Proteins 0.000 description 1
- 108060003951 Immunoglobulin Proteins 0.000 description 1
- 206010062016 Immunosuppression Diseases 0.000 description 1
- 238000012404 In vitro experiment Methods 0.000 description 1
- 241000713196 Influenza B virus Species 0.000 description 1
- 241000274177 Juniperus sabina Species 0.000 description 1
- CLVUXCBGKUECIT-HJGDQZAQSA-N Leu-Asp-Thr Chemical compound [H]N[C@@H](CC(C)C)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H]([C@@H](C)O)C(O)=O CLVUXCBGKUECIT-HJGDQZAQSA-N 0.000 description 1
- QVFGXCVIXXBFHO-AVGNSLFASA-N Leu-Glu-Leu Chemical compound CC(C)C[C@H](N)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(C)C)C(O)=O QVFGXCVIXXBFHO-AVGNSLFASA-N 0.000 description 1
- 208000016604 Lyme disease Diseases 0.000 description 1
- MLLKLNYPZRDIQG-GUBZILKMSA-N Lys-Cys-Gln Chemical compound C(CCN)C[C@@H](C(=O)N[C@@H](CS)C(=O)N[C@@H](CCC(=O)N)C(=O)O)N MLLKLNYPZRDIQG-GUBZILKMSA-N 0.000 description 1
- QQYRCUXKLDGCQN-SRVKXCTJSA-N Lys-Cys-His Chemical compound C1=C(NC=N1)C[C@@H](C(=O)O)NC(=O)[C@H](CS)NC(=O)[C@H](CCCCN)N QQYRCUXKLDGCQN-SRVKXCTJSA-N 0.000 description 1
- MUXNCRWTWBMNHX-SRVKXCTJSA-N Lys-Leu-Asp Chemical compound [H]N[C@@H](CCCCN)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(O)=O)C(O)=O MUXNCRWTWBMNHX-SRVKXCTJSA-N 0.000 description 1
- KTINOHQFVVCEGQ-XIRDDKMYSA-N Lys-Trp-Asp Chemical compound NCCCC[C@H](N)C(=O)N[C@@H](Cc1c[nH]c2ccccc12)C(=O)N[C@@H](CC(O)=O)C(O)=O KTINOHQFVVCEGQ-XIRDDKMYSA-N 0.000 description 1
- OKCJTECLRDARDZ-XIRDDKMYSA-N Lys-Trp-Cys Chemical compound C1=CC=C2C(C[C@H](NC(=O)[C@@H](N)CCCCN)C(=O)N[C@@H](CS)C(O)=O)=CNC2=C1 OKCJTECLRDARDZ-XIRDDKMYSA-N 0.000 description 1
- CFOLERIRBUAYAD-HOCLYGCPSA-N Lys-Trp-Gly Chemical compound [H]N[C@@H](CCCCN)C(=O)N[C@@H](CC1=CNC2=C1C=CC=C2)C(=O)NCC(O)=O CFOLERIRBUAYAD-HOCLYGCPSA-N 0.000 description 1
- GVKINWYYLOLEFQ-XIRDDKMYSA-N Lys-Trp-Ser Chemical compound [H]N[C@@H](CCCCN)C(=O)N[C@@H](CC1=CNC2=C1C=CC=C2)C(=O)N[C@@H](CO)C(O)=O GVKINWYYLOLEFQ-XIRDDKMYSA-N 0.000 description 1
- 108010090054 Membrane Glycoproteins Proteins 0.000 description 1
- 102000012750 Membrane Glycoproteins Human genes 0.000 description 1
- 241001465754 Metazoa Species 0.000 description 1
- 241000353097 Molva molva Species 0.000 description 1
- 101100194706 Mus musculus Arhgap32 gene Proteins 0.000 description 1
- 108010087066 N2-tryptophyllysine Proteins 0.000 description 1
- 206010028980 Neoplasm Diseases 0.000 description 1
- 108700006640 OspA Proteins 0.000 description 1
- 241000282579 Pan Species 0.000 description 1
- 241000237988 Patellidae Species 0.000 description 1
- 208000000474 Poliomyelitis Diseases 0.000 description 1
- 229920001213 Polysorbate 20 Polymers 0.000 description 1
- 101001120093 Pseudoalteromonas phage PM2 Protein P8 Proteins 0.000 description 1
- 241000702263 Reovirus sp. Species 0.000 description 1
- 241000242677 Schistosoma japonicum Species 0.000 description 1
- 241000700584 Simplexvirus Species 0.000 description 1
- FBQHKSPOIAFUEI-OWLDWWDNSA-N Thr-Trp-Ala Chemical compound [H]N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CC1=CNC2=C1C=CC=C2)C(=O)N[C@@H](C)C(O)=O FBQHKSPOIAFUEI-OWLDWWDNSA-N 0.000 description 1
- 239000007983 Tris buffer Substances 0.000 description 1
- OHGNSVACHBZKSS-KWQFWETISA-N Trp-Ala Chemical compound C1=CC=C2C(C[C@H]([NH3+])C(=O)N[C@@H](C)C([O-])=O)=CNC2=C1 OHGNSVACHBZKSS-KWQFWETISA-N 0.000 description 1
- AVYVKJMBNLPWRX-WFBYXXMGSA-N Trp-Ala-Ser Chemical compound C1=CC=C2C(C[C@H](N)C(=O)N[C@@H](C)C(=O)N[C@@H](CO)C(O)=O)=CNC2=C1 AVYVKJMBNLPWRX-WFBYXXMGSA-N 0.000 description 1
- 241001442397 Trypanosoma brucei rhodesiense Species 0.000 description 1
- 206010046865 Vaccinia virus infection Diseases 0.000 description 1
- 101100194707 Xenopus laevis arhgap32 gene Proteins 0.000 description 1
- 230000000240 adjuvant effect Effects 0.000 description 1
- 230000036436 anti-hiv Effects 0.000 description 1
- 230000027645 antigenic variation Effects 0.000 description 1
- 238000013459 approach Methods 0.000 description 1
- 108010038633 aspartylglutamate Proteins 0.000 description 1
- 230000001363 autoimmune Effects 0.000 description 1
- 230000001580 bacterial effect Effects 0.000 description 1
- 230000000903 blocking effect Effects 0.000 description 1
- 230000008859 change Effects 0.000 description 1
- 238000012512 characterization method Methods 0.000 description 1
- 238000006243 chemical reaction Methods 0.000 description 1
- 239000003795 chemical substances by application Substances 0.000 description 1
- 230000002759 chromosomal effect Effects 0.000 description 1
- 238000012411 cloning technique Methods 0.000 description 1
- 239000011248 coating agent Substances 0.000 description 1
- 238000000576 coating method Methods 0.000 description 1
- 238000004132 cross linking Methods 0.000 description 1
- 210000001151 cytotoxic T lymphocyte Anatomy 0.000 description 1
- LOKCTEFSRHRXRJ-UHFFFAOYSA-I dipotassium trisodium dihydrogen phosphate hydrogen phosphate dichloride Chemical compound P(=O)(O)(O)[O-].[K+].P(=O)(O)([O-])[O-].[Na+].[Na+].[Cl-].[K+].[Cl-].[Na+] LOKCTEFSRHRXRJ-UHFFFAOYSA-I 0.000 description 1
- 231100000676 disease causative agent Toxicity 0.000 description 1
- 230000005750 disease progression Effects 0.000 description 1
- 238000001962 electrophoresis Methods 0.000 description 1
- 239000012149 elution buffer Substances 0.000 description 1
- 239000000499 gel Substances 0.000 description 1
- 208000002672 hepatitis B Diseases 0.000 description 1
- 238000009396 hybridization Methods 0.000 description 1
- 210000000987 immune system Anatomy 0.000 description 1
- 238000003119 immunoblot Methods 0.000 description 1
- 230000005847 immunogenicity Effects 0.000 description 1
- 102000018358 immunoglobulin Human genes 0.000 description 1
- 230000001506 immunosuppresive effect Effects 0.000 description 1
- 238000011534 incubation Methods 0.000 description 1
- 230000006698 induction Effects 0.000 description 1
- 230000010354 integration Effects 0.000 description 1
- 239000003446 ligand Substances 0.000 description 1
- 230000036210 malignancy Effects 0.000 description 1
- 230000007246 mechanism Effects 0.000 description 1
- 238000010369 molecular cloning Methods 0.000 description 1
- 230000035772 mutation Effects 0.000 description 1
- 210000002569 neuron Anatomy 0.000 description 1
- 239000002245 particle Substances 0.000 description 1
- 238000002823 phage display Methods 0.000 description 1
- DDBREPKUVSBGFI-UHFFFAOYSA-N phenobarbital Chemical compound C=1C=CC=CC=1C1(CC)C(=O)NC(=O)NC1=O DDBREPKUVSBGFI-UHFFFAOYSA-N 0.000 description 1
- 229920002401 polyacrylamide Polymers 0.000 description 1
- 235000010486 polyoxyethylene sorbitan monolaurate Nutrition 0.000 description 1
- 239000000256 polyoxyethylene sorbitan monolaurate Substances 0.000 description 1
- 229920002223 polystyrene Polymers 0.000 description 1
- 239000000843 powder Substances 0.000 description 1
- 238000001556 precipitation Methods 0.000 description 1
- 238000002360 preparation method Methods 0.000 description 1
- 230000002265 prevention Effects 0.000 description 1
- 208000028529 primary immunodeficiency disease Diseases 0.000 description 1
- 238000010079 rubber tapping Methods 0.000 description 1
- 230000003248 secreting effect Effects 0.000 description 1
- 210000002966 serum Anatomy 0.000 description 1
- 235000020183 skimmed milk Nutrition 0.000 description 1
- 238000001179 sorption measurement Methods 0.000 description 1
- 238000006467 substitution reaction Methods 0.000 description 1
- 229940031626 subunit vaccine Drugs 0.000 description 1
- 239000006228 supernatant Substances 0.000 description 1
- 208000010648 susceptibility to HIV infection Diseases 0.000 description 1
- 208000004441 taeniasis Diseases 0.000 description 1
- 238000012360 testing method Methods 0.000 description 1
- 229960000814 tetanus toxoid Drugs 0.000 description 1
- SRVJKTDHMYAMHA-WUXMJOGZSA-N thioacetazone Chemical compound CC(=O)NC1=CC=C(\C=N\NC(N)=S)C=C1 SRVJKTDHMYAMHA-WUXMJOGZSA-N 0.000 description 1
- 230000026683 transduction Effects 0.000 description 1
- 238000010361 transduction Methods 0.000 description 1
- 238000013519 translation Methods 0.000 description 1
- 230000001960 triggered effect Effects 0.000 description 1
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 1
- 208000007089 vaccinia Diseases 0.000 description 1
- 238000001262 western blot Methods 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/005—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from viruses
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P31/00—Antiinfectives, i.e. antibiotics, antiseptics, chemotherapeutics
- A61P31/12—Antivirals
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P31/00—Antiinfectives, i.e. antibiotics, antiseptics, chemotherapeutics
- A61P31/12—Antivirals
- A61P31/14—Antivirals for RNA viruses
- A61P31/18—Antivirals for RNA viruses for HIV
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/08—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from viruses
- C07K16/10—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from viruses from RNA viruses
- C07K16/1036—Retroviridae, e.g. leukemia viruses
- C07K16/1045—Lentiviridae, e.g. HIV, FIV, SIV
- C07K16/1063—Lentiviridae, e.g. HIV, FIV, SIV env, e.g. gp41, gp110/120, gp160, V3, PND, CD4 binding site
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/42—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against immunoglobulins
- C07K16/4208—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against immunoglobulins against an idiotypic determinant on Ig
- C07K16/4216—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against immunoglobulins against an idiotypic determinant on Ig against anti-viral Ig
- C07K16/4225—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against immunoglobulins against an idiotypic determinant on Ig against anti-viral Ig against anti-HIV Ig
-
- 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
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N2740/00—Reverse transcribing RNA viruses
- C12N2740/00011—Details
- C12N2740/10011—Retroviridae
- C12N2740/16011—Human Immunodeficiency Virus, HIV
- C12N2740/16111—Human Immunodeficiency Virus, HIV concerning HIV env
- C12N2740/16122—New viral proteins or individual genes, new structural or functional aspects of known viral proteins or genes
-
- Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y02—TECHNOLOGIES OR APPLICATIONS FOR MITIGATION OR ADAPTATION AGAINST CLIMATE CHANGE
- Y02A—TECHNOLOGIES FOR ADAPTATION TO CLIMATE CHANGE
- Y02A50/00—TECHNOLOGIES FOR ADAPTATION TO CLIMATE CHANGE in human health protection, e.g. against extreme weather
- Y02A50/30—Against vector-borne diseases, e.g. mosquito-borne, fly-borne, tick-borne or waterborne diseases whose impact is exacerbated by climate change
Landscapes
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Organic Chemistry (AREA)
- Virology (AREA)
- Medicinal Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Immunology (AREA)
- Molecular Biology (AREA)
- Biophysics (AREA)
- Genetics & Genomics (AREA)
- Biochemistry (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- AIDS & HIV (AREA)
- Oncology (AREA)
- Veterinary Medicine (AREA)
- Communicable Diseases (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Pharmacology & Pharmacy (AREA)
- Animal Behavior & Ethology (AREA)
- Public Health (AREA)
- General Chemical & Material Sciences (AREA)
- Gastroenterology & Hepatology (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Hematology (AREA)
- Tropical Medicine & Parasitology (AREA)
- Peptides Or Proteins (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
Applications Claiming Priority (4)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| ATA987/92 | 1992-05-14 | ||
| AT98792A AT403050B (de) | 1992-05-14 | 1992-05-14 | Peptide, die antikörper binden |
| US93278792A | 1992-08-29 | 1992-08-29 | |
| US932,787 | 1992-08-29 |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| CA2096159A1 CA2096159A1 (en) | 1993-11-15 |
| CA2096159C true CA2096159C (en) | 2004-07-20 |
Family
ID=25594514
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CA002096159A Expired - Lifetime CA2096159C (en) | 1992-05-14 | 1993-05-13 | Peptides that induce antibodies which neutralize genetically divergent hiv-1 isolates |
Country Status (6)
| Country | Link |
|---|---|
| US (3) | US5693752A (enExample) |
| EP (1) | EP0570357B1 (enExample) |
| JP (1) | JP3369246B2 (enExample) |
| CA (1) | CA2096159C (enExample) |
| DE (2) | DE69311764T2 (enExample) |
| ES (1) | ES2053413T3 (enExample) |
Families Citing this family (38)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPH06506947A (ja) * | 1991-04-18 | 1994-08-04 | マウント シナイ スクール オブ メディスン オブ ザ シティー ユニバーシティー オブ ニューヨーク | 抗ウィルスハイブリッド抗体 |
| DE69311764T2 (de) * | 1992-05-14 | 1998-02-05 | Polymun Scient Immunbio Forsch | Peptide, die Antikörper induzieren, die genetisch divergierende HIV-1 Isolationen neutralisieren |
| BR9407531A (pt) * | 1993-09-11 | 1997-08-26 | Polymun Scient Immunbio Forsch | Peptideos que provocam a formação de anticorpos neutralizadores contra cepas de HIV-1 geneticamente divergentes |
| EP0787191B2 (fr) | 1994-10-20 | 2011-10-26 | Institut Pasteur | Sequences nucleotidiques d'antigenes retroviraux vih-1 groupe (ou sous-groupe) o |
| FR2731225B1 (fr) * | 1995-03-03 | 2003-10-31 | Pasteur Institut | Peptides de glycoproteine transmembranaire d'enveloppe et de proteine de capside du retrovirus humain du type hiv-1 et peptides presentant avec eux une parente immunologique |
| GB9424631D0 (en) * | 1994-12-06 | 1995-01-25 | Lynxvale Ltd | Modulating the immune response |
| MX9708008A (es) * | 1995-04-19 | 1998-03-31 | Polymun Scient Immunbio Forsch | Anticuerpos monoclonales contra vih-1 y vacunas hechas de los mismos. |
| US5891994A (en) * | 1997-07-11 | 1999-04-06 | Thymon L.L.C. | Methods and compositions for impairing multiplication of HIV-1 |
| US6492110B1 (en) | 1998-11-02 | 2002-12-10 | Uab Research Foundation | Reference clones and sequences for non-subtype B isolates of human immunodeficiency virus type 1 |
| ES2400445T3 (es) * | 1998-06-12 | 2013-04-09 | Mount Sinai School Of Medicine | Virus atenuados con cadena de polaridad negativa con actividad antagonista de interferón alterada para uso como vacunas y productos farmacéuticos |
| ES2301241T3 (es) * | 1998-06-12 | 2008-06-16 | Mount Sinai School Of Medicine Of The City University Of New York | Virus de influenza a atenuados, y composiciones inmunogenicas y formulaciones de vacunas que los contienen. |
| US7090848B1 (en) | 1998-08-04 | 2006-08-15 | Henry M. Jackson Foundation For The Advancement Of Military Medicine | HIV-1 envelope protein associated with a broadly reactive neutralizing antibody response |
| CA2338886C (en) * | 1998-08-04 | 2011-10-04 | Gerald V. Quinnan, Jr. | Expression and characterization of hiv-1 envelope protein associated with a broadly reactive neutralizing antibody response |
| US7115262B1 (en) | 1999-03-16 | 2006-10-03 | The United States Of America As Represented By The Department Of Health And Human Services | Chimeric protein for prevention and treatment of HIV infection |
| WO2001077394A1 (en) * | 2000-04-10 | 2001-10-18 | Mount Sinai School Of Medicine Of New York University | Screening methods for identifying viral proteins with interferon antagonizing functions and potential antiviral agents |
| US6399067B1 (en) * | 2000-04-28 | 2002-06-04 | Thymon L.L.C. | Methods and compositions for impairing multiplication of HIV-1 |
| EP1465928B1 (en) | 2002-01-17 | 2009-09-30 | Polymun Scientific Immunbiologische Forschung GmbH | Anti-idiotypic antibody inducing hiv-1 neutralizing antibodies |
| JP2007515394A (ja) * | 2003-05-06 | 2007-06-14 | ザ スクリプス リサーチ インスティチュート | ドメイン交換結合分子、その使用方法および製造方法 |
| CN1993140A (zh) | 2004-06-01 | 2007-07-04 | 纽约大学西奈山医学院 | 遗传工程猪流感病毒及其应用 |
| JP2008535783A (ja) | 2005-02-15 | 2008-09-04 | サイモン・エル・エル・シー | Ｈｉｖ−１の増殖を弱めるための方法および組成物 |
| WO2006088481A2 (en) * | 2005-02-15 | 2006-08-24 | Mount Sinai School Of Medicine Of New York University | Genetically engineered equine influenza virus and uses thereof |
| TW200726479A (en) * | 2005-04-12 | 2007-07-16 | Univ Duke | Method of inducing neutralizing antibodies to human immunodeficiency virus |
| WO2007084568A2 (en) | 2006-01-17 | 2007-07-26 | Health Research, Inc. | Heteroduplex tracking assay |
| WO2008127651A1 (en) * | 2007-04-13 | 2008-10-23 | Duke University | Method of inducing neutralizing antibodies to human immunodeficiency virus |
| AU2011230619C1 (en) | 2010-03-25 | 2016-06-23 | Oregon Health & Science University | CMV glycoproteins and recombinant vectors |
| HRP20180607T1 (hr) | 2011-06-10 | 2019-04-05 | Oregon Health & Science University | Glikoproteini i rekombinantni vektori cmv |
| CA2789539A1 (en) | 2011-09-12 | 2013-03-12 | International Aids Vaccine Initiative | Immunoselection of recombinant vesicular stomatitis virus expressing hiv-1 proteins by broadly neutralizing antibodies |
| US9402894B2 (en) | 2011-10-27 | 2016-08-02 | International Aids Vaccine Initiative | Viral particles derived from an enveloped virus |
| EP2679596B1 (en) | 2012-06-27 | 2017-04-12 | International Aids Vaccine Initiative | HIV-1 env glycoprotein variant |
| EP2848937A1 (en) | 2013-09-05 | 2015-03-18 | International Aids Vaccine Initiative | Methods of identifying novel HIV-1 immunogens |
| WO2015048635A1 (en) | 2013-09-27 | 2015-04-02 | Duke University | Mper-liposome conjugates and uses thereof |
| EP2873423B1 (en) | 2013-10-07 | 2017-05-31 | International Aids Vaccine Initiative | Soluble hiv-1 envelope glycoprotein trimers |
| CN107250353B (zh) | 2015-02-26 | 2021-07-23 | 勃林格殷格翰动物保健有限公司 | 二价猪流感病毒疫苗 |
| EP3069730A3 (en) | 2015-03-20 | 2017-03-15 | International Aids Vaccine Initiative | Soluble hiv-1 envelope glycoprotein trimers |
| EP3072901A1 (en) | 2015-03-23 | 2016-09-28 | International Aids Vaccine Initiative | Soluble hiv-1 envelope glycoprotein trimers |
| WO2017093985A1 (en) | 2015-12-05 | 2017-06-08 | Centre Hospitalier Universitaire Vaudois | Hiv binding agents |
| WO2020012435A1 (en) | 2018-07-13 | 2020-01-16 | Lausanne University Hospital | Hiv binding agents |
| EP3996815A2 (en) | 2019-07-15 | 2022-05-18 | Lausanne University Hospital | Hiv binding agents |
Family Cites Families (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| AU617088B2 (en) * | 1986-06-12 | 1991-11-21 | Biogen, Inc. | Peptides involved in the pathogenesis of hiv infection |
| EP0330359A3 (en) * | 1988-02-25 | 1991-06-05 | Bio-Rad Laboratories, Inc. | Composition useful in the diagnosis and treating of hiv-1 infection |
| EP0362910A3 (en) * | 1988-08-27 | 1991-01-09 | Akzo N.V. | Synthetic peptides immunochemically reactive with hiv-antibodies |
| DE69311764T2 (de) * | 1992-05-14 | 1998-02-05 | Polymun Scient Immunbio Forsch | Peptide, die Antikörper induzieren, die genetisch divergierende HIV-1 Isolationen neutralisieren |
-
1993
- 1993-05-13 DE DE69311764T patent/DE69311764T2/de not_active Expired - Lifetime
- 1993-05-13 EP EP93890100A patent/EP0570357B1/en not_active Expired - Lifetime
- 1993-05-13 DE DE0570357T patent/DE570357T1/de active Pending
- 1993-05-13 ES ES93890100T patent/ES2053413T3/es not_active Expired - Lifetime
- 1993-05-13 CA CA002096159A patent/CA2096159C/en not_active Expired - Lifetime
- 1993-05-14 JP JP11300793A patent/JP3369246B2/ja not_active Expired - Fee Related
-
1994
- 1994-12-22 US US08/361,479 patent/US5693752A/en not_active Expired - Lifetime
-
1995
- 1995-06-07 US US08/473,576 patent/US5756674A/en not_active Expired - Fee Related
-
1997
- 1997-04-17 US US08/843,718 patent/US5866694A/en not_active Expired - Lifetime
Also Published As
| Publication number | Publication date |
|---|---|
| US5866694A (en) | 1999-02-02 |
| JPH06293797A (ja) | 1994-10-21 |
| DE69311764D1 (de) | 1997-07-31 |
| DE570357T1 (de) | 1994-07-28 |
| EP0570357A2 (en) | 1993-11-18 |
| ES2053413T1 (es) | 1994-08-01 |
| DE69311764T2 (de) | 1998-02-05 |
| EP0570357B1 (en) | 1997-06-25 |
| EP0570357A3 (enExample) | 1994-04-20 |
| JP3369246B2 (ja) | 2003-01-20 |
| US5693752A (en) | 1997-12-02 |
| ES2053413T3 (es) | 1997-11-16 |
| US5756674A (en) | 1998-05-26 |
| CA2096159A1 (en) | 1993-11-15 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| CA2096159C (en) | Peptides that induce antibodies which neutralize genetically divergent hiv-1 isolates | |
| McLain et al. | Stimulation of neutralizing antibodies to human immunodeficiency virus type 1 in three strains of mice immunized with a 22 amino acid peptide of gp41 expressed on the surface of a plant virus | |
| US6335017B1 (en) | Compositions and methods for treating viral infections | |
| Nardelli et al. | A chemically defined synthetic vaccine model for HIV-1 | |
| HUT51296A (en) | Process for producing hn env-coded peptide for producing antibodies for inhibiting human hiv virus in mammalian | |
| EP0492560B1 (en) | Human monoclonal antibodies directed against the transmembrane glycoprotein (gp41) of HIV-1, and related peptides | |
| US6171596B1 (en) | Oligomeric HIV-1 envelope glycoproteins | |
| CS68091A2 (en) | Synthetic polypeptides | |
| WO1992008491A1 (en) | Conjugates of anti-idiotype antibodies and carriers and their use in epitope-directed immunization | |
| Kalyan et al. | Immunogenicity of recombinant influenza virus haemagglutinin carrying peptides from the envelope protein of human immunodeficiency virus type 1 | |
| US5003043A (en) | Peptides representing epitopic sites for the major HTLV-I envelope protein, antibodies thereto, and uses thereof | |
| WO1989005821A1 (en) | Hiv-related antigens and antibodies | |
| AU2017251715A1 (en) | Antibody recognizing arbitrarily designed epitope of three or more amino acid residues in a peptide and method of generating thereof | |
| Boudet et al. | Anti-idiotypic antibodies to the third variable domain of gp120 induce an anti-HIV-1 antibody response in mice | |
| WO1989005820A1 (en) | Hiv-related antigens and antibodies | |
| Boudet et al. | Single peptide and anti-idiotype based immunizations can broaden the antibody response against the variable V3 domain of HIV-1 in mice | |
| WO1994023746A1 (en) | Peptides for use in vaccination and induction of neutralizing antibodies against human immunodeficiency virus | |
| US10660951B2 (en) | Antibody recognizing arbitrarily designed epitope of three or more amino acid residues in a peptide and method of generating thereof | |
| AU2006200454A1 (en) | Compositions and methods for treating viral infections | |
| McLain et al. | Claudine Portal, George P. LomonossoffS and Nigel J. Dimmock* zyxwvutsrqponmlkjihgfedcbaZYXWVUTSRQPONMLKJIHG | |
| Boudet et al. | Fine analysis of immunoreactivity of V3 peptides: antibodies specific for V3 domain of laboratory HIV type 1 strains recognize multiple V3 sequences synthesized from field HIV type 1 isolates | |
| AU2006200455A1 (en) | Compositions and methods for treating viral infections | |
| AU6655300A (en) | Compositions and methods for treating infections |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| EEER | Examination request | ||
| MKLA | Lapsed |
Effective date: 20130513 |
|
| MKEC | Expiry (correction) |
Effective date: 20131009 |