RU2272809C2 - Специфичные в отношении вируса бешенства нейтрализующие моноклональные антитела человека и нуклеиновые кислоты и связанные с ними способы - Google Patents
Специфичные в отношении вируса бешенства нейтрализующие моноклональные антитела человека и нуклеиновые кислоты и связанные с ними способы Download PDFInfo
- Publication number
- RU2272809C2 RU2272809C2 RU2002133470/13A RU2002133470A RU2272809C2 RU 2272809 C2 RU2272809 C2 RU 2272809C2 RU 2002133470/13 A RU2002133470/13 A RU 2002133470/13A RU 2002133470 A RU2002133470 A RU 2002133470A RU 2272809 C2 RU2272809 C2 RU 2272809C2
- Authority
- RU
- Russia
- Prior art keywords
- antibody
- rabies virus
- seq
- amino acid
- cells
- Prior art date
Links
- 241000711798 Rabies lyssavirus Species 0.000 title claims abstract description 63
- 230000003472 neutralizing effect Effects 0.000 title claims abstract description 21
- 238000000034 method Methods 0.000 title claims abstract description 19
- 150000007523 nucleic acids Chemical class 0.000 title claims abstract description 17
- 108020004707 nucleic acids Proteins 0.000 title claims abstract description 13
- 102000039446 nucleic acids Human genes 0.000 title claims abstract description 13
- 239000012634 fragment Substances 0.000 claims abstract description 19
- 229920001184 polypeptide Polymers 0.000 claims abstract description 14
- 108090000765 processed proteins & peptides Proteins 0.000 claims abstract description 14
- 102000004196 processed proteins & peptides Human genes 0.000 claims abstract description 14
- 239000013598 vector Substances 0.000 claims abstract description 14
- 239000013604 expression vector Substances 0.000 claims description 8
- 125000003729 nucleotide group Chemical group 0.000 claims description 8
- 239000002773 nucleotide Substances 0.000 claims description 7
- 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 description 4
- 102000001706 Immunoglobulin Fab Fragments Human genes 0.000 claims description 3
- 108010054477 Immunoglobulin Fab Fragments Proteins 0.000 claims description 3
- 102000017727 Immunoglobulin Variable Region Human genes 0.000 claims description 3
- 108010067060 Immunoglobulin Variable Region Proteins 0.000 claims description 3
- 125000003275 alpha amino acid group Chemical group 0.000 claims 10
- 230000000694 effects Effects 0.000 abstract description 6
- 238000011282 treatment Methods 0.000 abstract description 3
- 239000000126 substance Substances 0.000 abstract description 2
- 230000007721 medicinal effect Effects 0.000 abstract 1
- 238000009117 preventive therapy Methods 0.000 abstract 1
- 210000004027 cell Anatomy 0.000 description 62
- 108090000623 proteins and genes Proteins 0.000 description 39
- 206010037742 Rabies Diseases 0.000 description 22
- 108060003951 Immunoglobulin Proteins 0.000 description 20
- 102000018358 immunoglobulin Human genes 0.000 description 20
- 241000700605 Viruses Species 0.000 description 18
- 239000002299 complementary DNA Substances 0.000 description 18
- 150000001413 amino acids Chemical group 0.000 description 16
- 230000004927 fusion Effects 0.000 description 16
- 239000013615 primer Substances 0.000 description 16
- 108091028043 Nucleic acid sequence Proteins 0.000 description 12
- 239000006228 supernatant Substances 0.000 description 12
- 238000003752 polymerase chain reaction Methods 0.000 description 11
- 108020004414 DNA Proteins 0.000 description 10
- 241000701044 Human gammaherpesvirus 4 Species 0.000 description 10
- 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 10
- 239000002953 phosphate buffered saline Substances 0.000 description 10
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 9
- 238000002360 preparation method Methods 0.000 description 9
- 239000000047 product Substances 0.000 description 9
- 102000004169 proteins and genes Human genes 0.000 description 9
- 238000012360 testing method Methods 0.000 description 9
- 108091034117 Oligonucleotide Proteins 0.000 description 7
- 238000007792 addition Methods 0.000 description 7
- CSCPPACGZOOCGX-UHFFFAOYSA-N Acetone Chemical compound CC(C)=O CSCPPACGZOOCGX-UHFFFAOYSA-N 0.000 description 6
- 230000003321 amplification Effects 0.000 description 6
- 230000015572 biosynthetic process Effects 0.000 description 6
- 238000003199 nucleic acid amplification method Methods 0.000 description 6
- 230000003612 virological effect Effects 0.000 description 6
- 241001465754 Metazoa Species 0.000 description 5
- 206010035226 Plasma cell myeloma Diseases 0.000 description 5
- 210000003719 b-lymphocyte Anatomy 0.000 description 5
- 210000003169 central nervous system Anatomy 0.000 description 5
- 238000006243 chemical reaction Methods 0.000 description 5
- 238000010790 dilution Methods 0.000 description 5
- 239000012895 dilution Substances 0.000 description 5
- 229940072221 immunoglobulins Drugs 0.000 description 5
- 208000015181 infectious disease Diseases 0.000 description 5
- 210000004698 lymphocyte Anatomy 0.000 description 5
- 238000004519 manufacturing process Methods 0.000 description 5
- 239000002609 medium Substances 0.000 description 5
- 201000000050 myeloid neoplasm Diseases 0.000 description 5
- 108091032973 (ribonucleotides)n+m Proteins 0.000 description 4
- LRFVTYWOQMYALW-UHFFFAOYSA-N 9H-xanthine Chemical compound O=C1NC(=O)NC2=C1NC=N2 LRFVTYWOQMYALW-UHFFFAOYSA-N 0.000 description 4
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 4
- 238000002965 ELISA Methods 0.000 description 4
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 4
- 102000003886 Glycoproteins Human genes 0.000 description 4
- 108090000288 Glycoproteins Proteins 0.000 description 4
- 108700005091 Immunoglobulin Genes Proteins 0.000 description 4
- 241000266847 Mephitidae Species 0.000 description 4
- 108091081024 Start codon Proteins 0.000 description 4
- 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 4
- 230000000295 complement effect Effects 0.000 description 4
- 238000006386 neutralization reaction Methods 0.000 description 4
- 241000894006 Bacteria Species 0.000 description 3
- 241000282465 Canis Species 0.000 description 3
- 241000282470 Canis latrans Species 0.000 description 3
- 241000288673 Chiroptera Species 0.000 description 3
- 108020004705 Codon Proteins 0.000 description 3
- 102000004190 Enzymes Human genes 0.000 description 3
- 108090000790 Enzymes Proteins 0.000 description 3
- 241000588724 Escherichia coli Species 0.000 description 3
- 241000282412 Homo Species 0.000 description 3
- 241001416166 Mephitis mephitis Species 0.000 description 3
- 241000699666 Mus <mouse, genus> Species 0.000 description 3
- 102000011931 Nucleoproteins Human genes 0.000 description 3
- 108010061100 Nucleoproteins Proteins 0.000 description 3
- 108020004511 Recombinant DNA Proteins 0.000 description 3
- 101710120037 Toxin CcdB Proteins 0.000 description 3
- 238000004458 analytical method Methods 0.000 description 3
- 210000000628 antibody-producing cell Anatomy 0.000 description 3
- 230000000890 antigenic effect Effects 0.000 description 3
- 230000001580 bacterial effect Effects 0.000 description 3
- 239000012148 binding buffer Substances 0.000 description 3
- 229940098773 bovine serum albumin Drugs 0.000 description 3
- 239000003153 chemical reaction reagent Substances 0.000 description 3
- KRKNYBCHXYNGOX-UHFFFAOYSA-N citric acid Chemical compound OC(=O)CC(O)(C(O)=O)CC(O)=O KRKNYBCHXYNGOX-UHFFFAOYSA-N 0.000 description 3
- 238000010367 cloning Methods 0.000 description 3
- 229940088598 enzyme Drugs 0.000 description 3
- 210000003527 eukaryotic cell Anatomy 0.000 description 3
- 238000001914 filtration Methods 0.000 description 3
- 239000001963 growth medium Substances 0.000 description 3
- 210000004408 hybridoma Anatomy 0.000 description 3
- 230000003053 immunization Effects 0.000 description 3
- 238000002649 immunization Methods 0.000 description 3
- 239000012535 impurity Substances 0.000 description 3
- 238000011534 incubation Methods 0.000 description 3
- 230000005764 inhibitory process Effects 0.000 description 3
- 239000000523 sample Substances 0.000 description 3
- 241000894007 species Species 0.000 description 3
- 238000010561 standard procedure Methods 0.000 description 3
- 239000000758 substrate Substances 0.000 description 3
- 238000003786 synthesis reaction Methods 0.000 description 3
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 3
- XZKIHKMTEMTJQX-UHFFFAOYSA-N 4-Nitrophenyl Phosphate Chemical compound OP(O)(=O)OC1=CC=C([N+]([O-])=O)C=C1 XZKIHKMTEMTJQX-UHFFFAOYSA-N 0.000 description 2
- 241000282421 Canidae Species 0.000 description 2
- 108091026890 Coding region Proteins 0.000 description 2
- 241000699800 Cricetinae Species 0.000 description 2
- 241001147414 Eptesicus fuscus Species 0.000 description 2
- 102000006395 Globulins Human genes 0.000 description 2
- 108010044091 Globulins Proteins 0.000 description 2
- 239000004471 Glycine Substances 0.000 description 2
- 102000008394 Immunoglobulin Fragments Human genes 0.000 description 2
- 108010021625 Immunoglobulin Fragments Proteins 0.000 description 2
- 102000006496 Immunoglobulin Heavy Chains Human genes 0.000 description 2
- 108010019476 Immunoglobulin Heavy Chains Proteins 0.000 description 2
- 102000013463 Immunoglobulin Light Chains Human genes 0.000 description 2
- 108010065825 Immunoglobulin Light Chains Proteins 0.000 description 2
- 102000012745 Immunoglobulin Subunits Human genes 0.000 description 2
- 108010079585 Immunoglobulin Subunits Proteins 0.000 description 2
- 241001125036 Lasionycteris noctivagans Species 0.000 description 2
- 206010029260 Neuroblastoma Diseases 0.000 description 2
- 239000002202 Polyethylene glycol Substances 0.000 description 2
- 241000282330 Procyon lotor Species 0.000 description 2
- 229920002684 Sepharose Polymers 0.000 description 2
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 2
- 241000596212 Vulpes lagopus Species 0.000 description 2
- 208000003455 anaphylaxis Diseases 0.000 description 2
- 238000003556 assay Methods 0.000 description 2
- 239000000872 buffer Substances 0.000 description 2
- 238000005119 centrifugation Methods 0.000 description 2
- 238000003776 cleavage reaction Methods 0.000 description 2
- 125000004122 cyclic group Chemical group 0.000 description 2
- 238000012217 deletion Methods 0.000 description 2
- 230000037430 deletion Effects 0.000 description 2
- 239000012636 effector Substances 0.000 description 2
- 238000001962 electrophoresis Methods 0.000 description 2
- 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 2
- 230000006870 function Effects 0.000 description 2
- 238000001727 in vivo Methods 0.000 description 2
- 239000010985 leather Substances 0.000 description 2
- 210000000265 leukocyte Anatomy 0.000 description 2
- 210000004379 membrane Anatomy 0.000 description 2
- 239000012528 membrane Substances 0.000 description 2
- 239000000203 mixture Substances 0.000 description 2
- 230000004048 modification Effects 0.000 description 2
- 238000012986 modification Methods 0.000 description 2
- 210000003819 peripheral blood mononuclear cell Anatomy 0.000 description 2
- 239000013612 plasmid Substances 0.000 description 2
- 229920001223 polyethylene glycol Polymers 0.000 description 2
- 238000011321 prophylaxis Methods 0.000 description 2
- 210000001938 protoplast Anatomy 0.000 description 2
- 238000000746 purification Methods 0.000 description 2
- 238000010839 reverse transcription Methods 0.000 description 2
- 230000007017 scission Effects 0.000 description 2
- 210000002966 serum Anatomy 0.000 description 2
- 239000012679 serum free medium Substances 0.000 description 2
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 2
- 239000000243 solution Substances 0.000 description 2
- 238000006467 substitution reaction Methods 0.000 description 2
- 239000013595 supernatant sample Substances 0.000 description 2
- 230000004083 survival effect Effects 0.000 description 2
- 230000014616 translation Effects 0.000 description 2
- 238000002255 vaccination Methods 0.000 description 2
- 229960005486 vaccine Drugs 0.000 description 2
- 238000005406 washing Methods 0.000 description 2
- 229940075420 xanthine Drugs 0.000 description 2
- BRZYSWJRSDMWLG-DJWUNRQOSA-N (2r,3r,4r,5r)-2-[(1s,2s,3r,4s,6r)-4,6-diamino-3-[(2s,3r,4r,5s,6r)-3-amino-4,5-dihydroxy-6-[(1r)-1-hydroxyethyl]oxan-2-yl]oxy-2-hydroxycyclohexyl]oxy-5-methyl-4-(methylamino)oxane-3,5-diol Chemical compound O1C[C@@](O)(C)[C@H](NC)[C@@H](O)[C@H]1O[C@@H]1[C@@H](O)[C@H](O[C@@H]2[C@@H]([C@@H](O)[C@H](O)[C@@H]([C@@H](C)O)O2)N)[C@@H](N)C[C@H]1N BRZYSWJRSDMWLG-DJWUNRQOSA-N 0.000 description 1
- AWKYSZSJPJUFQS-UHFFFAOYSA-N 3,7-dihydropurine-2,6-dione;phosphoric acid Chemical compound OP(O)(O)=O.O=C1NC(=O)NC2=C1NC=N2 AWKYSZSJPJUFQS-UHFFFAOYSA-N 0.000 description 1
- TVZGACDUOSZQKY-LBPRGKRZSA-N 4-aminofolic acid Chemical compound C1=NC2=NC(N)=NC(N)=C2N=C1CNC1=CC=C(C(=O)N[C@@H](CCC(O)=O)C(O)=O)C=C1 TVZGACDUOSZQKY-LBPRGKRZSA-N 0.000 description 1
- UZOVYGYOLBIAJR-UHFFFAOYSA-N 4-isocyanato-4'-methyldiphenylmethane Chemical compound C1=CC(C)=CC=C1CC1=CC=C(N=C=O)C=C1 UZOVYGYOLBIAJR-UHFFFAOYSA-N 0.000 description 1
- XZKIHKMTEMTJQX-UHFFFAOYSA-L 4-nitrophenyl phosphate(2-) Chemical compound [O-][N+](=O)C1=CC=C(OP([O-])([O-])=O)C=C1 XZKIHKMTEMTJQX-UHFFFAOYSA-L 0.000 description 1
- LPMXVESGRSUGHW-UHFFFAOYSA-N Acolongiflorosid K Natural products OC1C(O)C(O)C(C)OC1OC1CC2(O)CCC3C4(O)CCC(C=5COC(=O)C=5)C4(C)CC(O)C3C2(CO)C(O)C1 LPMXVESGRSUGHW-UHFFFAOYSA-N 0.000 description 1
- 241001404203 Aeorestes cinereus Species 0.000 description 1
- 229920000936 Agarose Polymers 0.000 description 1
- 206010002198 Anaphylactic reaction Diseases 0.000 description 1
- 206010003445 Ascites Diseases 0.000 description 1
- 241000713838 Avian myeloblastosis virus Species 0.000 description 1
- CURLTUGMZLYLDI-UHFFFAOYSA-N Carbon dioxide Chemical compound O=C=O CURLTUGMZLYLDI-UHFFFAOYSA-N 0.000 description 1
- 108020004635 Complementary DNA Proteins 0.000 description 1
- 102000053602 DNA Human genes 0.000 description 1
- 239000003155 DNA primer Substances 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
- 241000282326 Felis catus Species 0.000 description 1
- 241000724791 Filamentous phage Species 0.000 description 1
- 108060003393 Granulin Proteins 0.000 description 1
- 101001008255 Homo sapiens Immunoglobulin kappa variable 1D-8 Proteins 0.000 description 1
- 101001047628 Homo sapiens Immunoglobulin kappa variable 2-29 Proteins 0.000 description 1
- 101001008321 Homo sapiens Immunoglobulin kappa variable 2D-26 Proteins 0.000 description 1
- 101001047619 Homo sapiens Immunoglobulin kappa variable 3-20 Proteins 0.000 description 1
- 101001008263 Homo sapiens Immunoglobulin kappa variable 3D-15 Proteins 0.000 description 1
- GRSZFWQUAKGDAV-KQYNXXCUSA-N IMP Chemical compound O[C@@H]1[C@H](O)[C@@H](COP(O)(O)=O)O[C@H]1N1C(NC=NC2=O)=C2N=C1 GRSZFWQUAKGDAV-KQYNXXCUSA-N 0.000 description 1
- 102100022964 Immunoglobulin kappa variable 3-20 Human genes 0.000 description 1
- 102100034343 Integrase Human genes 0.000 description 1
- 108091092195 Intron Proteins 0.000 description 1
- 241000711828 Lyssavirus Species 0.000 description 1
- 241000124008 Mammalia Species 0.000 description 1
- 229920000057 Mannan Polymers 0.000 description 1
- 102000009112 Mannose-Binding Lectin Human genes 0.000 description 1
- 108010087870 Mannose-Binding Lectin Proteins 0.000 description 1
- 241000699673 Mesocricetus auratus Species 0.000 description 1
- 102000016943 Muramidase Human genes 0.000 description 1
- 108010014251 Muramidase Proteins 0.000 description 1
- 241000699670 Mus sp. Species 0.000 description 1
- 241000514943 Myotis grisescens Species 0.000 description 1
- 108010062010 N-Acetylmuramoyl-L-alanine Amidase Proteins 0.000 description 1
- 108091007491 NSP3 Papain-like protease domains Proteins 0.000 description 1
- 208000012902 Nervous system disease Diseases 0.000 description 1
- 208000025966 Neurological disease Diseases 0.000 description 1
- 108700026244 Open Reading Frames Proteins 0.000 description 1
- 241000283973 Oryctolagus cuniculus Species 0.000 description 1
- LPMXVESGRSUGHW-GHYGWZAOSA-N Ouabain Natural products O([C@@H]1[C@@H](O)[C@@H](O)[C@@H](O)[C@H](C)O1)[C@H]1C[C@@H](O)[C@@]2(CO)[C@@](O)(C1)CC[C@H]1[C@]3(O)[C@@](C)([C@H](C4=CC(=O)OC4)CC3)C[C@@H](O)[C@H]21 LPMXVESGRSUGHW-GHYGWZAOSA-N 0.000 description 1
- 238000012408 PCR amplification Methods 0.000 description 1
- 108090000526 Papain Proteins 0.000 description 1
- 102000057297 Pepsin A Human genes 0.000 description 1
- 108090000284 Pepsin A Proteins 0.000 description 1
- 102000007982 Phosphoproteins Human genes 0.000 description 1
- 108010089430 Phosphoproteins Proteins 0.000 description 1
- 102000004160 Phosphoric Monoester Hydrolases Human genes 0.000 description 1
- 108090000608 Phosphoric Monoester Hydrolases Proteins 0.000 description 1
- 108091000080 Phosphotransferase Proteins 0.000 description 1
- 239000004793 Polystyrene Substances 0.000 description 1
- 241000282335 Procyon Species 0.000 description 1
- 239000004365 Protease Substances 0.000 description 1
- 108010076504 Protein Sorting Signals Proteins 0.000 description 1
- 238000002123 RNA extraction Methods 0.000 description 1
- 108010092799 RNA-directed DNA polymerase Proteins 0.000 description 1
- 239000012980 RPMI-1640 medium Substances 0.000 description 1
- 101900083372 Rabies virus Glycoprotein Proteins 0.000 description 1
- 101900236200 Rabies virus Nucleoprotein Proteins 0.000 description 1
- 241000711931 Rhabdoviridae Species 0.000 description 1
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 1
- BQCADISMDOOEFD-UHFFFAOYSA-N Silver Chemical compound [Ag] BQCADISMDOOEFD-UHFFFAOYSA-N 0.000 description 1
- 108020004682 Single-Stranded DNA Proteins 0.000 description 1
- 244000166550 Strophanthus gratus Species 0.000 description 1
- 230000005867 T cell response Effects 0.000 description 1
- 210000001744 T-lymphocyte Anatomy 0.000 description 1
- 108010006785 Taq Polymerase Proteins 0.000 description 1
- 241000555295 Urocyon cinereoargenteus Species 0.000 description 1
- 108010027570 Xanthine phosphoribosyltransferase Proteins 0.000 description 1
- 210000000683 abdominal cavity Anatomy 0.000 description 1
- 238000002835 absorbance Methods 0.000 description 1
- 230000009471 action Effects 0.000 description 1
- 230000001154 acute effect Effects 0.000 description 1
- 238000001042 affinity chromatography Methods 0.000 description 1
- 125000000539 amino acid group Chemical group 0.000 description 1
- 229960003896 aminopterin Drugs 0.000 description 1
- 229960000723 ampicillin Drugs 0.000 description 1
- AVKUERGKIZMTKX-NJBDSQKTSA-N ampicillin Chemical compound C1([C@@H](N)C(=O)N[C@H]2[C@H]3SC([C@@H](N3C2=O)C(O)=O)(C)C)=CC=CC=C1 AVKUERGKIZMTKX-NJBDSQKTSA-N 0.000 description 1
- 238000000137 annealing Methods 0.000 description 1
- 239000003242 anti bacterial agent Substances 0.000 description 1
- 230000000692 anti-sense effect Effects 0.000 description 1
- 229940088710 antibiotic agent Drugs 0.000 description 1
- 239000000427 antigen Substances 0.000 description 1
- 102000036639 antigens Human genes 0.000 description 1
- 108091007433 antigens Proteins 0.000 description 1
- 239000011324 bead Substances 0.000 description 1
- 102000023732 binding proteins Human genes 0.000 description 1
- 108091008324 binding proteins Proteins 0.000 description 1
- 210000004369 blood Anatomy 0.000 description 1
- 239000008280 blood Substances 0.000 description 1
- 210000004556 brain Anatomy 0.000 description 1
- 238000010804 cDNA synthesis Methods 0.000 description 1
- 239000001506 calcium phosphate Substances 0.000 description 1
- 229910000389 calcium phosphate Inorganic materials 0.000 description 1
- 235000011010 calcium phosphates Nutrition 0.000 description 1
- 235000011089 carbon dioxide Nutrition 0.000 description 1
- 238000004113 cell culture Methods 0.000 description 1
- 239000006285 cell suspension Substances 0.000 description 1
- 229940030156 cell vaccine Drugs 0.000 description 1
- 210000002421 cell wall Anatomy 0.000 description 1
- 229960005091 chloramphenicol Drugs 0.000 description 1
- WIIZWVCIJKGZOK-RKDXNWHRSA-N chloramphenicol Chemical compound ClC(Cl)C(=O)N[C@H](CO)[C@H](O)C1=CC=C([N+]([O-])=O)C=C1 WIIZWVCIJKGZOK-RKDXNWHRSA-N 0.000 description 1
- 230000002759 chromosomal effect Effects 0.000 description 1
- 210000000349 chromosome Anatomy 0.000 description 1
- 239000013599 cloning vector Substances 0.000 description 1
- 238000004925 denaturation Methods 0.000 description 1
- 230000036425 denaturation Effects 0.000 description 1
- 238000000432 density-gradient centrifugation Methods 0.000 description 1
- 238000001514 detection method Methods 0.000 description 1
- 239000000539 dimer Substances 0.000 description 1
- 210000001840 diploid cell Anatomy 0.000 description 1
- 201000010099 disease Diseases 0.000 description 1
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 1
- 239000012153 distilled water Substances 0.000 description 1
- 229940079593 drug Drugs 0.000 description 1
- 239000003814 drug Substances 0.000 description 1
- 239000012143 dye reagent concentrate Substances 0.000 description 1
- 238000004520 electroporation Methods 0.000 description 1
- 230000008030 elimination Effects 0.000 description 1
- 238000003379 elimination reaction Methods 0.000 description 1
- 238000005516 engineering process Methods 0.000 description 1
- 230000002255 enzymatic effect Effects 0.000 description 1
- 238000002474 experimental method Methods 0.000 description 1
- 239000012894 fetal calf serum Substances 0.000 description 1
- 239000012997 ficoll-paque Substances 0.000 description 1
- 239000012467 final product Substances 0.000 description 1
- 239000012530 fluid Substances 0.000 description 1
- 102000037865 fusion proteins Human genes 0.000 description 1
- 108020001507 fusion proteins Proteins 0.000 description 1
- 230000002068 genetic effect Effects 0.000 description 1
- 230000013595 glycosylation Effects 0.000 description 1
- 238000006206 glycosylation reaction Methods 0.000 description 1
- 101150106093 gpt gene Proteins 0.000 description 1
- 230000036541 health Effects 0.000 description 1
- 208000002672 hepatitis B Diseases 0.000 description 1
- 244000052637 human pathogen Species 0.000 description 1
- 238000009396 hybridization Methods 0.000 description 1
- 230000000521 hyperimmunizing effect Effects 0.000 description 1
- 230000001900 immune effect Effects 0.000 description 1
- 230000028993 immune response Effects 0.000 description 1
- 230000036039 immunity Effects 0.000 description 1
- 230000000984 immunochemical effect Effects 0.000 description 1
- 229940099472 immunoglobulin a Drugs 0.000 description 1
- 210000003000 inclusion body Anatomy 0.000 description 1
- 235000013902 inosinic acid Nutrition 0.000 description 1
- 230000003834 intracellular effect Effects 0.000 description 1
- 238000002955 isolation Methods 0.000 description 1
- 210000003734 kidney Anatomy 0.000 description 1
- 229960000274 lysozyme Drugs 0.000 description 1
- 239000004325 lysozyme Substances 0.000 description 1
- 235000010335 lysozyme Nutrition 0.000 description 1
- 239000006249 magnetic particle Substances 0.000 description 1
- LUEWUZLMQUOBSB-GFVSVBBRSA-N mannan Chemical class O[C@H]1[C@@H](O)[C@H](O)[C@@H](CO)O[C@H]1O[C@@H]1[C@@H](CO)O[C@@H](O[C@@H]2[C@H](O[C@@H](O[C@H]3[C@H](O[C@@H](O)[C@@H](O)[C@H]3O)CO)[C@@H](O)[C@H]2O)CO)[C@H](O)[C@H]1O LUEWUZLMQUOBSB-GFVSVBBRSA-N 0.000 description 1
- 230000007246 mechanism Effects 0.000 description 1
- HPNSFSBZBAHARI-UHFFFAOYSA-N micophenolic acid Natural products OC1=C(CC=C(C)CCC(O)=O)C(OC)=C(C)C2=C1C(=O)OC2 HPNSFSBZBAHARI-UHFFFAOYSA-N 0.000 description 1
- 238000010369 molecular cloning Methods 0.000 description 1
- 229940126619 mouse monoclonal antibody Drugs 0.000 description 1
- 210000004400 mucous membrane Anatomy 0.000 description 1
- HPNSFSBZBAHARI-RUDMXATFSA-N mycophenolic acid Chemical compound OC1=C(C\C=C(/C)CCC(O)=O)C(OC)=C(C)C2=C1C(=O)OC2 HPNSFSBZBAHARI-RUDMXATFSA-N 0.000 description 1
- 229960000951 mycophenolic acid Drugs 0.000 description 1
- 210000002569 neuron Anatomy 0.000 description 1
- 230000008520 organization Effects 0.000 description 1
- LPMXVESGRSUGHW-HBYQJFLCSA-N ouabain Chemical compound O[C@@H]1[C@H](O)[C@@H](O)[C@H](C)O[C@H]1O[C@@H]1C[C@@]2(O)CC[C@H]3[C@@]4(O)CC[C@H](C=5COC(=O)C=5)[C@@]4(C)C[C@@H](O)[C@@H]3[C@@]2(CO)[C@H](O)C1 LPMXVESGRSUGHW-HBYQJFLCSA-N 0.000 description 1
- 229960003343 ouabain Drugs 0.000 description 1
- 229940055729 papain Drugs 0.000 description 1
- 235000019834 papain Nutrition 0.000 description 1
- 239000002245 particle Substances 0.000 description 1
- 239000008188 pellet Substances 0.000 description 1
- 229940111202 pepsin Drugs 0.000 description 1
- 210000005259 peripheral blood Anatomy 0.000 description 1
- 239000011886 peripheral blood Substances 0.000 description 1
- 239000007981 phosphate-citrate buffer Substances 0.000 description 1
- 229920002401 polyacrylamide Polymers 0.000 description 1
- 238000006116 polymerization reaction Methods 0.000 description 1
- 239000000256 polyoxyethylene sorbitan monolaurate Substances 0.000 description 1
- 229920002223 polystyrene Polymers 0.000 description 1
- 230000002064 post-exposure prophylaxis Effects 0.000 description 1
- 235000008476 powdered milk Nutrition 0.000 description 1
- 238000001556 precipitation Methods 0.000 description 1
- 238000002331 protein detection Methods 0.000 description 1
- 238000001243 protein synthesis Methods 0.000 description 1
- 239000002213 purine nucleotide Substances 0.000 description 1
- 150000003212 purines Chemical class 0.000 description 1
- 229940036105 rabies immunoglobulin Drugs 0.000 description 1
- 210000003079 salivary gland Anatomy 0.000 description 1
- 230000028327 secretion Effects 0.000 description 1
- 238000010187 selection method Methods 0.000 description 1
- 238000000926 separation method Methods 0.000 description 1
- 229910052709 silver Inorganic materials 0.000 description 1
- 239000004332 silver Substances 0.000 description 1
- 210000002027 skeletal muscle Anatomy 0.000 description 1
- 239000011780 sodium chloride Substances 0.000 description 1
- 239000007790 solid phase Substances 0.000 description 1
- 230000007480 spreading Effects 0.000 description 1
- 238000003892 spreading Methods 0.000 description 1
- 238000010186 staining Methods 0.000 description 1
- 230000004936 stimulating effect Effects 0.000 description 1
- 239000000725 suspension Substances 0.000 description 1
- 208000024891 symptom Diseases 0.000 description 1
- 238000004448 titration Methods 0.000 description 1
- 238000013518 transcription Methods 0.000 description 1
- 230000035897 transcription Effects 0.000 description 1
- 238000001890 transfection Methods 0.000 description 1
- 230000009466 transformation Effects 0.000 description 1
- 238000013519 translation Methods 0.000 description 1
- QORWJWZARLRLPR-UHFFFAOYSA-H tricalcium bis(phosphate) Chemical compound [Ca+2].[Ca+2].[Ca+2].[O-]P([O-])([O-])=O.[O-]P([O-])([O-])=O QORWJWZARLRLPR-UHFFFAOYSA-H 0.000 description 1
- 238000011144 upstream manufacturing Methods 0.000 description 1
- 230000029812 viral genome replication Effects 0.000 description 1
- 210000002845 virion Anatomy 0.000 description 1
Classifications
-
- 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
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P25/00—Drugs for disorders of the nervous system
-
- 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
-
- 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
- C07K2317/21—Immunoglobulins specific features characterized by taxonomic origin from primates, e.g. man
Landscapes
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Virology (AREA)
- Organic Chemistry (AREA)
- Medicinal Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Public Health (AREA)
- Veterinary Medicine (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Pharmacology & Pharmacy (AREA)
- Animal Behavior & Ethology (AREA)
- General Chemical & Material Sciences (AREA)
- Molecular Biology (AREA)
- Biochemistry (AREA)
- Genetics & Genomics (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Communicable Diseases (AREA)
- Biophysics (AREA)
- Oncology (AREA)
- Immunology (AREA)
- Neurosurgery (AREA)
- Neurology (AREA)
- Biomedical Technology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Engineering & Computer Science (AREA)
- Peptides Or Proteins (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US20451800P | 2000-05-16 | 2000-05-16 | |
| US60/204,518 | 2000-05-16 |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| RU2002133470A RU2002133470A (ru) | 2004-06-10 |
| RU2272809C2 true RU2272809C2 (ru) | 2006-03-27 |
Family
ID=22758233
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| RU2002133470/13A RU2272809C2 (ru) | 2000-05-16 | 2001-05-04 | Специфичные в отношении вируса бешенства нейтрализующие моноклональные антитела человека и нуклеиновые кислоты и связанные с ними способы |
Country Status (9)
| Country | Link |
|---|---|
| US (1) | US6890532B2 (enExample) |
| EP (1) | EP1282703B1 (enExample) |
| JP (1) | JP4819285B2 (enExample) |
| AT (1) | ATE411387T1 (enExample) |
| CA (1) | CA2419148C (enExample) |
| DE (1) | DE60136174D1 (enExample) |
| IL (1) | IL152825A (enExample) |
| RU (1) | RU2272809C2 (enExample) |
| WO (1) | WO2001088132A2 (enExample) |
Cited By (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| RU2533802C1 (ru) * | 2013-08-30 | 2014-11-20 | федеральное государственное бюджетное учреждение "Научно-исследовательский институт эпидемиологии и микробиологии имени почетного академика Н.Ф. Гамалеи" Министерства здравоохранения Российской Федерации | Тримеризованное однодоменное антитело, специфически связывающееся с гликопротеином g вируса бешенства, нейтрализующее вирус бешенства |
Families Citing this family (18)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US20040013672A1 (en) * | 2000-05-16 | 2004-01-22 | Thomas Jefferson University | Recombinant antibodies, and compositions and methods for making and using the same |
| WO2002016437A2 (en) * | 2000-08-24 | 2002-02-28 | Thomas Jefferson University | Rhabdovirus-based vectors to express high levels of functional human antibodies |
| ATE557040T1 (de) * | 2001-08-21 | 2012-05-15 | Univ Jefferson | Rekombinante antikörper sowie zusammensetzungen und verfahren zu deren herstellung und verwendung |
| US7084257B2 (en) | 2001-10-05 | 2006-08-01 | Amgen Inc. | Fully human antibody Fab fragments with human interferon-gamma neutralizing activity |
| USRE47770E1 (en) | 2002-07-18 | 2019-12-17 | Merus N.V. | Recombinant production of mixtures of antibodies |
| SI1523496T1 (sl) | 2002-07-18 | 2011-11-30 | Merus B V | Rekombinantno proizvajanje zmesi protiteles |
| US20100069614A1 (en) | 2008-06-27 | 2010-03-18 | Merus B.V. | Antibody producing non-human mammals |
| EP2395017A3 (en) * | 2003-05-30 | 2012-12-19 | Merus B.V. | Design and use of paired variable regions of specific binding molecules |
| EP1737971B1 (en) | 2004-01-20 | 2017-08-16 | Merus N.V. | Mixtures of binding proteins |
| SI1851315T1 (sl) * | 2005-02-02 | 2014-06-30 | University Of Massachusetts | Humana protitelesa proti steklini in njihova uporaba |
| JP2008263964A (ja) * | 2007-03-29 | 2008-11-06 | Yamaguchi Univ | コウモリ由来細胞株 |
| JP2010085126A (ja) * | 2008-09-29 | 2010-04-15 | Adtec Kk | 狂犬病ウイルス中和抗体価判定具および狂犬病ウイルス中和抗体価の測定方法 |
| KR101388680B1 (ko) * | 2011-03-18 | 2014-04-28 | (주)셀트리온 | 광견병 바이러스를 중화시킬 수 있는 결합 분자 |
| ES2743399T3 (es) | 2012-04-20 | 2020-02-19 | Merus Nv | Métodos y medios para la producción de moléculas heterodiméricas similares a Ig |
| WO2019227039A1 (en) * | 2018-05-24 | 2019-11-28 | Lankenau Institute For Medical Research | Compositions comprising antibodies to rabies virus and the uses thereof |
| CN111166877A (zh) * | 2019-12-30 | 2020-05-19 | 西安回天血液制品有限责任公司 | 一种狂犬病人免疫球蛋白的制备方法 |
| CN114958774B (zh) * | 2022-05-08 | 2023-10-27 | 中国医学科学院医学生物学研究所 | 抗狂犬病病毒单克隆抗体及分泌该抗体的杂交瘤细胞株与应用 |
| CN119431525B (zh) * | 2024-10-08 | 2025-04-11 | 北京溯本源和生物科技有限公司 | 狂犬病毒g蛋白重组抗原、单克隆抗体及其制备方法和应用 |
Family Cites Families (6)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| GB8607679D0 (en) | 1986-03-27 | 1986-04-30 | Winter G P | Recombinant dna product |
| IL89489A0 (en) | 1988-03-09 | 1989-09-10 | Hybritech Inc | Chimeric antibodies directed against human carcinoembryonic antigen |
| AU3432389A (en) | 1988-04-07 | 1989-11-03 | Farmitalia Carlo Erba S.R.L. | Human monoclonal antibodies against rabies virus |
| EP0362371A4 (en) | 1988-04-15 | 1990-10-24 | Protein Design Labs, Inc. | Il-2 receptor-specific chimeric antibodies |
| ATE119198T1 (de) | 1988-04-16 | 1995-03-15 | Celltech Ltd | Verfahren zur herstellung von proteinen mittels rekombinanter dna. |
| WO1993021319A1 (en) | 1992-04-08 | 1993-10-28 | Cetus Oncology Corporation | HUMANIZED C-erbB-2 SPECIFIC ANTIBODIES |
-
2001
- 2001-05-04 IL IL152825A patent/IL152825A/en not_active IP Right Cessation
- 2001-05-04 DE DE60136174T patent/DE60136174D1/de not_active Expired - Lifetime
- 2001-05-04 AT AT01933020T patent/ATE411387T1/de not_active IP Right Cessation
- 2001-05-04 EP EP01933020A patent/EP1282703B1/en not_active Expired - Lifetime
- 2001-05-04 RU RU2002133470/13A patent/RU2272809C2/ru not_active IP Right Cessation
- 2001-05-04 WO PCT/US2001/014468 patent/WO2001088132A2/en not_active Ceased
- 2001-05-04 US US09/848,832 patent/US6890532B2/en not_active Expired - Lifetime
- 2001-05-04 CA CA2419148A patent/CA2419148C/en not_active Expired - Fee Related
- 2001-05-04 JP JP2001584514A patent/JP4819285B2/ja not_active Expired - Fee Related
Non-Patent Citations (1)
| Title |
|---|
| CHEUNG et al., A recombinant human Fab expressed in Escherichia coli neutralizes rabies virus, Journal of virology, Nov.1992, стр.6714-6720. PATERSON et al., Variation in IgG1 heavy chain allotype does not con-tribute to differences in biological activity of two human anti-Rhesus (D) monoclonal antibodies, Immunotechnology, 1998, Jun, 4 (1): стр.37-47. http://ww../query.fcgi&cmd=Retrieve&db=Protein&list_uids=11275302&do pt=GenPep, Submitted 17.05.1999 Masataka Takekoshi. * |
Cited By (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| RU2533802C1 (ru) * | 2013-08-30 | 2014-11-20 | федеральное государственное бюджетное учреждение "Научно-исследовательский институт эпидемиологии и микробиологии имени почетного академика Н.Ф. Гамалеи" Министерства здравоохранения Российской Федерации | Тримеризованное однодоменное антитело, специфически связывающееся с гликопротеином g вируса бешенства, нейтрализующее вирус бешенства |
Also Published As
| Publication number | Publication date |
|---|---|
| DE60136174D1 (de) | 2008-11-27 |
| WO2001088132A2 (en) | 2001-11-22 |
| CA2419148C (en) | 2011-07-12 |
| WO2001088132A3 (en) | 2002-07-18 |
| IL152825A0 (en) | 2003-06-24 |
| JP2004528803A (ja) | 2004-09-24 |
| US6890532B2 (en) | 2005-05-10 |
| IL152825A (en) | 2009-07-20 |
| EP1282703A2 (en) | 2003-02-12 |
| CA2419148A1 (en) | 2001-11-22 |
| ATE411387T1 (de) | 2008-10-15 |
| EP1282703B1 (en) | 2008-10-15 |
| US20030165507A1 (en) | 2003-09-04 |
| JP4819285B2 (ja) | 2011-11-24 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| RU2272809C2 (ru) | Специфичные в отношении вируса бешенства нейтрализующие моноклональные антитела человека и нуклеиновые кислоты и связанные с ними способы | |
| CN113354729B (zh) | 一种抗新型冠状病毒的单克隆抗体及其应用 | |
| EP0690132B1 (en) | Anti-hiv monoclonal antibody | |
| RU2764740C1 (ru) | Биспецифическое антитело против вируса бешенства и его применение | |
| CA2091335A1 (en) | Antibodies for treatment and prevention of infection in animals and man | |
| RU2292353C2 (ru) | Рекомбинантные антитела и композиции, а также способы их создания и использования | |
| JPWO1994020632A1 (ja) | 抗ｈｉｖモノクローナル抗体 | |
| WO2004076677A2 (en) | Monoclonal antibody production by ebv transformation of b cells | |
| CN113354730B (zh) | 一种抗新型冠状病毒的单克隆抗体及其应用 | |
| CN103221063B (zh) | 针对人类巨细胞病毒(cmv)gb蛋白质的高亲和力人类抗体 | |
| AU2002332600A1 (en) | Recombinant antibodies, and compositions and methods for making and using the same | |
| Hamilton et al. | A humanized antibody against human cytomegalovirus (CMV) gpUL75 (gH) for prophylaxis or treatment of CMV infections | |
| WO1994028933A1 (en) | Bispecific human monoclonal antibodies specific for human immunodeficiency virus | |
| CN113748203B (zh) | 重组经典猪瘟病毒 | |
| Cheung et al. | A recombinant human Fab expressed in Escherichia coli neutralizes rabies virus | |
| US7071319B2 (en) | Recombinant antibodies, and compositions and methods for making and using the same | |
| CN114957479B (zh) | 抗H1N1流感病毒双特异性中和抗体Bis-Hu11-1及其应用 | |
| CN118530348A (zh) | 一种广谱中和冠状病毒的抗体及其应用 | |
| JP4263951B2 (ja) | イヌ化抗体の作成方法および使用 | |
| RU2793967C1 (ru) | Однодоменное антитело ламы Н5 и его производное H5-Fc, специфически связывающие RBD-домен S-белка вируса SARS-CoV-2, обладающие вируснейтрализующей активностью | |
| RU2769223C1 (ru) | Средство и способ терапии и экстренной профилактики заболеваний, вызываемых вирусом SARS-CoV-2 на основе рекомбинантного антитела и гуманизированного моноклонального антитела | |
| RU2765731C1 (ru) | Гуманизированное моноклональное антитело, специфически связывающиеся с RBD S белка вируса SARS-CoV-2, средство и способ для терапии и экстренной профилактики заболеваний, вызываемых вирусом SARS-CoV-2 | |
| HK1071898B (en) | Recombinant antibodies, and compositions and methods for making and using the same | |
| US20020115143A1 (en) | Rhabdovirus-based vectors to express high levels of functional human antibodies | |
| JPH06506947A (ja) | 抗ウィルスハイブリッド抗体 |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| MM4A | The patent is invalid due to non-payment of fees |
Effective date: 20190505 |