ES2210832T3 - Secuencias de aminoacidos para uso terapeutico y profilactico contra enfermedades debidas a las toxinas de clostridium difficile. - Google Patents
Secuencias de aminoacidos para uso terapeutico y profilactico contra enfermedades debidas a las toxinas de clostridium difficile.Info
- Publication number
- ES2210832T3 ES2210832T3 ES98951374T ES98951374T ES2210832T3 ES 2210832 T3 ES2210832 T3 ES 2210832T3 ES 98951374 T ES98951374 T ES 98951374T ES 98951374 T ES98951374 T ES 98951374T ES 2210832 T3 ES2210832 T3 ES 2210832T3
- Authority
- ES
- Spain
- Prior art keywords
- baselineskip
- seq
- sequence
- antibody
- antibodies
- 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
- 241000193163 Clostridioides difficile Species 0.000 title claims abstract description 27
- 150000001413 amino acids Chemical class 0.000 title claims description 38
- 239000003053 toxin Substances 0.000 title abstract description 21
- 231100000765 toxin Toxicity 0.000 title abstract description 21
- 108700012359 toxins Proteins 0.000 title abstract description 21
- 201000010099 disease Diseases 0.000 title abstract description 16
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 title abstract description 16
- 230000001225 therapeutic effect Effects 0.000 title abstract description 8
- 101710182532 Toxin a Proteins 0.000 claims abstract description 17
- 101710084578 Short neurotoxin 1 Proteins 0.000 claims abstract description 15
- 210000004408 hybridoma Anatomy 0.000 claims description 13
- 108091028043 Nucleic acid sequence Proteins 0.000 claims description 10
- 230000004071 biological effect Effects 0.000 claims description 3
- 125000003275 alpha amino acid group Chemical group 0.000 claims 7
- 238000004519 manufacturing process Methods 0.000 abstract description 15
- 239000003446 ligand Substances 0.000 abstract description 7
- 230000003472 neutralizing effect Effects 0.000 abstract description 7
- 101710146739 Enterotoxin Proteins 0.000 abstract description 6
- 230000003197 catalytic effect Effects 0.000 abstract description 6
- 239000000147 enterotoxin Substances 0.000 abstract description 6
- 231100000655 enterotoxin Toxicity 0.000 abstract description 6
- 230000005945 translocation Effects 0.000 abstract description 6
- 101710182223 Toxin B Proteins 0.000 abstract description 5
- 231100000599 cytotoxic agent Toxicity 0.000 abstract description 5
- 239000002619 cytotoxin Substances 0.000 abstract description 5
- 101710112752 Cytotoxin Proteins 0.000 abstract description 4
- 230000000069 prophylactic effect Effects 0.000 abstract description 4
- 108090000623 proteins and genes Proteins 0.000 description 35
- 101000845196 Homo sapiens Tetratricopeptide repeat protein 8 Proteins 0.000 description 32
- 102100031271 Tetratricopeptide repeat protein 8 Human genes 0.000 description 32
- 210000004027 cell Anatomy 0.000 description 16
- 238000000034 method Methods 0.000 description 16
- 108090000765 processed proteins & peptides Proteins 0.000 description 15
- 241000196324 Embryophyta Species 0.000 description 13
- 108091032973 (ribonucleotides)n+m Proteins 0.000 description 12
- 239000002299 complementary DNA Substances 0.000 description 12
- 239000013615 primer Substances 0.000 description 12
- 206010009657 Clostridium difficile colitis Diseases 0.000 description 11
- 102000004169 proteins and genes Human genes 0.000 description 11
- 208000003100 Pseudomembranous Enterocolitis Diseases 0.000 description 10
- 206010037128 Pseudomembranous colitis Diseases 0.000 description 10
- 239000012634 fragment Substances 0.000 description 10
- 239000002773 nucleotide Substances 0.000 description 10
- 102000004196 processed proteins & peptides Human genes 0.000 description 10
- 241000894007 species Species 0.000 description 10
- 238000006243 chemical reaction Methods 0.000 description 9
- 125000003729 nucleotide group Chemical group 0.000 description 9
- UDPGUMQDCGORJQ-UHFFFAOYSA-N (2-chloroethyl)phosphonic acid Chemical compound OP(O)(=O)CCCl UDPGUMQDCGORJQ-UHFFFAOYSA-N 0.000 description 8
- 238000004690 coupled electron pair approximation Methods 0.000 description 8
- 230000035772 mutation Effects 0.000 description 8
- 238000002560 therapeutic procedure Methods 0.000 description 8
- 241000282412 Homo Species 0.000 description 7
- 108020004999 messenger RNA Proteins 0.000 description 7
- 239000013598 vector Substances 0.000 description 7
- 230000003321 amplification Effects 0.000 description 6
- 238000003199 nucleic acid amplification method Methods 0.000 description 6
- 241000699666 Mus <mouse, genus> Species 0.000 description 5
- 241000699670 Mus sp. Species 0.000 description 5
- 238000011321 prophylaxis Methods 0.000 description 5
- 238000000746 purification Methods 0.000 description 5
- 208000024891 symptom Diseases 0.000 description 5
- 206010012735 Diarrhoea Diseases 0.000 description 4
- 108060003951 Immunoglobulin Proteins 0.000 description 4
- 108010076504 Protein Sorting Signals Proteins 0.000 description 4
- 238000007792 addition Methods 0.000 description 4
- 239000003242 anti bacterial agent Substances 0.000 description 4
- 229940088710 antibiotic agent Drugs 0.000 description 4
- AIYUHDOJVYHVIT-UHFFFAOYSA-M caesium chloride Chemical compound [Cl-].[Cs+] AIYUHDOJVYHVIT-UHFFFAOYSA-M 0.000 description 4
- 238000010367 cloning Methods 0.000 description 4
- 239000003814 drug Substances 0.000 description 4
- 230000000694 effects Effects 0.000 description 4
- 210000004602 germ cell Anatomy 0.000 description 4
- 102000018358 immunoglobulin Human genes 0.000 description 4
- KWGKDLIKAYFUFQ-UHFFFAOYSA-M lithium chloride Chemical compound [Li+].[Cl-] KWGKDLIKAYFUFQ-UHFFFAOYSA-M 0.000 description 4
- 239000011049 pearl Substances 0.000 description 4
- 150000003839 salts Chemical class 0.000 description 4
- 230000009466 transformation Effects 0.000 description 4
- 102000004190 Enzymes Human genes 0.000 description 3
- 108090000790 Enzymes Proteins 0.000 description 3
- 239000000427 antigen Substances 0.000 description 3
- 108091007433 antigens Proteins 0.000 description 3
- 102000036639 antigens Human genes 0.000 description 3
- 230000031018 biological processes and functions Effects 0.000 description 3
- 239000000872 buffer Substances 0.000 description 3
- 229940088598 enzyme Drugs 0.000 description 3
- 230000002163 immunogen Effects 0.000 description 3
- 230000003252 repetitive effect Effects 0.000 description 3
- 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 2
- FNXCAFKDGBROCU-STECZYCISA-N Arg-Ile-Tyr Chemical compound NC(N)=NCCC[C@H](N)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@H](C(O)=O)CC1=CC=C(O)C=C1 FNXCAFKDGBROCU-STECZYCISA-N 0.000 description 2
- CGYKCTPUGXFPMG-IHPCNDPISA-N Asn-Tyr-Trp Chemical compound [H]N[C@@H](CC(N)=O)C(=O)N[C@@H](CC1=CC=C(O)C=C1)C(=O)N[C@@H](CC1=CNC2=C1C=CC=C2)C(O)=O CGYKCTPUGXFPMG-IHPCNDPISA-N 0.000 description 2
- 241000894006 Bacteria Species 0.000 description 2
- 241000699800 Cricetinae Species 0.000 description 2
- SRBFZHDQGSBBOR-IOVATXLUSA-N D-xylopyranose Chemical compound O[C@@H]1COC(O)[C@H](O)[C@H]1O SRBFZHDQGSBBOR-IOVATXLUSA-N 0.000 description 2
- 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 2
- LMPBBFWHCRURJD-LAEOZQHASA-N Gln-Asn-Val Chemical compound CC(C)[C@@H](C(=O)O)NC(=O)[C@H](CC(=O)N)NC(=O)[C@H](CCC(=O)N)N LMPBBFWHCRURJD-LAEOZQHASA-N 0.000 description 2
- LOJYQMFIIJVETK-WDSKDSINSA-N Gln-Gln Chemical compound NC(=O)CC[C@H](N)C(=O)N[C@@H](CCC(N)=O)C(O)=O LOJYQMFIIJVETK-WDSKDSINSA-N 0.000 description 2
- KMSGYZQRXPUKGI-BYPYZUCNSA-N Gly-Gly-Asn Chemical compound NCC(=O)NCC(=O)N[C@H](C(O)=O)CC(N)=O KMSGYZQRXPUKGI-BYPYZUCNSA-N 0.000 description 2
- MHZXESQPPXOING-KBPBESRZSA-N Gly-Lys-Phe Chemical compound [H]NCC(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC1=CC=CC=C1)C(O)=O MHZXESQPPXOING-KBPBESRZSA-N 0.000 description 2
- FKESCSGWBPUTPN-FOHZUACHSA-N Gly-Thr-Asn Chemical compound [H]NCC(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CC(N)=O)C(O)=O FKESCSGWBPUTPN-FOHZUACHSA-N 0.000 description 2
- 108700023372 Glycosyltransferases Proteins 0.000 description 2
- SWBUZLFWGJETAO-KKUMJFAQSA-N His-Tyr-Asn Chemical compound C1=CC(=CC=C1C[C@@H](C(=O)N[C@@H](CC(=O)N)C(=O)O)NC(=O)[C@H](CC2=CN=CN2)N)O SWBUZLFWGJETAO-KKUMJFAQSA-N 0.000 description 2
- FADYJNXDPBKVCA-UHFFFAOYSA-N L-Phenylalanyl-L-lysin Natural products NCCCCC(C(O)=O)NC(=O)C(N)CC1=CC=CC=C1 FADYJNXDPBKVCA-UHFFFAOYSA-N 0.000 description 2
- UWKNTTJNVSYXPC-CIUDSAMLSA-N Lys-Ala-Ser Chemical compound OC[C@@H](C(O)=O)NC(=O)[C@H](C)NC(=O)[C@@H](N)CCCCN UWKNTTJNVSYXPC-CIUDSAMLSA-N 0.000 description 2
- 241001465754 Metazoa Species 0.000 description 2
- 241000713869 Moloney murine leukemia virus Species 0.000 description 2
- 108091007491 NSP3 Papain-like protease domains Proteins 0.000 description 2
- 102000005348 Neuraminidase Human genes 0.000 description 2
- 108010006232 Neuraminidase Proteins 0.000 description 2
- 244000061176 Nicotiana tabacum Species 0.000 description 2
- 235000002637 Nicotiana tabacum Nutrition 0.000 description 2
- 108091034117 Oligonucleotide Proteins 0.000 description 2
- 238000012408 PCR amplification Methods 0.000 description 2
- ULIWFCCJIOEHMU-BQBZGAKWSA-N Pro-Gly-Asp Chemical compound OC(=O)C[C@@H](C(O)=O)NC(=O)CNC(=O)[C@@H]1CCCN1 ULIWFCCJIOEHMU-BQBZGAKWSA-N 0.000 description 2
- 108010025216 RVF peptide Proteins 0.000 description 2
- AZWNCEBQZXELEZ-FXQIFTODSA-N Ser-Pro-Ser Chemical compound OC[C@H](N)C(=O)N1CCC[C@H]1C(=O)N[C@@H](CO)C(O)=O AZWNCEBQZXELEZ-FXQIFTODSA-N 0.000 description 2
- 239000007983 Tris buffer Substances 0.000 description 2
- DYEGCOJHFNJBKB-UFYCRDLUSA-N Tyr-Arg-Tyr Chemical compound C([C@H](N)C(=O)N[C@@H](CCCN=C(N)N)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(O)=O)C1=CC=C(O)C=C1 DYEGCOJHFNJBKB-UFYCRDLUSA-N 0.000 description 2
- SCCKSNREWHMKOJ-SRVKXCTJSA-N Tyr-Asn-Ser Chemical compound N[C@@H](Cc1ccc(O)cc1)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CO)C(O)=O SCCKSNREWHMKOJ-SRVKXCTJSA-N 0.000 description 2
- BARBHMSSVWPKPZ-IHRRRGAJSA-N Tyr-Asp-Arg Chemical compound [H]N[C@@H](CC1=CC=C(O)C=C1)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CCCNC(N)=N)C(O)=O BARBHMSSVWPKPZ-IHRRRGAJSA-N 0.000 description 2
- BIWVVOHTKDLRMP-ULQDDVLXSA-N Tyr-Pro-Leu Chemical compound [H]N[C@@H](CC1=CC=C(O)C=C1)C(=O)N1CCC[C@H]1C(=O)N[C@@H](CC(C)C)C(O)=O BIWVVOHTKDLRMP-ULQDDVLXSA-N 0.000 description 2
- BCBFMJYTNKDALA-UFYCRDLUSA-N Val-Phe-Phe Chemical compound N[C@@H](C(C)C)C(=O)N[C@@H](CC1=CC=CC=C1)C(=O)N[C@@H](CC1=CC=CC=C1)C(=O)O BCBFMJYTNKDALA-UFYCRDLUSA-N 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
- 230000009471 action Effects 0.000 description 2
- 238000004458 analytical method Methods 0.000 description 2
- 238000013459 approach Methods 0.000 description 2
- PYMYPHUHKUWMLA-UHFFFAOYSA-N arabinose Natural products OCC(O)C(O)C(O)C=O PYMYPHUHKUWMLA-UHFFFAOYSA-N 0.000 description 2
- 108010038850 arginyl-isoleucyl-tyrosine Proteins 0.000 description 2
- 108010031045 aspartyl-glycyl-aspartyl-alanine Proteins 0.000 description 2
- 108010068265 aspartyltyrosine Proteins 0.000 description 2
- SRBFZHDQGSBBOR-UHFFFAOYSA-N beta-D-Pyranose-Lyxose Natural products OC1COC(O)C(O)C1O SRBFZHDQGSBBOR-UHFFFAOYSA-N 0.000 description 2
- 102000023732 binding proteins Human genes 0.000 description 2
- 108091008324 binding proteins Proteins 0.000 description 2
- 210000004899 c-terminal region Anatomy 0.000 description 2
- 230000001413 cellular effect Effects 0.000 description 2
- 230000008859 change Effects 0.000 description 2
- 239000003795 chemical substances by application Substances 0.000 description 2
- 229960002227 clindamycin Drugs 0.000 description 2
- KDLRVYVGXIQJDK-AWPVFWJPSA-N clindamycin Chemical compound CN1C[C@H](CCC)C[C@H]1C(=O)N[C@H]([C@H](C)Cl)[C@@H]1[C@H](O)[C@H](O)[C@@H](O)[C@@H](SC)O1 KDLRVYVGXIQJDK-AWPVFWJPSA-N 0.000 description 2
- 239000000824 cytostatic agent Substances 0.000 description 2
- 230000036425 denaturation Effects 0.000 description 2
- 238000004925 denaturation Methods 0.000 description 2
- 230000029087 digestion Effects 0.000 description 2
- 239000003792 electrolyte Substances 0.000 description 2
- 208000010227 enterocolitis Diseases 0.000 description 2
- 238000002474 experimental method Methods 0.000 description 2
- 102000045442 glycosyltransferase activity proteins Human genes 0.000 description 2
- 108700014210 glycosyltransferase activity proteins Proteins 0.000 description 2
- 230000008105 immune reaction Effects 0.000 description 2
- 230000028993 immune response Effects 0.000 description 2
- 238000010348 incorporation Methods 0.000 description 2
- 230000000968 intestinal effect Effects 0.000 description 2
- 231100000518 lethal Toxicity 0.000 description 2
- 230000001665 lethal effect Effects 0.000 description 2
- 239000007788 liquid Substances 0.000 description 2
- 108010064235 lysylglycine Proteins 0.000 description 2
- 150000002772 monosaccharides Chemical class 0.000 description 2
- 231100000252 nontoxic Toxicity 0.000 description 2
- 230000003000 nontoxic effect Effects 0.000 description 2
- 108020003175 receptors Proteins 0.000 description 2
- 102000005962 receptors Human genes 0.000 description 2
- 229940051173 recombinant immunotoxin Drugs 0.000 description 2
- 230000004044 response Effects 0.000 description 2
- 239000013049 sediment Substances 0.000 description 2
- 239000000243 solution Substances 0.000 description 2
- 238000005496 tempering Methods 0.000 description 2
- 238000012360 testing method Methods 0.000 description 2
- 238000012546 transfer Methods 0.000 description 2
- 230000009261 transgenic effect Effects 0.000 description 2
- 238000011282 treatment Methods 0.000 description 2
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 2
- 238000002255 vaccination Methods 0.000 description 2
- JBFQOLHAGBKPTP-NZATWWQASA-N (2s)-2-[[(2s)-4-carboxy-2-[[3-carboxy-2-[[(2s)-2,6-diaminohexanoyl]amino]propanoyl]amino]butanoyl]amino]-4-methylpentanoic acid Chemical compound CC(C)C[C@@H](C(O)=O)NC(=O)[C@H](CCC(O)=O)NC(=O)C(CC(O)=O)NC(=O)[C@@H](N)CCCCN JBFQOLHAGBKPTP-NZATWWQASA-N 0.000 description 1
- 208000004998 Abdominal Pain Diseases 0.000 description 1
- 241000589158 Agrobacterium Species 0.000 description 1
- 241000193830 Bacillus <bacterium> Species 0.000 description 1
- 240000002791 Brassica napus Species 0.000 description 1
- 235000004977 Brassica sinapistrum Nutrition 0.000 description 1
- 241000193403 Clostridium Species 0.000 description 1
- 208000037384 Clostridium Infections Diseases 0.000 description 1
- 206010054236 Clostridium difficile infection Diseases 0.000 description 1
- 108091026890 Coding region Proteins 0.000 description 1
- 241000699802 Cricetulus griseus Species 0.000 description 1
- WQZGKKKJIJFFOK-QTVWNMPRSA-N D-mannopyranose Chemical compound OC[C@H]1OC(O)[C@@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-QTVWNMPRSA-N 0.000 description 1
- 108020004414 DNA Proteins 0.000 description 1
- 102000053602 DNA Human genes 0.000 description 1
- 239000003155 DNA primer Substances 0.000 description 1
- 244000000626 Daucus carota Species 0.000 description 1
- 235000002767 Daucus carota Nutrition 0.000 description 1
- 241000588724 Escherichia coli Species 0.000 description 1
- 241000233866 Fungi Species 0.000 description 1
- WQZGKKKJIJFFOK-GASJEMHNSA-N Glucose Natural products OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-GASJEMHNSA-N 0.000 description 1
- 208000032843 Hemorrhage Diseases 0.000 description 1
- 240000005979 Hordeum vulgare Species 0.000 description 1
- 235000007340 Hordeum vulgare Nutrition 0.000 description 1
- 102000001706 Immunoglobulin Fab Fragments Human genes 0.000 description 1
- 108010054477 Immunoglobulin Fab Fragments Proteins 0.000 description 1
- 102000008394 Immunoglobulin Fragments Human genes 0.000 description 1
- 108010021625 Immunoglobulin Fragments Proteins 0.000 description 1
- 108700005091 Immunoglobulin Genes Proteins 0.000 description 1
- 102100034343 Integrase Human genes 0.000 description 1
- 241000209510 Liliopsida Species 0.000 description 1
- 102000016943 Muramidase Human genes 0.000 description 1
- 108010014251 Muramidase Proteins 0.000 description 1
- 241001529936 Murinae Species 0.000 description 1
- 108010062010 N-Acetylmuramoyl-L-alanine Amidase Proteins 0.000 description 1
- OVRNDRQMDRJTHS-UHFFFAOYSA-N N-acelyl-D-glucosamine Natural products CC(=O)NC1C(O)OC(CO)C(O)C1O OVRNDRQMDRJTHS-UHFFFAOYSA-N 0.000 description 1
- OVRNDRQMDRJTHS-FMDGEEDCSA-N N-acetyl-beta-D-glucosamine Chemical compound CC(=O)N[C@H]1[C@H](O)O[C@H](CO)[C@@H](O)[C@@H]1O OVRNDRQMDRJTHS-FMDGEEDCSA-N 0.000 description 1
- SQVRNKJHWKZAKO-PFQGKNLYSA-N N-acetyl-beta-neuraminic acid Chemical compound CC(=O)N[C@@H]1[C@@H](O)C[C@@](O)(C(O)=O)O[C@H]1[C@H](O)[C@H](O)CO SQVRNKJHWKZAKO-PFQGKNLYSA-N 0.000 description 1
- MBLBDJOUHNCFQT-LXGUWJNJSA-N N-acetylglucosamine Natural products CC(=O)N[C@@H](C=O)[C@@H](O)[C@H](O)[C@H](O)CO MBLBDJOUHNCFQT-LXGUWJNJSA-N 0.000 description 1
- -1 Nucleotide triphosphates Chemical class 0.000 description 1
- 108700026244 Open Reading Frames Proteins 0.000 description 1
- 206010033128 Ovarian cancer Diseases 0.000 description 1
- 240000004713 Pisum sativum Species 0.000 description 1
- 235000010582 Pisum sativum Nutrition 0.000 description 1
- 108020005120 Plant DNA Proteins 0.000 description 1
- 239000004793 Polystyrene Substances 0.000 description 1
- 206010037660 Pyrexia Diseases 0.000 description 1
- 108010092799 RNA-directed DNA polymerase Proteins 0.000 description 1
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 description 1
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 description 1
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 1
- 244000061456 Solanum tuberosum Species 0.000 description 1
- 235000002595 Solanum tuberosum Nutrition 0.000 description 1
- 235000021307 Triticum Nutrition 0.000 description 1
- 244000098338 Triticum aestivum Species 0.000 description 1
- 108010059993 Vancomycin Proteins 0.000 description 1
- 239000002253 acid Substances 0.000 description 1
- 230000006978 adaptation Effects 0.000 description 1
- 239000011543 agarose gel Substances 0.000 description 1
- 230000004075 alteration Effects 0.000 description 1
- 238000004873 anchoring Methods 0.000 description 1
- PYMYPHUHKUWMLA-WDCZJNDASA-N arabinose Chemical compound OC[C@@H](O)[C@@H](O)[C@H](O)C=O PYMYPHUHKUWMLA-WDCZJNDASA-N 0.000 description 1
- 230000001580 bacterial effect Effects 0.000 description 1
- 239000011324 bead Substances 0.000 description 1
- 230000008901 benefit Effects 0.000 description 1
- WQZGKKKJIJFFOK-VFUOTHLCSA-N beta-D-glucose Chemical compound OC[C@H]1O[C@@H](O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-VFUOTHLCSA-N 0.000 description 1
- 108010005774 beta-Galactosidase Proteins 0.000 description 1
- 102000005936 beta-Galactosidase Human genes 0.000 description 1
- SQVRNKJHWKZAKO-UHFFFAOYSA-N beta-N-Acetyl-D-neuraminic acid Natural products CC(=O)NC1C(O)CC(O)(C(O)=O)OC1C(O)C(O)CO SQVRNKJHWKZAKO-UHFFFAOYSA-N 0.000 description 1
- 230000003115 biocidal effect Effects 0.000 description 1
- 208000034158 bleeding Diseases 0.000 description 1
- 230000000740 bleeding effect Effects 0.000 description 1
- 230000000903 blocking effect Effects 0.000 description 1
- 230000037396 body weight Effects 0.000 description 1
- 238000010804 cDNA synthesis Methods 0.000 description 1
- 238000005119 centrifugation Methods 0.000 description 1
- 230000009920 chelation Effects 0.000 description 1
- 210000004978 chinese hamster ovary cell Anatomy 0.000 description 1
- 238000004587 chromatography analysis Methods 0.000 description 1
- 206010009887 colitis Diseases 0.000 description 1
- 230000000295 complement effect Effects 0.000 description 1
- 238000010276 construction Methods 0.000 description 1
- 230000008878 coupling Effects 0.000 description 1
- 238000010168 coupling process Methods 0.000 description 1
- 238000005859 coupling reaction Methods 0.000 description 1
- 238000005520 cutting process Methods 0.000 description 1
- 231100000433 cytotoxic Toxicity 0.000 description 1
- 230000001472 cytotoxic effect Effects 0.000 description 1
- 230000007547 defect Effects 0.000 description 1
- 238000012217 deletion Methods 0.000 description 1
- 230000037430 deletion Effects 0.000 description 1
- 230000008021 deposition Effects 0.000 description 1
- 238000011161 development Methods 0.000 description 1
- 238000003745 diagnosis Methods 0.000 description 1
- 238000004090 dissolution Methods 0.000 description 1
- 229940079593 drug Drugs 0.000 description 1
- 230000008030 elimination Effects 0.000 description 1
- 238000003379 elimination reaction Methods 0.000 description 1
- 210000002472 endoplasmic reticulum Anatomy 0.000 description 1
- 241001233957 eudicotyledons Species 0.000 description 1
- 210000003527 eukaryotic cell Anatomy 0.000 description 1
- 239000000284 extract Substances 0.000 description 1
- 230000002496 gastric effect Effects 0.000 description 1
- 239000008103 glucose Substances 0.000 description 1
- ZJYYHGLJYGJLLN-UHFFFAOYSA-N guanidinium thiocyanate Chemical compound SC#N.NC(N)=N ZJYYHGLJYGJLLN-UHFFFAOYSA-N 0.000 description 1
- 238000009396 hybridization Methods 0.000 description 1
- 210000000987 immune system Anatomy 0.000 description 1
- 230000003053 immunization Effects 0.000 description 1
- 238000002649 immunization Methods 0.000 description 1
- 230000005847 immunogenicity Effects 0.000 description 1
- 230000016784 immunoglobulin production Effects 0.000 description 1
- 238000001727 in vivo Methods 0.000 description 1
- 230000001939 inductive effect Effects 0.000 description 1
- 208000015181 infectious disease Diseases 0.000 description 1
- 238000003780 insertion Methods 0.000 description 1
- 230000037431 insertion Effects 0.000 description 1
- 230000010354 integration Effects 0.000 description 1
- 230000003993 interaction Effects 0.000 description 1
- 238000002955 isolation Methods 0.000 description 1
- 206010024378 leukocytosis Diseases 0.000 description 1
- 229960000274 lysozyme Drugs 0.000 description 1
- 235000010335 lysozyme Nutrition 0.000 description 1
- 239000004325 lysozyme Substances 0.000 description 1
- 108010089256 lysyl-aspartyl-glutamyl-leucine Proteins 0.000 description 1
- 238000010841 mRNA extraction Methods 0.000 description 1
- 239000003120 macrolide antibiotic agent Substances 0.000 description 1
- 229940041033 macrolides Drugs 0.000 description 1
- 230000014759 maintenance of location Effects 0.000 description 1
- 235000012054 meals Nutrition 0.000 description 1
- 230000001404 mediated effect Effects 0.000 description 1
- 239000002184 metal Substances 0.000 description 1
- 244000005700 microbiome Species 0.000 description 1
- 230000002969 morbid Effects 0.000 description 1
- 229940126619 mouse monoclonal antibody Drugs 0.000 description 1
- 229950006780 n-acetylglucosamine Drugs 0.000 description 1
- 238000006386 neutralization reaction Methods 0.000 description 1
- 210000000056 organ Anatomy 0.000 description 1
- 210000001672 ovary Anatomy 0.000 description 1
- 239000002245 particle Substances 0.000 description 1
- 210000002826 placenta Anatomy 0.000 description 1
- 239000013612 plasmid Substances 0.000 description 1
- 238000003752 polymerase chain reaction Methods 0.000 description 1
- 229920002223 polystyrene Polymers 0.000 description 1
- 235000012015 potatoes Nutrition 0.000 description 1
- 238000001556 precipitation Methods 0.000 description 1
- 230000002028 premature Effects 0.000 description 1
- 238000002360 preparation method Methods 0.000 description 1
- 230000009257 reactivity Effects 0.000 description 1
- 230000010076 replication Effects 0.000 description 1
- 238000011160 research Methods 0.000 description 1
- 230000000717 retained effect Effects 0.000 description 1
- 210000003660 reticulum Anatomy 0.000 description 1
- 239000003161 ribonuclease inhibitor Substances 0.000 description 1
- 230000028327 secretion Effects 0.000 description 1
- 238000012163 sequencing technique Methods 0.000 description 1
- 238000002741 site-directed mutagenesis Methods 0.000 description 1
- 210000002784 stomach Anatomy 0.000 description 1
- 238000010998 test method Methods 0.000 description 1
- 210000001519 tissue Anatomy 0.000 description 1
- 230000002588 toxic effect Effects 0.000 description 1
- 230000032258 transport Effects 0.000 description 1
- 239000001226 triphosphate Substances 0.000 description 1
- 235000011178 triphosphate Nutrition 0.000 description 1
- 229960003165 vancomycin Drugs 0.000 description 1
- MYPYJXKWCTUITO-LYRMYLQWSA-N vancomycin Chemical compound O([C@@H]1[C@@H](O)[C@H](O)[C@@H](CO)O[C@H]1OC1=C2C=C3C=C1OC1=CC=C(C=C1Cl)[C@@H](O)[C@H](C(N[C@@H](CC(N)=O)C(=O)N[C@H]3C(=O)N[C@H]1C(=O)N[C@H](C(N[C@@H](C3=CC(O)=CC(O)=C3C=3C(O)=CC=C1C=3)C(O)=O)=O)[C@H](O)C1=CC=C(C(=C1)Cl)O2)=O)NC(=O)[C@@H](CC(C)C)NC)[C@H]1C[C@](C)(N)[C@H](O)[C@H](C)O1 MYPYJXKWCTUITO-LYRMYLQWSA-N 0.000 description 1
- MYPYJXKWCTUITO-UHFFFAOYSA-N vancomycin Natural products O1C(C(=C2)Cl)=CC=C2C(O)C(C(NC(C2=CC(O)=CC(O)=C2C=2C(O)=CC=C3C=2)C(O)=O)=O)NC(=O)C3NC(=O)C2NC(=O)C(CC(N)=O)NC(=O)C(NC(=O)C(CC(C)C)NC)C(O)C(C=C3Cl)=CC=C3OC3=CC2=CC1=C3OC1OC(CO)C(O)C(O)C1OC1CC(C)(N)C(O)C(C)O1 MYPYJXKWCTUITO-UHFFFAOYSA-N 0.000 description 1
- 235000013311 vegetables Nutrition 0.000 description 1
- 239000000304 virulence factor Substances 0.000 description 1
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 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
- C07K14/195—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria
- C07K14/33—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria from Clostridium (G)
-
- 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
- A61P31/04—Antibacterial agents
-
- 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
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/12—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from bacteria
- C07K16/1267—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from bacteria from Gram-positive bacteria
- C07K16/1282—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from bacteria from Gram-positive bacteria from Clostridium (G)
-
- 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
- C07K2317/00—Immunoglobulins specific features
- C07K2317/10—Immunoglobulins specific features characterized by their source of isolation or production
- C07K2317/13—Immunoglobulins specific features characterized by their source of isolation or production isolated from plants
-
- 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
Landscapes
- Chemical & Material Sciences (AREA)
- Health & Medical Sciences (AREA)
- Organic Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Medicinal Chemistry (AREA)
- Life Sciences & Earth Sciences (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Molecular Biology (AREA)
- Genetics & Genomics (AREA)
- Biophysics (AREA)
- Biochemistry (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- General Chemical & Material Sciences (AREA)
- Public Health (AREA)
- Veterinary Medicine (AREA)
- Immunology (AREA)
- Animal Behavior & Ethology (AREA)
- Gastroenterology & Hepatology (AREA)
- Pharmacology & Pharmacy (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Oncology (AREA)
- Engineering & Computer Science (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Communicable Diseases (AREA)
- Peptides Or Proteins (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (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 |
|---|---|---|---|
| DE19739685A DE19739685A1 (de) | 1997-09-10 | 1997-09-10 | Monoklonale Antikörper zur Therapie und Prophylaxe von Erkrankungen durch Clostridium difficile |
| DE19739685 | 1997-09-10 |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| ES2210832T3 true ES2210832T3 (es) | 2004-07-01 |
Family
ID=7841840
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| ES98951374T Expired - Lifetime ES2210832T3 (es) | 1997-09-10 | 1998-09-10 | Secuencias de aminoacidos para uso terapeutico y profilactico contra enfermedades debidas a las toxinas de clostridium difficile. |
Country Status (11)
| Country | Link |
|---|---|
| US (2) | US6667035B1 (enExample) |
| EP (1) | EP0994904B1 (enExample) |
| JP (1) | JP4318398B2 (enExample) |
| CN (1) | CN1273588A (enExample) |
| AT (1) | ATE254139T1 (enExample) |
| AU (1) | AU9742698A (enExample) |
| BR (1) | BR9815367A (enExample) |
| CA (1) | CA2303202C (enExample) |
| DE (2) | DE19739685A1 (enExample) |
| ES (1) | ES2210832T3 (enExample) |
| WO (1) | WO1999012971A2 (enExample) |
Families Citing this family (27)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| DE19739685A1 (de) * | 1997-09-10 | 1999-03-11 | Eichel Streiber Christoph Von | Monoklonale Antikörper zur Therapie und Prophylaxe von Erkrankungen durch Clostridium difficile |
| EP1358331A2 (en) * | 2001-02-09 | 2003-11-05 | The Provost, Fellows And Scholars Of The College Of The Holy And Undivided Trinity Of Queen Elizabeth Near Dublin | Clostridium difficile vaccine |
| GB0130267D0 (en) * | 2001-12-19 | 2002-02-06 | Neutec Pharma Plc | Focussed antibody technology |
| GB0205206D0 (en) * | 2002-03-06 | 2002-04-17 | Oxoid Ltd | Synthetic peptides |
| GB0309126D0 (en) * | 2003-04-17 | 2003-05-28 | Neutec Pharma Plc | Clostridium difficile focussed antibodies |
| JP4588763B2 (ja) * | 2004-02-06 | 2010-12-01 | ユニバーシティー オブ マサチューセッツ | クロストリジウム・ディフィシル（Ｃｌｏｓｔｒｉｄｉｕｍｄｉｆｆｉｃｉｌｅ）毒素に対する抗体およびその使用 |
| EP1609491B1 (en) * | 2004-06-16 | 2008-02-06 | Straumann Holding AG | Barrier membrane |
| GB0414886D0 (en) | 2004-07-02 | 2004-08-04 | Neutec Pharma Plc | Treatment of bacterial infections |
| AU2005321974B2 (en) * | 2004-12-27 | 2011-11-17 | Progenics Pharmaceuticals (Nevada), Inc. | Orally deliverable and anti-toxin antibodies and methods for making and using them |
| AU2012241141B2 (en) * | 2005-08-11 | 2015-08-20 | Arpi Matossian-Rogers | TCR-V-beta related peptides for treatment and diagnosis of autoimmune disease |
| CN105017423B (zh) * | 2005-08-11 | 2019-06-04 | 阿皮·马托西安-罗杰斯 | 用于自身免疫性疾病治疗和诊断的TCR-V-β相关肽 |
| US8598321B2 (en) | 2007-03-22 | 2013-12-03 | The Regents Of The University Of California | Therapeutic monoclonal antibodies that neutralize botulinum neurotoxins |
| WO2009136297A2 (en) * | 2008-05-09 | 2009-11-12 | Recopharma Ab | Compositions and methods for inhibiting toxin a from clostridium difficile |
| DE102008029688B4 (de) * | 2008-06-24 | 2016-06-23 | Biodics Gmbh | Verfahren zum Nachweis und zur Identifikation eines varianten C. difficile Stammes in einer Probe |
| WO2010014854A2 (en) * | 2008-07-31 | 2010-02-04 | The Regents Of The University Of California | Antibodies that neutralize botulinum neurotoxins |
| ES2589606T3 (es) * | 2009-07-27 | 2016-11-15 | Biodics Gmbh | Procedimiento para la detección y para la identificación de una cepa de C. difficile variante en una muestra |
| US8889363B2 (en) | 2009-07-27 | 2014-11-18 | Biodics | Method for the detection and identification of a variant C. difficile strain in a sample |
| US20120269814A1 (en) * | 2009-11-10 | 2012-10-25 | Amgen Inc. | Anti-c mpl antibodies |
| US9243057B2 (en) | 2010-08-31 | 2016-01-26 | The Regents Of The University Of California | Antibodies for botulinum neurotoxins |
| WO2012118693A1 (en) * | 2011-02-28 | 2012-09-07 | Northshore University Healthsystem | Methods of diagnosing clostridium difficile infection |
| HUE047085T2 (hu) | 2011-04-22 | 2020-04-28 | Wyeth Llc | Clostridium difficile mutáns toxinjához kapcsolódó készítmények és eljárásai |
| SG11201400916XA (en) | 2011-08-22 | 2014-06-27 | Cangene Corp | Clostridium difficile antibodies |
| WO2013071409A1 (en) | 2011-11-18 | 2013-05-23 | National Research Council Of Canada (Nrc) | Clostridium difficile lipoteichoic acid and uses thereof |
| WO2013130981A1 (en) * | 2012-03-02 | 2013-09-06 | Regeneron Pharmaceuticals, Inc. | Human antibodies to clostridium difficile toxins |
| BR122016023101B1 (pt) | 2012-10-21 | 2022-03-22 | Pfizer Inc | Polipeptídeo, composição imunogênica que o compreende, bem como célula recombinante derivada de clostridium difficile |
| US10117933B2 (en) * | 2012-11-28 | 2018-11-06 | Emergent Biosolutions Canada Inc. | Antibodies against Clostridium difficile |
| WO2014144292A2 (en) | 2013-03-15 | 2014-09-18 | Sanofi Pasteur Biologics , Llc | Antibodies against clostridium difficile toxins and methods of using the same |
Family Cites Families (16)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4879218A (en) | 1982-09-13 | 1989-11-07 | Virginia Tech Intellectual Properties, Inc. | Antibody for C.difficile |
| DE3471661D1 (en) | 1984-03-02 | 1988-07-07 | Tracy Dale Wilkins | Toxins and antibodies of c. difficile |
| JPS6147500A (ja) | 1984-08-15 | 1986-03-07 | Res Dev Corp Of Japan | キメラモノクロ−ナル抗体及びその製造法 |
| EP0173494A3 (en) | 1984-08-27 | 1987-11-25 | The Board Of Trustees Of The Leland Stanford Junior University | Chimeric receptors by dna splicing and expression |
| JPS61134325A (ja) | 1984-12-04 | 1986-06-21 | Teijin Ltd | ハイブリツド抗体遺伝子の発現方法 |
| US4863852A (en) | 1985-07-03 | 1989-09-05 | Virginia Tech Intellectual Properties, Inc. | Method of detecting, isolating and purifying clostridium difficile toxin A and its receptors |
| US5071759A (en) | 1986-05-30 | 1991-12-10 | The United States Of America As Represented By The Secretary Of The Army | Hybridoma cell lines and monoclonal antibodies to clostridum difficile toxins A and B |
| US5580774A (en) * | 1989-07-31 | 1996-12-03 | Eli Lilly And Company | Chimeric antibodies directed against a human glycoprotein antigen |
| WO1991010737A1 (en) | 1990-01-11 | 1991-07-25 | Molecular Affinities Corporation | Production of antibodies using gene libraries |
| US5098826A (en) | 1990-03-09 | 1992-03-24 | Virginia Tech Intellectual Properties, Inc. | Detection, isolation and purification of Clostridium difficile toxin A with toxin receptors |
| US5231003A (en) | 1990-05-11 | 1993-07-27 | Cambridge Bioscience Corporation | Monoclonal antibodies specific for toxin b of clostridium difficile |
| US5858725A (en) | 1990-10-10 | 1999-01-12 | Glaxo Wellcome Inc. | Preparation of chimaeric antibodies using the recombinant PCR strategy |
| GB9109645D0 (en) * | 1991-05-03 | 1991-06-26 | Celltech Ltd | Recombinant antibodies |
| GB9317423D0 (en) * | 1993-08-21 | 1993-10-06 | Imp Cancer Res Tech | Monoclonal antibodies |
| CZ296806B6 (cs) | 1994-10-24 | 2006-06-14 | Allergan, Inc. | Rozpustný fúzní protein a zpusob výroby rozpustného rekombinantního botulinového toxinu |
| DE19739685A1 (de) * | 1997-09-10 | 1999-03-11 | Eichel Streiber Christoph Von | Monoklonale Antikörper zur Therapie und Prophylaxe von Erkrankungen durch Clostridium difficile |
-
1997
- 1997-09-10 DE DE19739685A patent/DE19739685A1/de not_active Ceased
-
1998
- 1998-09-10 DE DE59810172T patent/DE59810172D1/de not_active Expired - Lifetime
- 1998-09-10 EP EP98951374A patent/EP0994904B1/de not_active Expired - Lifetime
- 1998-09-10 AT AT98951374T patent/ATE254139T1/de active
- 1998-09-10 CN CN98808996A patent/CN1273588A/zh active Pending
- 1998-09-10 WO PCT/EP1998/005759 patent/WO1999012971A2/de not_active Ceased
- 1998-09-10 US US09/508,413 patent/US6667035B1/en not_active Expired - Fee Related
- 1998-09-10 BR BR9815367-6A patent/BR9815367A/pt not_active Application Discontinuation
- 1998-09-10 ES ES98951374T patent/ES2210832T3/es not_active Expired - Lifetime
- 1998-09-10 AU AU97426/98A patent/AU9742698A/en not_active Abandoned
- 1998-09-10 CA CA2303202A patent/CA2303202C/en not_active Expired - Fee Related
- 1998-09-10 JP JP2000510776A patent/JP4318398B2/ja not_active Expired - Fee Related
-
2003
- 2003-12-23 US US10/745,102 patent/US7151159B2/en not_active Expired - Fee Related
Also Published As
| Publication number | Publication date |
|---|---|
| AU9742698A (en) | 1999-03-29 |
| JP2001515920A (ja) | 2001-09-25 |
| DE59810172D1 (de) | 2003-12-18 |
| CA2303202C (en) | 2010-04-27 |
| WO1999012971A2 (de) | 1999-03-18 |
| US20040137601A1 (en) | 2004-07-15 |
| DE19739685A1 (de) | 1999-03-11 |
| CN1273588A (zh) | 2000-11-15 |
| EP0994904B1 (de) | 2003-11-12 |
| WO1999012971A3 (de) | 1999-07-22 |
| ATE254139T1 (de) | 2003-11-15 |
| CA2303202A1 (en) | 1999-03-18 |
| JP4318398B2 (ja) | 2009-08-19 |
| BR9815367A (pt) | 2001-11-06 |
| US7151159B2 (en) | 2006-12-19 |
| EP0994904A2 (de) | 2000-04-26 |
| US6667035B1 (en) | 2003-12-23 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| ES2210832T3 (es) | Secuencias de aminoacidos para uso terapeutico y profilactico contra enfermedades debidas a las toxinas de clostridium difficile. | |
| RU2757813C2 (ru) | Антитело против lag-3, его антигенсвязывающий фрагмент и их фармацевтическое применение | |
| FI115462B (fi) | Menetelmä immunoglobuliinin valmistamiseksi | |
| AU2018243123B2 (en) | B7-H3 antibody, antigen-binding fragment thereof and medical use thereof | |
| EP3689909A1 (en) | Tigit antibody, antigen-binding fragment thereof, and medical use thereof | |
| ES2052027T5 (es) | Clonacion de secuencias de dominio variable de inmunoglobulina. | |
| EP0937140B1 (en) | Antibody molecules which interact specifically with the active site or cleft of a target molecule | |
| JP4954104B2 (ja) | Ｉｌ−５介在障害を治療および診断するための改良方法 | |
| HK1247214B (zh) | 一种pdl-1抗体、其药物组合物及其用途 | |
| JP2012515746A (ja) | 抗ｃｄ１６０モノクローナル抗体及びその使用 | |
| WO2019091449A1 (zh) | Cd96抗体、其抗原结合片段及医药用途 | |
| TW526206B (en) | Reshaped human antibody to human medulloblastoma cells | |
| CN102906111A (zh) | 特异性结合乙型肝炎病毒表面抗原的人抗体 | |
| CN112513088B (zh) | 抗ox40抗体、其抗原结合片段及其医药用途 | |
| CN101580546B (zh) | 人源抗人干扰素α抗体及其应用 | |
| KR101613347B1 (ko) | 비브리오 패혈증균 알티엑스에이-1 단백질에 특이적으로 결합하는 단일클론항체 및 이의 용도 | |
| EP1079856B1 (en) | Humanized antibodies that recognize verotoxin ii and cell line producing same | |
| CN100441689C (zh) | 抗ehec o157志贺样毒素ⅱa亚单位单克隆抗体5f3轻、重链可变区基因及应用 | |
| KR100506118B1 (ko) | 수막염균증 백신 조성물 | |
| KR100509993B1 (ko) | Il-5 매개된 질환의 치료에 유용한 재조합 il-5 길항제 | |
| MXPA00002491A (en) | Amino acid sequences for therapeutical and prophylactic applications to diseases due to clostridium difficile | |
| KR20040084875A (ko) | Ｂ형 간염 바이러스의 표면 항원에 대한 인간항체의가변영역을 삽입할 수 있는 항체발현 플라스미드 | |
| WO2022063100A1 (zh) | 抗tigit抗体及双抗体和它们的应用 | |
| KR101553845B1 (ko) | 비브리오 패혈증균 알티엑스에이-1 단백질에 특이적으로 결합하는 단일클론항체 및 이의 용도 | |
| MX2008005405A (es) | Anticuerpos quimericos equinos: humanos. |