JP4637350B2 - グループｂ連鎖球菌抗原 - Google Patents
グループｂ連鎖球菌抗原 Download PDFInfo
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- JP4637350B2 JP4637350B2 JP2000532528A JP2000532528A JP4637350B2 JP 4637350 B2 JP4637350 B2 JP 4637350B2 JP 2000532528 A JP2000532528 A JP 2000532528A JP 2000532528 A JP2000532528 A JP 2000532528A JP 4637350 B2 JP4637350 B2 JP 4637350B2
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- C07K14/195—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria
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| US7098182B2 (en) | 1998-07-27 | 2006-08-29 | Microbial Technics Limited | Nucleic acids and proteins from group B streptococcus |
| WO2000006736A2 (en) * | 1998-07-27 | 2000-02-10 | Microbial Technics Limited | Nucleic acids and proteins from group b streptococcus |
| GB0105922D0 (en) * | 2001-03-09 | 2001-04-25 | Microscience Ltd | Genes and proteins, and their use |
| US6890539B2 (en) | 1998-12-22 | 2005-05-10 | Microscience, Ltd. | Genes and proteins, and their use |
| CN101066447A (zh) | 1998-12-22 | 2007-11-07 | 微科学有限公司 | 基因和蛋白质,及它们的用途 |
| US7128918B1 (en) | 1998-12-23 | 2006-10-31 | Id Biomedical Corporation | Streptococcus antigens |
| US6833356B1 (en) | 1999-08-25 | 2004-12-21 | Medimmune, Inc. | Pneumococcal protein homologs and fragments for vaccines |
| AU7076100A (en) * | 1999-08-25 | 2001-03-19 | Med Immune, Inc. | Homologs of a pneumococcal protein and fragments for vaccines |
| US6866855B2 (en) | 2000-06-12 | 2005-03-15 | University Of Saskatchewan | Immunization of dairy cattle with GapC protein against Streptococcus infection |
| US6833134B2 (en) | 2000-06-12 | 2004-12-21 | University Of Saskacthewan | Immunization of dairy cattle with GapC protein against Streptococcus infection |
| DK1294771T3 (da) | 2000-06-12 | 2008-12-15 | Univ Saskatchewan | Kimært GapC-protein fra Streptococcus og anvendelse deraf til vaccinering og diagnosticering |
| EP1734050A3 (en) * | 2000-06-12 | 2012-12-05 | University Of Saskatchewan | Immunization of dairy cattle with GapC protein against streptococcus infection |
| ES2273861T3 (es) * | 2000-06-12 | 2007-05-16 | University Of Saskatchewan | Inmunizacion de ganado vacuno lechero con proteina gapc frente a infecciones por streptococcus. |
| JP4102186B2 (ja) | 2000-10-13 | 2008-06-18 | アイディー バイオメディカル コーポレイション | グループｂストレプトコッカスのｂｖｈ−ａ２及びｂｖｈ−ａ３抗原 |
| CA2881568C (en) | 2000-10-27 | 2019-09-24 | Novartis Vaccines And Diagnostics, Inc. | Nucleic acids and proteins from streptococcus groups a & b |
| AU2002216863B8 (en) * | 2000-12-21 | 2008-03-20 | Id Biomedical Corporation | Streptococcus pyogenes antigens and corresponding DNA fragments |
| FR2824074A1 (fr) * | 2001-04-26 | 2002-10-31 | Pasteur Institut | Sequence du genome streptococcus agalactiae, application au developpement de vaccins, d'outils de diagnostic, et a l'identification de cibles therapeutiques |
| ES2381967T3 (es) * | 2002-02-11 | 2012-06-04 | Id Biomedical Corporation | Antígeno de streptococcus del grupo B |
| GB0210128D0 (en) * | 2002-05-02 | 2002-06-12 | Chiron Spa | Nucleic acids and proteins from streptococcus groups A & B |
| ES2505695T3 (es) | 2003-07-31 | 2014-10-10 | Novartis Vaccines And Diagnostics, Inc. | Composiciones inmunógenas para Streptococcus pyogenes |
| US8945589B2 (en) | 2003-09-15 | 2015-02-03 | Novartis Vaccines And Diagnostics, Srl | Immunogenic compositions for Streptococcus agalactiae |
| JP2008508320A (ja) | 2004-07-29 | 2008-03-21 | カイロン コーポレイション | Ｓｔｒｅｐｔｏｃｏｃｃｕｓａｇａｌａｃｔｉａｅのようなグラム陽性細菌に対する免疫原性組成物 |
| US7838010B2 (en) | 2004-10-08 | 2010-11-23 | Novartis Vaccines And Diagnostics S.R.L. | Immunogenic and therapeutic compositions for Streptococcus pyogenes |
| EP1845944A4 (en) * | 2005-02-08 | 2011-07-27 | Id Biomedical Corp Of Quebec C O B As Glaxosmithkline Biolog North America | PHARMACEUTICAL COMPOSITIONS |
| GB0605247D0 (en) * | 2006-03-15 | 2006-04-26 | Chiron Srl | Compositions and methods for immunisation |
| KR101621837B1 (ko) | 2007-09-12 | 2016-05-17 | 노파르티스 아게 | Ｇａｓ57 돌연변이 항원 및 ｇａｓ57 항체 |
| EP2537857B1 (en) | 2007-12-21 | 2017-01-18 | GlaxoSmithKline Biologicals SA | Mutant forms of streptolysin O |
| CN102304185A (zh) * | 2011-09-02 | 2012-01-04 | 黑龙江八一农垦大学 | 预防奶牛乳房炎的融合蛋白sip-trap及制备方法和应用 |
| EP2949340A1 (en) * | 2014-05-30 | 2015-12-02 | IDT Biologika GmbH | Vaccine composition against Streptococcus suis infection |
| CN115057944B (zh) * | 2022-06-24 | 2025-06-24 | 南京农业大学 | 一种针对所有gbs血清型的多表位亚单位疫苗 |
Family Cites Families (19)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4431739A (en) | 1979-11-05 | 1984-02-14 | Genentech, Inc. | Transformant bacterial culture capable of expressing heterologous protein |
| US4425437A (en) | 1979-11-05 | 1984-01-10 | Genentech, Inc. | Microbial polypeptide expression vehicle |
| US5302386A (en) * | 1986-04-16 | 1994-04-12 | Brigham And Women's Hospital, Inc. | Bacterial antigens, antibodies, vaccines and methods of manufacture |
| US5472696A (en) * | 1988-02-26 | 1995-12-05 | Univ. Of Florida Research Foundation, Inc. | Antigen of group B streptococci |
| US5648241A (en) * | 1989-09-15 | 1997-07-15 | The General Hospital Corporation | Conjugate vaccine against group B streptococcus |
| US5679768A (en) * | 1991-02-15 | 1997-10-21 | Uab Research Foundation | Epitopic regions of pneumococcal surface protein A |
| US5225331A (en) * | 1991-04-25 | 1993-07-06 | National Research Council Of Canada | Immunoassay for detecting group b streptococcus |
| HU217582B (hu) * | 1993-03-19 | 2000-02-28 | Gunnar Lindahl | Streptococcus B csoportba tartozó törzsek elleni immunitást biztosító, Rib fehérjenevű felületi protein, eljárás a protein tisztítására, reagenskészlet és gyógyszerkészítmény |
| US5595740A (en) * | 1994-05-16 | 1997-01-21 | University Of Florida | Cloning of non-IgA FC binding forms of the group B streptococcal beta antigens |
| TW448184B (en) * | 1994-11-01 | 2001-08-01 | Kirin Brewery | Peptide sequence that forms muscous glycoprotein chain and technique for producing thereof |
| JP4469026B2 (ja) * | 1996-10-31 | 2010-05-26 | ヒューマン ジノーム サイエンシーズ，インコーポレイテッド | Ｓｔｒｅｐｔｏｃｏｃｃｕｓ ｐｎｅｕｍｏｎｉａｅの抗原およびワクチン |
| CA2321106C (en) * | 1998-02-20 | 2013-07-23 | Biochem Pharma Inc. | Group b streptococcus antigens |
| US6248329B1 (en) * | 1998-06-01 | 2001-06-19 | Ramaswamy Chandrashekar | Parasitic helminth cuticlin nucleic acid molecules and uses thereof |
| WO2000006736A2 (en) | 1998-07-27 | 2000-02-10 | Microbial Technics Limited | Nucleic acids and proteins from group b streptococcus |
| EP1140157B1 (en) | 1998-12-21 | 2009-02-18 | MedImmune, Inc. | Streptococcus pneumoniae proteins and immunogenic fragments for vaccines |
| KR100802198B1 (ko) | 1998-12-23 | 2008-02-11 | 샤이어 바이오켐 인코포레이티드 | 신규한 스트렙토코커스 항원 |
| US7128918B1 (en) | 1998-12-23 | 2006-10-31 | Id Biomedical Corporation | Streptococcus antigens |
| GB9921125D0 (en) | 1999-09-07 | 1999-11-10 | Microbial Technics Limited | Proteins |
| ES2381967T3 (es) * | 2002-02-11 | 2012-06-04 | Id Biomedical Corporation | Antígeno de streptococcus del grupo B |
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Cited By (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2009242403A (ja) * | 1998-02-20 | 2009-10-22 | Id Biomedical Corp | グループｂ連鎖球菌抗原 |
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