HU228706B1 - Streptococcus antigens - Google Patents
Streptococcus antigens Download PDFInfo
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- HU228706B1 HU228706B1 HU0301656A HUP0301656A HU228706B1 HU 228706 B1 HU228706 B1 HU 228706B1 HU 0301656 A HU0301656 A HU 0301656A HU P0301656 A HUP0301656 A HU P0301656A HU 228706 B1 HU228706 B1 HU 228706B1
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| AU2002351623A1 (en) * | 2001-12-20 | 2003-07-09 | Shire Biochem Inc. | Streptococcus antigens |
| TWI457133B (zh) | 2005-12-13 | 2014-10-21 | Glaxosmithkline Biolog Sa | 新穎組合物 |
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| PT2097102E (pt) | 2006-09-07 | 2012-08-03 | Glaxosmithkline Biolog Sa | Vacina de combinação tendo quantidades reduzidas de antigénio de poliovírus |
| MX2009011837A (es) | 2007-05-02 | 2010-04-22 | Glaxosmithkline Biolog Sa | Vacuna. |
| EA201391788A1 (ru) | 2007-06-26 | 2014-08-29 | Глаксосмитклайн Байолоджикалс С.А. | Вакцина, содержащая конъюгаты капсульных полисахаридов streptococcus pneumoniae |
| CA2694466A1 (en) * | 2007-07-23 | 2009-01-29 | Sanofi Pasteur Limited | Immunogenic polypeptides and monoclonal antibodies |
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| CN102223876A (zh) | 2008-09-26 | 2011-10-19 | 纳米生物公司 | 纳米乳剂治疗性组合物及其使用方法 |
| KR101450958B1 (ko) | 2009-04-30 | 2014-10-15 | 콜레이 파마시티컬 그룹, 인코포레이티드 | 폐렴구균 백신 및 그의 용도 |
| US8668911B2 (en) | 2009-05-14 | 2014-03-11 | The Regents Of The University Of Michigan | Streptococcus vaccine compositions and methods of using the same |
| US20120135037A1 (en) | 2009-06-01 | 2012-05-31 | Mizel Steven B | Flagellin fusion proteins and conjugates comprising pneumococcus antigens and methods of using the same |
| PT2473605T (pt) | 2009-09-03 | 2018-05-28 | Pfizer Vaccines Llc | Vacina pcsk9 |
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| KR101272351B1 (ko) | 2010-04-23 | 2013-06-07 | 이화여자대학교 산학협력단 | 새로운 카나마이신 화합물, 카나마이신 생산 스트렙토마이세스 속 미생물 및 카나마이신의 생산 방법 |
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| CA2834834A1 (en) | 2011-05-17 | 2012-11-22 | Glaxosmithkline Biologicals S.A. | Vaccine against streptococcus pneumoniae |
| US11708411B2 (en) | 2013-12-20 | 2023-07-25 | Wake Forest University Health Sciences | Methods and compositions for increasing protective antibody levels induced by pneumococcal polysaccharide vaccines |
| HRP20211288T1 (hr) | 2014-01-21 | 2021-11-26 | Pfizer Inc. | Kapsularni polisaharidi bakterije streptococcus pneumoniae i njihovi konjugati |
| US11160855B2 (en) | 2014-01-21 | 2021-11-02 | Pfizer Inc. | Immunogenic compositions comprising conjugated capsular saccharide antigens and uses thereof |
| DK3096783T3 (da) | 2014-01-21 | 2021-08-02 | Pfizer | Streptococcus pneumoniae-kapselpolysaccharider og konjugater deraf |
| PE20161095A1 (es) | 2014-01-21 | 2016-10-26 | Pfizer | Composiciones inmunogenicas que comprenden antigenos de sacaridos capsulares conjugados y uso de los mismos |
| WO2015121783A1 (en) | 2014-02-14 | 2015-08-20 | Pfizer Inc. | Immunogenic glycoprotein conjugates |
| HRP20230416T1 (hr) | 2015-01-15 | 2023-07-07 | Pfizer Inc. | Imunogeni pripravci, namijenjeni upotrebi u cjepivima protiv pneumokoka |
| KR20250058066A (ko) | 2015-07-21 | 2025-04-29 | 화이자 인코포레이티드 | 접합된 캡슐형 사카라이드 항원을 포함하는 면역원성 조성물, 그를 포함하는 키트 및 그의 용도 |
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| US20200222550A1 (en) | 2017-01-31 | 2020-07-16 | Merck Sharp & Dohme Corp. | Methods for production of capsular polysaccharide protein conjugates from streptococcus pneumoniae serotype 19f |
| EP3576784B1 (en) | 2017-01-31 | 2025-09-24 | Merck Sharp & Dohme LLC | Methods for making polysaccharide-protein conjugates |
| EP4656650A2 (en) | 2017-02-24 | 2025-12-03 | Merck Sharp & Dohme LLC | Pneumococcal conjugate vaccine formulations |
| JP7438102B2 (ja) | 2017-09-07 | 2024-02-26 | メルク・シャープ・アンド・ドーム・エルエルシー | 肺炎球菌多糖体および免疫原性多糖体－キャリアタンパク質コンジュゲートでのその使用 |
| MX2020005779A (es) | 2017-12-06 | 2020-10-28 | Merck Sharp & Dohme | Composiciones que comprenden conjugados de polisacarido de streptococcus pneumoniae con proteina y metodos de uso de estos. |
| US11260119B2 (en) | 2018-08-24 | 2022-03-01 | Pfizer Inc. | Escherichia coli compositions and methods thereof |
| WO2020121159A1 (en) | 2018-12-12 | 2020-06-18 | Pfizer Inc. | Immunogenic multiple hetero-antigen polysaccharide-protein conjugates and uses thereof |
| AU2019401535B2 (en) | 2018-12-19 | 2023-12-14 | Merck Sharp & Dohme Llc | Compositions comprising Streptococcus pneumoniae polysaccharide-protein conjugates and methods of use thereof |
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| CA3136278A1 (en) | 2019-04-10 | 2020-10-15 | Pfizer Inc. | Immunogenic compositions comprising conjugated capsular saccharide antigens, kits comprising the same and uses thereof |
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| CN115362177A (zh) | 2020-02-21 | 2022-11-18 | 辉瑞公司 | 糖类的纯化 |
| EP4107170A2 (en) | 2020-02-23 | 2022-12-28 | Pfizer Inc. | Escherichia coli compositions and methods thereof |
| JP2023546446A (ja) | 2020-10-22 | 2023-11-02 | ファイザー・インク | 細菌多糖を精製する方法 |
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| MX2023005221A (es) | 2020-11-04 | 2023-05-16 | Pfizer | Composiciones inmunogenicas para uso en vacunas neumococicas. |
| US12357681B2 (en) | 2020-12-23 | 2025-07-15 | Pfizer Inc. | E. coli FimH mutants and uses thereof |
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| CN118510548A (zh) | 2022-01-13 | 2024-08-16 | 辉瑞公司 | 包含缀合的荚膜糖抗原的免疫原性组合物及其用途 |
| WO2023161817A1 (en) | 2022-02-25 | 2023-08-31 | Pfizer Inc. | Methods for incorporating azido groups in bacterial capsular polysaccharides |
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| AU2023385908A1 (en) | 2022-11-22 | 2025-05-15 | Pfizer Inc. | Immunogenic compositions comprising conjugated capsular saccharide antigens and uses thereof |
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| WO2025057078A1 (en) | 2023-09-14 | 2025-03-20 | Pfizer Inc. | Adjuvanted immunogenic compositions comprising conjugated pneumococcal capsular saccharide antigens and uses thereof |
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| WO2025133971A1 (en) | 2023-12-23 | 2025-06-26 | Pfizer Inc. | Improved methods for producing bacterial capsular saccharide glycoconjugates |
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| WO2025191415A1 (en) | 2024-03-11 | 2025-09-18 | Pfizer Inc. | Immunogenic compositions comprising conjugated escherichia coli saccharides and uses thereof |
| WO2025219908A2 (en) | 2024-04-19 | 2025-10-23 | Pfizer Inc. | Media and fermentation methods for polysaccharide production in bacterial cell culture |
| WO2025219904A1 (en) | 2024-04-19 | 2025-10-23 | Pfizer Inc. | Improved methods for producing glycoconjugates by reductive amination in aprotic solvent |
Family Cites Families (12)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4425437A (en) | 1979-11-05 | 1984-01-10 | Genentech, Inc. | Microbial polypeptide expression vehicle |
| US4431739A (en) | 1979-11-05 | 1984-02-14 | Genentech, Inc. | Transformant bacterial culture capable of expressing heterologous protein |
| US4338397A (en) | 1980-04-11 | 1982-07-06 | President And Fellows Of Harvard College | Mature protein synthesis |
| US5866135A (en) * | 1994-04-21 | 1999-02-02 | North American Vaccine, Inc. | Group A streptococcal polysaccharide immunogenic compositions and methods |
| EP0831894A1 (en) * | 1995-06-07 | 1998-04-01 | Alberta Research Council | Immunogenic and immunostimulatory oligosaccharide compositions and methods of making and using them |
| DE69739981D1 (de) * | 1996-10-31 | 2010-10-14 | Human Genome Sciences Inc | Streptococcus pneumoniae-Antigene und Impfstoffe |
| CN1291233A (zh) * | 1997-09-24 | 2001-04-11 | 美国明尼苏达州大学 | 来自肺炎链球菌之人类补体c3降解蛋白酶 |
| WO2000006737A2 (en) * | 1998-07-27 | 2000-02-10 | Microbial Technics Limited | Streptococcus pneumoniae proteins and nucleic acid molecules |
| WO2000010599A2 (en) * | 1998-08-19 | 2000-03-02 | North American Vaccine, Inc. | IMMUNOGENIC β-PROPIONAMIDO-LINKED POLYSACCHARIDE PROTEIN CONJUGATE USEFUL AS A VACCINE PRODUCED USING AN N-ACRYLOYLATED POLYSACCHARIDE |
| JP2002526082A (ja) * | 1998-09-24 | 2002-08-20 | リージェンツ オブ ザ ユニバーシティ オブ ミネソタ | ストレプトコッカス・ニューモニア由来のヒト補体ｃ３分解ポリペプチド |
| DE69940439D1 (de) * | 1998-12-21 | 2009-04-02 | Medimmune Inc | Streptococcus pneumoniae proteine und immunogene fragmente für impstoffe |
| NZ512574A (en) * | 1998-12-23 | 2004-03-26 | Iaf Biochem Int | Novel streptococcus antigens useful as vaccines |
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