RU2518315C2 - Иммуногенные белки streptococcus - Google Patents
Иммуногенные белки streptococcus Download PDFInfo
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- RU2518315C2 RU2518315C2 RU2010107878/15A RU2010107878A RU2518315C2 RU 2518315 C2 RU2518315 C2 RU 2518315C2 RU 2010107878/15 A RU2010107878/15 A RU 2010107878/15A RU 2010107878 A RU2010107878 A RU 2010107878A RU 2518315 C2 RU2518315 C2 RU 2518315C2
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- G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
- G01N33/53—Immunoassay; Biospecific binding assay; Materials therefor
- G01N33/569—Immunoassay; Biospecific binding assay; Materials therefor for microorganisms, e.g. protozoa, bacteria, viruses
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| WO2000005378A2 (en) | 1998-07-22 | 2000-02-03 | Id-Lelystad Instituut Voor Dierhouderij En Diergezondheid B.V. | Streptococcus suis vaccines and diagnostic tests |
| WO2002061070A2 (en) | 2001-02-02 | 2002-08-08 | Id-Lelystad, Instituut Voor Dierhouderij En Diergezondheid B.V. | Environmentally regulated genes, involved in the virulence of streptococcus suis |
| GB0818231D0 (en) * | 2008-10-06 | 2008-11-12 | Univ Nottingham | Composition |
| KR20200039025A (ko) * | 2013-09-19 | 2020-04-14 | 조에티스 서비시즈 엘엘씨 | 유성 아쥬반트 |
| JP2018504381A (ja) * | 2014-12-22 | 2018-02-15 | エフ．ホフマン−ラ ロシュ アーゲーＦ． Ｈｏｆｆｍａｎｎ−Ｌａ Ｒｏｃｈｅ Ａｋｔｉｅｎｇｅｓｅｌｌｓｃｈａｆｔ | 細胞透過性ペプチド |
| CA3001433A1 (en) | 2015-10-21 | 2017-04-27 | Minervax Aps | Immunogenic fusion protein |
| US10738338B2 (en) | 2016-10-18 | 2020-08-11 | The Research Foundation for the State University | Method and composition for biocatalytic protein-oligonucleotide conjugation and protein-oligonucleotide conjugate |
| RU2685957C2 (ru) * | 2016-12-28 | 2019-04-23 | Федеральное государственное бюджетное научное учреждение "Институт экспериментальной медицины" (ФГБНУ "ИЭМ") | Химерный рекомбинантный белок, обладающий протективными свойствами в отношении Streptococcus pyogenes |
| JP2024500837A (ja) * | 2020-12-23 | 2024-01-10 | チャン ザッカーバーグ バイオハブ， インコーポレイテッド | 抗原特異的ｔ細胞を惹起するように操作された細菌 |
| CN112773891B (zh) * | 2021-02-01 | 2022-03-25 | 北部湾大学 | 卵形鲳鲹源无乳链球菌dna疫苗及其制备方法和应用 |
| CN119219752B (zh) * | 2024-09-12 | 2026-04-03 | 华中农业大学 | 一种猪链球菌抗原蛋白及其筛选方法及其应用 |
| CN119780429B (zh) * | 2024-12-27 | 2025-12-26 | 华派生物技术(集团)股份有限公司 | 一种提高猪圆环病毒2型Cap蛋白抗原琼扩检测灵敏度的方法 |
Citations (1)
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| US5283507A (en) | 1990-12-20 | 1994-02-01 | General Electric Company | Regenerative braking protection for an electrically-propelled traction vehicle |
| NL9100510A (nl) * | 1991-03-21 | 1992-10-16 | Centraal Diergeneeskundig Inst | Dna-sequenties die coderen voor kenmerken van virulentie van streptococcus suis en delen daarvan, daarvan afgeleide polypeptiden en antilichamen, alsmede toepassing daarvan bij de diagnose van en de bescherming tegen infectie met s. suis bij zoogdieren, waaronder de mens. |
| IT1251435B (it) | 1991-09-04 | 1995-05-09 | Sclavo Spa | Vettore genetico per la integrazione multipla stabile di sequenze di dna nel genoma dei lieviti kluyveromyces lactis e saccharomyces cerevisiae e plasmidi che lo contengono. |
| US5928900A (en) * | 1993-09-01 | 1999-07-27 | The Rockefeller University | Bacterial exported proteins and acellular vaccines based thereon |
| AU2638595A (en) * | 1994-05-16 | 1995-12-05 | Uab Research Foundation, The | (streptococcus pneumoniae) capsular polysaccharide genes and flanking regions |
| US5681570A (en) * | 1995-01-12 | 1997-10-28 | Connaught Laboratories Limited | Immunogenic conjugate molecules |
| EP0750042A1 (fr) * | 1995-06-20 | 1996-12-27 | Societe Des Produits Nestle S.A. | Bactéries lactiques produisant des exopolysaccharides |
| DE69723434T2 (de) | 1996-04-26 | 2004-05-19 | Rijksuniversiteit Te Leiden | Verfahren zur selektion und produktion von t-zell-peptide epitope und vakzine mit diese epitope |
| US6800744B1 (en) * | 1997-07-02 | 2004-10-05 | Genome Therapeutics Corporation | Nucleic acid and amino acid sequences relating to Streptococcus pneumoniae for diagnostics and therapeutics |
| WO2000005378A2 (en) * | 1998-07-22 | 2000-02-03 | Id-Lelystad Instituut Voor Dierhouderij En Diergezondheid B.V. | Streptococcus suis vaccines and diagnostic tests |
| CA2355364C (en) * | 1998-12-21 | 2014-03-18 | Medimmune, Inc. | Streptococcus pneumoniae proteins and immunogenic fragments for vaccines |
| JP5249482B2 (ja) * | 1999-06-16 | 2013-07-31 | ボストン・バイオメデイカル・リサーチ・インステイテユート | インビボのβ−アミロイドレベルの免疫学的制御 |
| ES2316450T3 (es) * | 2000-06-12 | 2009-04-16 | University Of Saskatchewan | Proteina gapc quimerica de streptococcus y su uso en vacunacion y diagnostico. |
| EP1205552A1 (en) * | 2000-11-09 | 2002-05-15 | ID-Lelystad, Instituut voor Dierhouderij en Diergezondheid B.V. | Virulence of streptococci, involving ORFs from Streptococcus suis |
| WO2002061070A2 (en) * | 2001-02-02 | 2002-08-08 | Id-Lelystad, Instituut Voor Dierhouderij En Diergezondheid B.V. | Environmentally regulated genes, involved in the virulence of streptococcus suis |
| EP1590368B1 (en) * | 2003-01-27 | 2014-02-26 | Københavns Universitet | Compounds useful in the diagnosis and treatment of pregnancy-associated malaria |
| EP1629005A2 (en) * | 2003-05-30 | 2006-03-01 | Intercell AG | Enterococcus antigens |
| WO2006048763A1 (en) * | 2004-11-05 | 2006-05-11 | Pharmacia & Upjohn Company Llc | Anti-bacterial vaccine compositions |
| EP2029173B1 (en) * | 2006-06-26 | 2016-07-20 | MacroGenics, Inc. | Fc riib-specific antibodies and methods of use thereof |
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- 2008-08-05 WO PCT/NL2008/050537 patent/WO2009020391A1/en not_active Ceased
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Patent Citations (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2004048515A2 (en) * | 2002-11-26 | 2004-06-10 | University Of Tennessee Research Foundation | Streptococcus uberis adhesion molecule |
Non-Patent Citations (2)
| Title |
|---|
| GROSCHUP M. H. et al Antigenic and genetic homogeneity of Streptococcus uberis strains from the bovine udder. Epidemiol Infect. 1991, v. 107(2), р297-310 * |
| LI Y., MARTINEZ G. et al Identification of a surface protein of Streptococcus suis and evaluation of its immunogenic and protective capacity in pigs. Infect Immun.2006, v 74(1), р.305-12. ALMEIDA R. A. et al Identification, isolation, and partial characterization of a novel Streptococcus uberis adhesion molecule (SUAM). 2006, v 15, 115 (1-3), р183-91. * |
Also Published As
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| CL2008002320A1 (es) | 2009-09-25 |
| AU2008284491A1 (en) | 2009-02-12 |
| ZA201000806B (en) | 2010-10-27 |
| EP2660604A3 (en) | 2014-02-12 |
| UA103885C2 (en) | 2013-12-10 |
| RU2010107878A (ru) | 2011-09-20 |
| CO6270172A2 (es) | 2011-04-20 |
| EP2183597B1 (en) | 2013-07-24 |
| CA2695721A1 (en) | 2009-02-12 |
| AR067830A1 (es) | 2009-10-21 |
| JP2010535500A (ja) | 2010-11-25 |
| MX2010001482A (es) | 2010-03-01 |
| CN101821627A (zh) | 2010-09-01 |
| EP2023143A1 (en) | 2009-02-11 |
| ES2432407T3 (es) | 2013-12-03 |
| JP2014095721A (ja) | 2014-05-22 |
| DK2183597T3 (da) | 2013-10-14 |
| KR20100063706A (ko) | 2010-06-11 |
| TW200911999A (en) | 2009-03-16 |
| WO2009020391A1 (en) | 2009-02-12 |
| EP2660604A2 (en) | 2013-11-06 |
| US20100297183A1 (en) | 2010-11-25 |
| EP2183597A1 (en) | 2010-05-12 |
| BRPI0815604A2 (pt) | 2015-03-03 |
| JP5462164B2 (ja) | 2014-04-02 |
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