EA015907B1 - Рекомбинантный флавивирус и его применение - Google Patents
Рекомбинантный флавивирус и его применение Download PDFInfo
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- EA015907B1 EA015907B1 EA200700904A EA200700904A EA015907B1 EA 015907 B1 EA015907 B1 EA 015907B1 EA 200700904 A EA200700904 A EA 200700904A EA 200700904 A EA200700904 A EA 200700904A EA 015907 B1 EA015907 B1 EA 015907B1
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- Prior art keywords
- flavivirus
- virus
- mutation
- protein
- mutations
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- C12N2770/24011—Flaviviridae
- C12N2770/24111—Flavivirus, e.g. yellow fever virus, dengue, JEV
- C12N2770/24122—New viral proteins or individual genes, new structural or functional aspects of known viral proteins or genes
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- Y02A50/00—TECHNOLOGIES FOR ADAPTATION TO CLIMATE CHANGE in human health protection, e.g. against extreme weather
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| PCT/US2005/037369 WO2006044857A2 (en) | 2004-10-20 | 2005-10-19 | Vaccines against japanese encephalitis virus and west nile virus |
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Cited By (1)
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| WO2014210358A1 (en) * | 2013-06-26 | 2014-12-31 | The University Of North Carolina At Chapel Hill | Methods and compositions for dengue virus vaccines |
Families Citing this family (29)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US7569383B2 (en) | 2001-06-01 | 2009-08-04 | Acambis Inc. | Chimeric flavivirus vectors |
| EP2295023A1 (en) | 2002-01-15 | 2011-03-16 | Sanofi Pasteur Biologics Co. | Flavivirus vaccines |
| JP4683926B2 (ja) | 2002-11-15 | 2011-05-18 | サノフィ パスツール バイオロジクス カンパニー | ウエストナイルウイルス・ワクチン |
| NZ584079A (en) | 2004-10-20 | 2011-10-28 | Acambis Inc | Vaccines against japanese encephalitis virus and west nile virus |
| AU2013204985B2 (en) * | 2005-04-24 | 2016-01-28 | Sanofi Pasteur Biologics, Llc | Recombinant flavivirus vaccines |
| RU2465326C2 (ru) | 2005-04-24 | 2012-10-27 | Санофи Пастер Байолоджикс Ко | Рекомбинантные флавивирусные вакцины |
| ES2618885T3 (es) | 2006-09-29 | 2017-06-22 | Takeda Vaccines, Inc. | Formulaciones de vacuna para norovirus |
| CL2007003209A1 (es) | 2006-11-07 | 2008-05-09 | Acambis Inc | Composicion que comprende una vacuna de flavivirus vivos atenuados; composicion que comprende un producto farmaceutico derivado de virus o proteina; un metodo para la elaboracion de una composicion terapeutica que comprende liofilizar las composicion |
| WO2008115314A2 (en) * | 2007-01-31 | 2008-09-25 | Sanofi Pasteur Biologics Co. | Flavivirus vaccine vector against influenza virus |
| US20100266636A1 (en) | 2007-09-18 | 2010-10-21 | Ligocyte Pharmaceuticals, Inc. | Method of conferring a protective immune response to norovirus |
| KR20100083150A (ko) | 2007-09-18 | 2010-07-21 | 리고사이트 파머슈티컬즈 인코퍼레이티드 | 노로바이러스에 대한 보호면역반응을 제공하는 방법 |
| US8715689B2 (en) * | 2008-04-30 | 2014-05-06 | The United States Of America As Represented By The Secretary Of The Department Of Health And Human Services, Centers For Disease Control And Prevention | Chimeric west nile/dengue viruses |
| AU2009279456B2 (en) | 2008-08-08 | 2015-02-05 | Takeda Vaccines, Inc. | Virus-like particles comprising composite capsid amino acid sequences for enhanced cross reactivity |
| CA2740598C (en) * | 2008-11-17 | 2018-05-22 | Mathura P. Ramanathan | Antigens that elicit immune response against flavivirus and methods of using same |
| US8968996B2 (en) | 2009-06-01 | 2015-03-03 | Takeda Vaccines, Inc. | Compositions and methods for rapid immunization against dengue virus |
| CN102449172A (zh) | 2009-06-01 | 2012-05-09 | 伊维拉根公司 | 施用针对登革病毒的疫苗的组合物和方法 |
| DK2459709T3 (en) * | 2009-07-31 | 2014-12-01 | Ge Healthcare Bio Sciences | HIGH-REPLACED YELLOW FEBER VIRUS TREASURY WITH INCREASED CELL STORAGE |
| BR112012024224A2 (pt) * | 2010-03-24 | 2016-11-29 | Arbovax Inc | mutações da faixa de hospedeiro de flavivírus e seu uso. |
| CN101926989A (zh) * | 2010-06-29 | 2010-12-29 | 西北农林科技大学 | 表达jev免疫原基因的重组减毒鼠伤寒沙门氏菌载体疫苗及其制备方法 |
| US8889148B2 (en) | 2010-07-01 | 2014-11-18 | Research Development Foundation | Flavivirus host-range mutations and uses thereof |
| HK1199202A1 (en) | 2011-07-11 | 2015-06-26 | 武田疫苗股份有限公司 | Parenteral norovirus vaccine formulations |
| US9267114B2 (en) * | 2012-11-07 | 2016-02-23 | Southern Research Institute | Flavivirus envelope protein mutations affecting virion disassembly |
| WO2014093182A1 (en) | 2012-12-14 | 2014-06-19 | Inviragen, Inc. | Compositions, methods of administration and uses for trivalent dengue virus formulations |
| US9861692B2 (en) | 2013-06-21 | 2018-01-09 | Merck Sharp & Dohme Corp. | Dengue virus vaccine compositions and methods of use thereof |
| WO2016079560A1 (en) * | 2014-11-21 | 2016-05-26 | Institut Pasteur | A live and attenuated japanese encephalitis virus comprising a mutated m protein |
| MX383329B (es) | 2014-12-22 | 2025-03-13 | Merck Sharp & Dohme Llc | Composiciones de vacuna para el virus del dengue y metodos de uso de las mismas. |
| MY187459A (en) * | 2015-07-16 | 2021-09-23 | Bharat Biotech Int Ltd | Vaccine compositions |
| EP3947655A1 (en) * | 2019-03-28 | 2022-02-09 | Institut Pasteur | A live and attenuated flavivirus comprising a mutated m protein |
| WO2024254552A1 (en) * | 2023-06-08 | 2024-12-12 | Modernatx, Inc. | Stabilized flavivirus vaccines |
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| US5173418A (en) | 1985-05-10 | 1992-12-22 | Benzon Pharma, A/S | Production in Escherichia coli of extracellular Serratia spp. hydrolases |
| US6184024B1 (en) * | 1988-07-14 | 2001-02-06 | The United States Of America As Represented By The Department Of Health And Human Services | Chimeric and/or growth-restricted flaviviruses |
| US6676936B1 (en) * | 1988-07-14 | 2004-01-13 | The United States Of America As Represented By The Department Of Health And Human Services. | Chimeric and/or growth-restricted flaviviruses |
| ES2244050T3 (es) * | 1997-02-28 | 2005-12-01 | Acambis Inc. | Vacunas quimericas de flavivirus. |
| US6962708B1 (en) * | 1997-02-28 | 2005-11-08 | Acambis, Inc. | Chimeric flavivirus vaccines |
| US6589533B1 (en) | 1997-09-18 | 2003-07-08 | Research Development Foundation | Genetically-engineered alphaviruses, flaviviruses, and bunyaviruses with modified envelope transmembrane glycoproteins and altered host-range phenotype |
| WO1999018216A2 (en) | 1997-10-08 | 1999-04-15 | The Government Of The United States Of America, Represented By The Secretary, Department Of Health And Human Services | Chimeric vaccine against tick-borne encephalitis virus |
| US7227011B2 (en) * | 1998-06-04 | 2007-06-05 | United States Of America As Represented By The Secretary Of The Department Of Health And Human Services, Centers For Disease Control And Prevention | Nucleic acid vaccines for prevention of flavivirus infection |
| WO2001039802A1 (en) | 1999-12-01 | 2001-06-07 | Oravax, Inc. | Chimeric flavivirus vaccines |
| WO2002081753A1 (en) | 2001-04-04 | 2002-10-17 | Advanced Research & Technology Institute | Method for identifying and characterizing individual dna molecules |
| WO2003060088A2 (en) | 2002-01-15 | 2003-07-24 | Acambis, Inc. | Viral vaccine production method |
| EP2295023A1 (en) | 2002-01-15 | 2011-03-16 | Sanofi Pasteur Biologics Co. | Flavivirus vaccines |
| US20050002968A1 (en) | 2002-01-15 | 2005-01-06 | Monath Thomas P. | Flavivirus vaccines |
| JP4683926B2 (ja) * | 2002-11-15 | 2011-05-18 | サノフィ パスツール バイオロジクス カンパニー | ウエストナイルウイルス・ワクチン |
| US7189403B2 (en) * | 2003-06-30 | 2007-03-13 | Institut Pasteur | Attenuated flavivirus strains containing a mutated M-ectodomain and their applications |
| NZ584079A (en) | 2004-10-20 | 2011-10-28 | Acambis Inc | Vaccines against japanese encephalitis virus and west nile virus |
| RU2465326C2 (ru) | 2005-04-24 | 2012-10-27 | Санофи Пастер Байолоджикс Ко | Рекомбинантные флавивирусные вакцины |
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2011
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Non-Patent Citations (1)
| Title |
|---|
| MONATH, T.P. Recombinant, chimeric live, attenuated vaccine (ChimeriVaxTM) incorporating the envelope genes of Japanese encephalitis (SA14-14-2) virus and the capsid and nonstructural genes of yellow fever (17D) virus is safe, immunogenic and protective in non-human primates, Vaccine, 1999, Vol. 17, pages 1869-1882 * |
Cited By (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2014210358A1 (en) * | 2013-06-26 | 2014-12-31 | The University Of North Carolina At Chapel Hill | Methods and compositions for dengue virus vaccines |
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| NO20071924L (no) | 2007-07-17 |
| US8029802B2 (en) | 2011-10-04 |
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| EP1809325A4 (en) | 2009-07-22 |
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| EP1809325A2 (en) | 2007-07-25 |
| WO2006044857A2 (en) | 2006-04-27 |
| US20120201852A1 (en) | 2012-08-09 |
| IL182453A0 (en) | 2007-07-24 |
| US8691550B2 (en) | 2014-04-08 |
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