SG176807A1 - Vaccine - Google Patents
Vaccine Download PDFInfo
- Publication number
- SG176807A1 SG176807A1 SG2011091881A SG2011091881A SG176807A1 SG 176807 A1 SG176807 A1 SG 176807A1 SG 2011091881 A SG2011091881 A SG 2011091881A SG 2011091881 A SG2011091881 A SG 2011091881A SG 176807 A1 SG176807 A1 SG 176807A1
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- Prior art keywords
- protein
- immunogenic composition
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- rsv
- polypeptide
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| US8563002B2 (en) * | 2007-12-24 | 2013-10-22 | Glaxosmithkline Biologicals, S.A. | Recombinant RSV antigens |
| PL2445526T3 (pl) | 2009-06-24 | 2017-08-31 | Glaxosmithkline Biologicals S.A. | Rekombinowane antygeny rsv |
| EP4183412B1 (en) | 2009-07-15 | 2024-08-14 | GlaxoSmithKline Biologicals SA | Rsv f protein compositions and methods for making same |
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| EP2668282A2 (en) * | 2011-01-28 | 2013-12-04 | MedImmune, LLC | Expression of soluble viral fusion glycoproteins in mammalian cells |
| RS56748B1 (sr) | 2011-05-13 | 2018-03-30 | Glaxosmithkline Biologicals Sa | Pre-fuzioni rsv f antigeni |
| US9463236B2 (en) | 2011-08-29 | 2016-10-11 | Tokushima University | RSV mucosal vaccine |
| DK2750683T4 (da) * | 2011-10-03 | 2021-04-12 | Croda Int Plc | Nanopartikler, fremgangsmåde til fremstilling og anvendelse deraf som bærer for amfipatiske eller hydrofobe molekyler inden for medicin, herunder cancerbehandling, og i fødevarerelaterede forbindelser |
| KR102149069B1 (ko) * | 2012-03-20 | 2020-08-28 | 후맙스 바이오메드 에스에이 | Rsv, mpv 및 pvm를 중화하는 항체 및 이의 용도 |
| EA039682B1 (ru) * | 2012-06-04 | 2022-02-28 | Хумабс Биомед Са | Антитела, нейтрализующие rsv, mpv и pvm, и их применения |
| CN102743750B (zh) * | 2012-07-09 | 2013-11-20 | 江苏省农业科学院 | 一种复方免疫增强剂、禽用疫苗及其制备方法 |
| SI2879702T1 (sl) | 2012-08-01 | 2020-02-28 | Bavarian Nordic A/S | Cepivo na osnovi rekombinantnega modificiranega virusa vakcinacije Ankara (MVA) proti respiratornemu sincitialnemu virusu (RSV) |
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| KR20150085843A (ko) * | 2012-11-20 | 2015-07-24 | 글락소스미스클라인 바이오로지칼즈 에스.에이. | Rsv f 융합전 삼합체 |
| EP4421177A3 (en) | 2013-03-13 | 2024-12-18 | The United States of America, as represented by the Secretary, Department of Health and Human Services | Prefusion rsv f proteins and their use |
| US9738689B2 (en) | 2013-03-13 | 2017-08-22 | The United States Of America, As Represented By The Secretary, Department Of Health And Human Services | Prefusion RSV F proteins and their use |
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| MX2015013832A (es) * | 2013-04-08 | 2016-06-10 | Medimmune Llc | Composicion de vacuna y metodo de uso. |
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| CN105408348B (zh) | 2013-06-17 | 2021-07-06 | 扬森疫苗与预防公司 | 稳定化的可溶性融合前rsv f多肽 |
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| US9322037B2 (en) * | 2013-09-06 | 2016-04-26 | President And Fellows Of Harvard College | Cas9-FokI fusion proteins and uses thereof |
| US10420834B2 (en) | 2014-12-24 | 2019-09-24 | The United States Of America, As Represented By The Secretary, Department Of Health And Human Services | Recombinant metapneumovirus F proteins and their use |
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| AU2016289496B2 (en) | 2015-07-07 | 2021-02-04 | Janssen Vaccines & Prevention B.V. | Stabilized soluble pre-fusion RSV F polypeptides |
| DE20164728T1 (de) | 2015-10-22 | 2021-09-30 | Modernatx, Inc. | Impfstoffe gegen atemwegsvirus |
| RU2723039C2 (ru) | 2015-12-23 | 2020-06-08 | Пфайзер Инк. | Мутанты белка f rsv |
| AU2017248018A1 (en) | 2016-04-05 | 2018-09-27 | Janssen Vaccines & Prevention B.V. | Vaccine against RSV |
| MX2018012094A (es) | 2016-04-05 | 2019-01-10 | Janssen Vaccines & Prevention Bv | Proteinas f de prefusion del virus respiratorio sincicial (vrs) solubles y estabilizadas. |
| CN105693829B (zh) * | 2016-04-14 | 2022-03-15 | 青岛易邦生物工程有限公司 | 一种b型禽偏肺病毒f蛋白 |
| US12128113B2 (en) | 2016-05-18 | 2024-10-29 | Modernatx, Inc. | Polynucleotides encoding JAGGED1 for the treatment of Alagille syndrome |
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| CN106119287B (zh) * | 2016-08-29 | 2019-10-11 | 广东华南疫苗股份有限公司 | 一种表达呼吸道合胞病毒f蛋白的重组载体及方法 |
| WO2018081289A2 (en) | 2016-10-25 | 2018-05-03 | The United States Of America, As Represented By The Secretary, Department Of Health And Human Services | Prefusion piv f immunogens and their use |
| TWI683826B (zh) * | 2016-11-22 | 2020-02-01 | 國立臺灣大學 | 重組rsv抗原 |
| EP3551193A4 (en) * | 2016-12-08 | 2020-08-19 | Modernatx, Inc. | NUCLEIC ACID VACCINES AGAINST RESPIRATORY VIRUSES |
| WO2018170270A1 (en) | 2017-03-15 | 2018-09-20 | Modernatx, Inc. | Varicella zoster virus (vzv) vaccine |
| WO2018170347A1 (en) | 2017-03-17 | 2018-09-20 | Modernatx, Inc. | Zoonotic disease rna vaccines |
| CA3062549A1 (en) | 2017-05-15 | 2018-11-22 | Janssen Vaccines & Prevention B.V. | Stable virus-containing composition |
| EP3624851A1 (en) | 2017-05-15 | 2020-03-25 | Janssen Vaccines & Prevention B.V. | Stable virus-containing composition |
| CA3061278A1 (en) | 2017-05-17 | 2018-11-22 | Janssen Vaccines & Prevention B.V. | Methods and compositions for inducing protective immunity against rsv infection |
| AU2018333566A1 (en) | 2017-09-15 | 2020-02-27 | Janssen Vaccines & Prevention B.V. | Method for the safe induction of immunity against RSV |
| WO2019063844A1 (en) * | 2017-09-29 | 2019-04-04 | Universiteit Antwerpen | VACCINATION AGAINST SYNCYTIAL RESPIRATORY VIRUS |
| WO2019092002A1 (en) * | 2017-11-07 | 2019-05-16 | Valneva Se | Pharmaceutical compositions for treatment or prevention of viral infections |
| US11911453B2 (en) | 2018-01-29 | 2024-02-27 | Modernatx, Inc. | RSV RNA vaccines |
| PE20211469A1 (es) | 2018-11-13 | 2021-08-05 | Janssen Vaccines And Prevention B V | Proteinas f de prefusion del vrs estabilizadas |
| EP3923983A4 (en) * | 2019-02-11 | 2023-02-22 | Emory University | CHIMERIC RSV AND HMPV F PROTEINS, IMMUNOGENIC COMPOSITIONS AND METHODS OF USE |
| US11351242B1 (en) | 2019-02-12 | 2022-06-07 | Modernatx, Inc. | HMPV/hPIV3 mRNA vaccine composition |
| KR20220010478A (ko) | 2019-05-20 | 2022-01-25 | 발네바 에스이 | 기도 감염의 치료 또는 예방용 서브유닛 백신 |
| KR20220133911A (ko) * | 2020-01-30 | 2022-10-05 | 모더나티엑스, 인크. | 호흡기 바이러스 면역화 조성물 |
| US12679870B2 (en) | 2020-04-29 | 2026-07-14 | The United States Of America, As Represented By The Secretary, Department Of Health And Human Services | Recombinant human metapneumovirus F proteins and their use |
| WO2022099003A1 (en) | 2020-11-06 | 2022-05-12 | Sanofi | Lipid nanoparticles for delivering mrna vaccines |
| AU2022220616A1 (en) * | 2021-02-12 | 2023-08-31 | Merck Sharp & Dohme Llc | Antibodies that bind metapneumovirus, antigenic metapneumovirus proteins, and uses thereof |
| US20240228548A9 (en) | 2021-02-19 | 2024-07-11 | Janssen Vaccines & Prevention B.V. | Stabilized pre-fusion rsv fb antigens |
| AR127808A1 (es) * | 2021-11-30 | 2024-02-28 | Sanofi Pasteur Inc | Vacunas contra el metapneumovirus humano |
| JP2024544054A (ja) * | 2021-11-30 | 2024-11-27 | サノフィ パスツール インコーポレイテッド | ヒトメタニューモウイルスのウイルスベクターに基づくワクチン |
| CN116554341B (zh) * | 2022-01-29 | 2026-06-12 | 中国疾病预防控制中心病毒病预防控制所 | 一种人偏肺病毒病毒样颗粒、制备方法、应用及疫苗 |
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| WO2026148356A1 (en) | 2025-01-06 | 2026-07-09 | BioNTech SE | Coronavirus and influenza immunogenic combinations |
Family Cites Families (60)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4235877A (en) | 1979-06-27 | 1980-11-25 | Merck & Co., Inc. | Liposome particle containing viral or bacterial antigenic subunit |
| US4372945A (en) | 1979-11-13 | 1983-02-08 | Likhite Vilas V | Antigen compounds |
| IL61904A (en) | 1981-01-13 | 1985-07-31 | Yeda Res & Dev | Synthetic vaccine against influenza virus infections comprising a synthetic peptide and process for producing same |
| US4866034A (en) | 1982-05-26 | 1989-09-12 | Ribi Immunochem Research Inc. | Refined detoxified endotoxin |
| US4436727A (en) | 1982-05-26 | 1984-03-13 | Ribi Immunochem Research, Inc. | Refined detoxified endotoxin product |
| SE8205892D0 (sv) | 1982-10-18 | 1982-10-18 | Bror Morein | Immunogent membranproteinkomplex, sett for framstellning och anvendning derav som immunstimulerande medel och sasom vaccin |
| US4707543A (en) | 1985-09-17 | 1987-11-17 | The United States Of America As Represented By The Secretary Of The Army | Process for the preparation of detoxified polysaccharide-outer membrane protein complexes, and their use as antibacterial vaccines |
| US5149650A (en) | 1986-01-14 | 1992-09-22 | University Of North Carolina At Chapel Hill | Vaccines for human respiratory virus |
| US4877611A (en) | 1986-04-15 | 1989-10-31 | Ribi Immunochem Research Inc. | Vaccine containing tumor antigens and adjuvants |
| CA1331443C (en) | 1987-05-29 | 1994-08-16 | Charlotte A. Kensil | Saponin adjuvant |
| US5057540A (en) | 1987-05-29 | 1991-10-15 | Cambridge Biotech Corporation | Saponin adjuvant |
| US5726292A (en) | 1987-06-23 | 1998-03-10 | Lowell; George H. | Immuno-potentiating systems for preparation of immunogenic materials |
| US5278302A (en) | 1988-05-26 | 1994-01-11 | University Patents, Inc. | Polynucleotide phosphorodithioates |
| US4912094B1 (en) | 1988-06-29 | 1994-02-15 | Ribi Immunochem Research Inc. | Modified lipopolysaccharides and process of preparation |
| US6245549B1 (en) * | 1990-06-28 | 2001-06-12 | Connaught Laboratories Limited | Production of virus and purification of viral envelope proteins for vaccine use |
| GB9120221D0 (en) | 1991-09-23 | 1991-11-06 | Smithkline Beecham Biolog | Novel compounds |
| GB9200117D0 (en) * | 1992-01-06 | 1992-02-26 | Connaught Lab | Production of recombinant chimeric proteins for vaccine use |
| DE69313134T2 (de) | 1992-06-25 | 1998-02-26 | Smithkline Beecham Biolog | Adjuvantien enthaltende impfstoffzusammensetzung |
| KR100310510B1 (ko) | 1993-03-23 | 2002-07-04 | 장 스테판느 | 3-0-탈아세틸화모노포스포릴지질a를함유하는백신조성물 |
| US5961970A (en) | 1993-10-29 | 1999-10-05 | Pharmos Corporation | Submicron emulsions as vaccine adjuvants |
| PT729473E (pt) | 1993-11-17 | 2001-02-28 | Deutsche Om Arzneimittel Gmbh | Dissacaridos de glucosamina metodo para a sua preparacao composicao farmaceutica contendo os mesmos e sua utilizacao |
| WO1995026204A1 (en) | 1994-03-25 | 1995-10-05 | Isis Pharmaceuticals, Inc. | Immune stimulation by phosphorothioate oligonucleotide analogs |
| FR2718452B1 (fr) | 1994-04-06 | 1996-06-28 | Pf Medicament | Elément d'immunogène, agent immunogène, composition pharmaceutique et procédé de préparation. |
| AU713040B2 (en) | 1994-07-15 | 1999-11-18 | University Of Iowa Research Foundation, The | Immunomodulatory oligonucleotides |
| AUPM873294A0 (en) | 1994-10-12 | 1994-11-03 | Csl Limited | Saponin preparations and use thereof in iscoms |
| UA56132C2 (uk) | 1995-04-25 | 2003-05-15 | Смітклайн Бічем Байолоджікалс С.А. | Композиція вакцини (варіанти), спосіб стабілізації qs21 відносно гідролізу (варіанти), спосіб приготування композиції вакцини |
| US5666153A (en) | 1995-10-03 | 1997-09-09 | Virtual Shopping, Inc. | Retractable teleconferencing apparatus |
| US5856462A (en) | 1996-09-10 | 1999-01-05 | Hybridon Incorporated | Oligonucleotides having modified CpG dinucleosides |
| US6764840B2 (en) | 1997-05-08 | 2004-07-20 | Corixa Corporation | Aminoalkyl glucosaminide phosphate compounds and their use as adjuvants and immunoeffectors |
| US6113918A (en) | 1997-05-08 | 2000-09-05 | Ribi Immunochem Research, Inc. | Aminoalkyl glucosamine phosphate compounds and their use as adjuvants and immunoeffectors |
| US6303347B1 (en) | 1997-05-08 | 2001-10-16 | Corixa Corporation | Aminoalkyl glucosaminide phosphate compounds and their use as adjuvants and immunoeffectors |
| US7208161B1 (en) | 1997-05-23 | 2007-04-24 | The United States Of America, Represented By The Secretary, Department Of Health And Human Services | Production of attenuated parainfluenza virus vaccines from cloned nucleotide sequences |
| CA2302833C (en) | 1997-09-19 | 2007-05-08 | American Cyanamid Company | Peptides derived from the attachment (g) protein of respiratory syncytial virus |
| GB9727262D0 (en) | 1997-12-24 | 1998-02-25 | Smithkline Beecham Biolog | Vaccine |
| EP1089913A1 (fr) | 1998-06-08 | 2001-04-11 | SCA Emballage France | Emballage a remise a plat rapide |
| SK287073B6 (sk) | 1998-06-30 | 2009-11-05 | Om Pharma | N-Acyldipeptidový derivát, spôsob jeho prípravy a farmaceutický prostriedok, ktorý ho obsahuje |
| ES2284287T3 (es) | 1998-10-16 | 2007-11-01 | Glaxosmithkline Biologicals S.A. | Sistemas adyuvantes y vacunas. |
| US6551600B2 (en) | 1999-02-01 | 2003-04-22 | Eisai Co., Ltd. | Immunological adjuvant compounds compositions and methods of use thereof |
| US20040006242A1 (en) | 1999-02-01 | 2004-01-08 | Hawkins Lynn D. | Immunomodulatory compounds and method of use thereof |
| AU1581400A (en) | 1999-12-22 | 2001-07-03 | Om Pharma | Acyl pseudopeptides bearing a functionalised auxiliary spacer |
| US20040161846A1 (en) | 2000-11-22 | 2004-08-19 | Mason Anthony John | Method of expression and agents identified thereby |
| US20040096451A1 (en) * | 2002-07-25 | 2004-05-20 | Young James F. | Methods of treating and preventing RSV, hMPV, and PIV using anti-RSV, anti-hMPV, and anti-PIV antibodies |
| DK1395669T3 (da) | 2001-01-26 | 2009-11-16 | Selexis Sa | Matriks bindingsregioner og fremgangsmåder til anvendelse af disse |
| EP1372706B1 (en) | 2001-03-09 | 2010-12-01 | ID Biomedical Corporation of Quebec | Proteosome-liposaccharide vaccine adjuvant |
| JP4331944B2 (ja) | 2001-04-17 | 2009-09-16 | 大日本住友製薬株式会社 | 新規アデニン誘導体 |
| DK1719511T3 (da) | 2001-11-16 | 2009-04-14 | Coley Pharm Group Inc | N-[4-(4-amino-2-ethyl-1H-imidazo[4,5-c]quinolin-1-yl)butyl]methansulfonamid, en farmaceutisk sammensætning omfattende samme, og anvendelse deraf |
| DE10221836A1 (de) * | 2002-05-16 | 2003-12-04 | Lohmann Animal Health Gmbh | Attenuierung von Metapneumovirus |
| JP2006517974A (ja) | 2003-02-13 | 2006-08-03 | スリーエム イノベイティブ プロパティズ カンパニー | Irm化合物およびトル様受容体8に関する方法および組成物 |
| US7563449B2 (en) | 2003-04-21 | 2009-07-21 | Pfizer Inc, | Methods for reducing cattle reproductive diseases |
| CA2523657A1 (en) * | 2003-04-25 | 2005-03-31 | Medimmune Vaccines, Inc. | Recombinant parainfluenza virus expression systems and vaccines comprising heterologous antigens derived from metapneumovirus |
| US7368537B2 (en) | 2003-07-15 | 2008-05-06 | Id Biomedical Corporation Of Quebec | Subunit vaccine against respiratory syncytial virus infection |
| KR101269656B1 (ko) | 2003-10-24 | 2013-05-30 | 셀렉시스 에스. 에이. | Mar 서열의 복합 트랜스펙션 방법에 의한 포유동물 세포에서의 고효율 유전자 전달 및 발현 |
| FR2873378A1 (fr) | 2004-07-23 | 2006-01-27 | Pierre Fabre Medicament Sa | Complexes immunogenes, leur procede de preparation et leur utilisation dans des compositions pharmaceutiques |
| GB0422439D0 (en) | 2004-10-08 | 2004-11-10 | European Molecular Biology Lab Embl | Inhibitors of infection |
| TWI457133B (zh) | 2005-12-13 | 2014-10-21 | Glaxosmithkline Biolog Sa | 新穎組合物 |
| EP2181121A4 (en) | 2007-03-21 | 2012-07-11 | Id Biomedical Corp Quebec | CHIMÄRE ANTIGENE |
| WO2008154456A2 (en) * | 2007-06-06 | 2008-12-18 | Nationwide Children's Hospital, Inc. | Methods and compositions relating to viral fusion proteins |
| CL2008002361A1 (es) | 2007-08-13 | 2009-08-07 | Glaxosmithkline Biologicals Sa | Uso de un antigeno derivado de la proteina circumesporozoito (cs) de plasmodium falciparum que se expresa en la etapa preeritrocitica de la infeccion por malaria para tratar bebes contra la malaria. |
| US8563002B2 (en) * | 2007-12-24 | 2013-10-22 | Glaxosmithkline Biologicals, S.A. | Recombinant RSV antigens |
| PL2445526T3 (pl) * | 2009-06-24 | 2017-08-31 | Glaxosmithkline Biologicals S.A. | Rekombinowane antygeny rsv |
-
2010
- 2010-06-24 SG SG2011091881A patent/SG176807A1/en unknown
- 2010-06-24 EA EA201270062A patent/EA201270062A1/ru unknown
- 2010-06-24 MX MX2012000036A patent/MX2012000036A/es not_active Application Discontinuation
- 2010-06-24 JP JP2012516745A patent/JP5796011B2/ja active Active
- 2010-06-24 US US13/378,402 patent/US8889146B2/en active Active
- 2010-06-24 EP EP10728203A patent/EP2445527A2/en not_active Withdrawn
- 2010-06-24 WO PCT/EP2010/059006 patent/WO2010149743A2/en not_active Ceased
- 2010-06-24 CA CA2766205A patent/CA2766205A1/en active Pending
- 2010-06-24 CN CN2010800374300A patent/CN102548578A/zh active Pending
- 2010-06-24 AU AU2010264686A patent/AU2010264686A1/en not_active Abandoned
- 2010-06-24 KR KR1020127001752A patent/KR20120093811A/ko not_active Withdrawn
-
2011
- 2011-12-13 ZA ZA2011/09164A patent/ZA201109164B/en unknown
- 2011-12-15 IL IL217008A patent/IL217008A0/en unknown
Also Published As
| Publication number | Publication date |
|---|---|
| MX2012000036A (es) | 2012-02-28 |
| EP2445527A2 (en) | 2012-05-02 |
| US20120135028A1 (en) | 2012-05-31 |
| ZA201109164B (en) | 2012-09-26 |
| AU2010264686A1 (en) | 2012-01-19 |
| EA201270062A1 (ru) | 2013-02-28 |
| CA2766205A1 (en) | 2010-12-29 |
| IL217008A0 (en) | 2012-02-29 |
| JP5796011B2 (ja) | 2015-10-21 |
| CN102548578A (zh) | 2012-07-04 |
| KR20120093811A (ko) | 2012-08-23 |
| WO2010149743A3 (en) | 2011-03-10 |
| WO2010149743A2 (en) | 2010-12-29 |
| US8889146B2 (en) | 2014-11-18 |
| JP2012530761A (ja) | 2012-12-06 |
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