KR20250023601A - 선융합(prefusion) RSV F 단백질 및 이의 용도 - Google Patents
선융합(prefusion) RSV F 단백질 및 이의 용도 Download PDFInfo
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- KR20250023601A KR20250023601A KR1020257003905A KR20257003905A KR20250023601A KR 20250023601 A KR20250023601 A KR 20250023601A KR 1020257003905 A KR1020257003905 A KR 1020257003905A KR 20257003905 A KR20257003905 A KR 20257003905A KR 20250023601 A KR20250023601 A KR 20250023601A
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Families Citing this family (155)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US20080124355A1 (en) | 2006-09-22 | 2008-05-29 | David Gordon Bermudes | Live bacterial vaccines for viral infection prophylaxis or treatment |
| US20110229471A1 (en) | 2008-11-26 | 2011-09-22 | Cedars-Sinai Medical Center | Methods of determining responsiveness to anti-tnf alpha therapy in inflammatory bowel disease |
| WO2012116715A1 (en) | 2011-03-02 | 2012-09-07 | Curevac Gmbh | Vaccination in newborns and infants |
| CA2900110A1 (en) | 2013-02-01 | 2014-08-07 | Medimmune, Llc | Respiratory syncytial virus f protein epitopes |
| 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 |
| EP2970398B1 (en) | 2013-03-13 | 2024-05-08 | The United States of America, as Represented by The Secretary, Department of Health and Human Services | Prefusion rsv f proteins and their use |
| EP3798310A1 (en) | 2013-03-14 | 2021-03-31 | Emory University | Recombinant rsv with silent mutations, vaccines, and methods related thereto |
| KR20230109779A (ko) | 2013-03-27 | 2023-07-20 | 세다르스-신나이 메디칼 센터 | Tl1a 기능 및 관련된 신호전달 경로의 저해에 의한섬유증 및 염증의 완화 및 반전 |
| KR102236497B1 (ko) | 2013-04-25 | 2021-04-06 | 얀센 백신스 앤드 프리벤션 비.브이. | 안정화된 가용성 예비융합 ｒｓｖ ｆ 폴리펩타이드 |
| 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 |
| EP3022295A4 (en) | 2013-07-19 | 2017-03-01 | Cedars-Sinai Medical Center | Signature of tl1a (tnfsf15) signaling pathway |
| US10125172B2 (en) | 2013-07-25 | 2018-11-13 | Calder Biosciences Inc. | Conformationally stabilized RSV pre-fusion F proteins |
| BR112016003361A2 (pt) | 2013-08-21 | 2017-11-21 | Curevac Ag | vacina do vírus sincicial respiratório (rsv) |
| JP2016533332A (ja) * | 2013-09-24 | 2016-10-27 | マサチューセッツ インスティテュート オブ テクノロジー | 自己集合型ナノ粒子ワクチン |
| US9630994B2 (en) | 2014-11-03 | 2017-04-25 | University Of Washington | Polypeptides for use in self-assembling protein nanostructures |
| DK3247388T3 (da) | 2015-01-20 | 2025-12-22 | Us Health | Rekombinant human/bovin parainfluenzavirus 3 (b/hpiv3), der udtrykker et kimærisk rsv/bpiv3 f-protein, og anvendelser deraf |
| EP3250233A4 (en) | 2015-01-29 | 2018-07-25 | Agency for Science, Technology and Research | Nanocapsules carrying chikungunya-associated peptides |
| US10676723B2 (en) | 2015-05-11 | 2020-06-09 | David Gordon Bermudes | Chimeric protein toxins for expression by therapeutic bacteria |
| US10457708B2 (en) | 2015-07-07 | 2019-10-29 | Janssen Vaccines & Prevention B.V. | Stabilized soluble pre-fusion RSV F polypeptides |
| EA039065B1 (ru) * | 2015-07-07 | 2021-11-29 | Янссен Вэксинс Энд Превеншн Б.В. | Вакцина против rsv |
| FR3041962B1 (fr) * | 2015-10-01 | 2018-01-05 | Lab Francais Du Fractionnement | Procede d'enrichissement d'une preparation d'immunoglobulines en immunoglobulines anti-rsv et preparation ainsi enrichie |
| EP4011451A1 (en) | 2015-10-22 | 2022-06-15 | ModernaTX, Inc. | Metapneumovirus mrna vaccines |
| EA201891000A1 (ru) * | 2015-10-22 | 2018-12-28 | МОДЕРНАТиЭкс, ИНК. | Вакцина против респираторно-синцитиального вируса |
| MX2018005462A (es) | 2015-10-29 | 2018-08-01 | Univ Emory | Composiciones inmunogénicas de rsv quimérico y métodos de uso. |
| RU2723039C2 (ru) * | 2015-12-23 | 2020-06-08 | Пфайзер Инк. | Мутанты белка f rsv |
| KR20240095481A (ko) | 2016-03-17 | 2024-06-25 | 세다르스-신나이 메디칼 센터 | Rnaset2를 통한 염증성 장 질환의 진단 방법 |
| WO2017172890A1 (en) | 2016-03-29 | 2017-10-05 | The United States Of America, As Represented By The Secretary, Department Of Health And Human Services | Substitutions-modified prefusion rsv f proteins and their use |
| JP7233928B2 (ja) | 2016-04-05 | 2023-03-07 | ヤンセン ファッシンズ アンド プリベンション ベーフェー | Ｒｓｖに対するワクチン |
| IL262108B2 (en) | 2016-04-05 | 2023-04-01 | Janssen Vaccines Prevention B V | Soluble pre-fusion rsv f proteins are stabilized |
| IL245059A0 (en) | 2016-04-12 | 2016-06-30 | Technion Res & Dev Foundation | Electrospun scaffolds from extracellular matrix |
| CN109311946A (zh) | 2016-05-30 | 2019-02-05 | 扬森疫苗与预防公司 | 稳定化的融合前rsv f蛋白 |
| US10961283B2 (en) | 2016-06-27 | 2021-03-30 | The United States Of America, As Represented By The Secretary, Department Of Health And Human Services | Self-assembling insect ferritin nanoparticles for display of co-assembled trimeric antigens |
| 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 |
| EP3518967A4 (en) | 2016-10-03 | 2020-04-29 | University of Massachusetts | Methods for immunizing pre-immune subjects against respiratory syncytial virus (rsv) |
| EP3532096B1 (en) | 2016-10-25 | 2023-02-22 | The U.S.A. as represented by the Secretary, Department of Health and Human Services | Prefusion piv f immunogens and their use |
| KR20190082815A (ko) | 2016-10-26 | 2019-07-10 | 세다르스-신나이 메디칼 센터 | 중화 항-tl1a 단일 클론 항체 |
| TWI683826B (zh) * | 2016-11-22 | 2020-02-01 | 國立臺灣大學 | 重組ｒｓｖ抗原 |
| US11129906B1 (en) | 2016-12-07 | 2021-09-28 | David Gordon Bermudes | Chimeric protein toxins for expression by therapeutic bacteria |
| US11180535B1 (en) | 2016-12-07 | 2021-11-23 | David Gordon Bermudes | Saccharide binding, tumor penetration, and cytotoxic antitumor chimeric peptides from therapeutic bacteria |
| WO2018107088A2 (en) | 2016-12-08 | 2018-06-14 | Modernatx, Inc. | Respiratory virus nucleic acid vaccines |
| US11084850B2 (en) | 2016-12-16 | 2021-08-10 | The Pirbright Institute | Recombinant prefusion RSV F proteins and uses thereof |
| GB201621686D0 (en) | 2016-12-20 | 2017-02-01 | Glaxosmithkline Biologicals Sa | Novel methods for inducing an immune response |
| CN108265079A (zh) * | 2017-01-02 | 2018-07-10 | 刘昕 | 一种新型呼吸道合胞体病毒pre-F融合蛋白载体的制备方法 |
| EP3595713A4 (en) | 2017-03-15 | 2021-01-13 | ModernaTX, Inc. | RESPIRATORY SYNCYTIAL VIRUS Vaccine |
| WO2018175518A1 (en) * | 2017-03-22 | 2018-09-27 | The Scripps Research Institute | Mini-protein immunogens displayng neutralization epitopes for respiratory syncytial virus (rsv) |
| HUE073526T2 (hu) | 2017-04-04 | 2026-01-28 | Univ Washington | Önmagát összeállító fehérje nanostruktúrák, amelyek paramyxovírus és/vagy pneumovírus F fehérjéket jelenítenek meg és azok használata |
| AU2018267971A1 (en) | 2017-05-17 | 2019-11-07 | Janssen Vaccines & Prevention B.V. | Methods and compositions for inducing protective immunity against RSV infection |
| GB2600653B (en) | 2017-05-30 | 2022-11-02 | Glaxosmithkline Biologicals Sa | Novel methods |
| CA3066026A1 (en) * | 2017-06-14 | 2018-12-20 | Virometix Ag | Cyclic peptides for protection against respiratory syncytial virus |
| CN119529036A (zh) * | 2017-08-07 | 2025-02-28 | 考尔德生物科技有限公司 | 构象稳定的rsv预融合f蛋白 |
| SG11202001458SA (en) | 2017-09-15 | 2020-03-30 | Janssen Vaccines & Prevention Bv | Method for the safe induction of immunity against rsv |
| JP2019092481A (ja) * | 2017-11-27 | 2019-06-20 | 国立大学法人東京工業大学 | ヘテロタンパク質ケージ |
| BR112020010790A2 (pt) | 2017-12-01 | 2020-11-10 | Glaxosmithkline Biologicals S.A. | purificação da saponina |
| BR112020015308A8 (pt) * | 2018-01-29 | 2023-02-07 | Merck Sharp & Dohme | Proteínas f de rsv estabilizadas e usos das mesmas |
| EP3746090A4 (en) * | 2018-01-29 | 2021-11-17 | ModernaTX, Inc. | RSV RNA Vaccines |
| WO2019169120A1 (en) | 2018-02-28 | 2019-09-06 | University Of Washington | Self-asssembling nanostructure vaccines |
| US11623004B2 (en) * | 2018-03-16 | 2023-04-11 | University Of Pittsburgh Of The Commonwealth System Of Higher Education | Compositions and methods for vaccination against respiratory syncytial virus infection |
| JP2021519600A (ja) * | 2018-04-03 | 2021-08-12 | サノフイＳａｎｏｆｉ | 抗原性インフルエンザ−フェリチンポリペプチド |
| WO2019195314A2 (en) | 2018-04-03 | 2019-10-10 | Sanofi | Antigenic epstein barr virus polypeptides |
| EP3773698A1 (en) | 2018-04-03 | 2021-02-17 | Sanofi | Ferritin proteins |
| JP7614841B2 (ja) * | 2018-04-03 | 2025-01-16 | サノフイ | 抗原性呼吸器合胞体ウイルスポリペプチド |
| AU2019254591B2 (en) | 2018-04-17 | 2025-12-11 | CureVac SE | Novel RSV RNA molecules and compositions for vaccination |
| CN112585165B8 (zh) | 2018-04-25 | 2025-02-14 | 普罗米修斯生物科学公司 | 优化的抗tl1a抗体 |
| CN112638411B (zh) | 2018-05-04 | 2025-03-04 | 斯拜生物技术有限公司 | 疫苗组合物 |
| CN110684747B (zh) | 2018-07-06 | 2024-05-24 | 厦门大学 | 灭活及保存呼吸道合胞病毒的方法 |
| CN112566654A (zh) * | 2018-07-31 | 2021-03-26 | 葛兰素史密丝克莱恩生物有限公司 | 抗原纯化方法 |
| US11890339B2 (en) | 2018-08-03 | 2024-02-06 | The United States of Americam as represented by the Secretary, Department of Health and Human Services | Nipah virus immunogens and their use |
| EP3833382A1 (en) | 2018-08-07 | 2021-06-16 | GlaxoSmithKline Biologicals S.A. | Processes and vaccines |
| MX2021005607A (es) * | 2018-11-13 | 2021-06-30 | Janssen Vaccines & Prevention Bv | Proteinas f de prefusion del vrs estabilizadas. |
| EP3880698A4 (en) | 2018-11-14 | 2022-11-30 | RubrYc Therapeutics, Inc. | MANIPULATED CD25 POLYPEPTIDES AND USES THEREOF |
| US11351242B1 (en) | 2019-02-12 | 2022-06-07 | Modernatx, Inc. | HMPV/hPIV3 mRNA vaccine composition |
| EP3932424A4 (en) | 2019-02-28 | 2022-10-12 | KM Biologics Co., Ltd. | Rsv f/g chimeric vaccine |
| WO2020245207A1 (en) | 2019-06-05 | 2020-12-10 | Glaxosmithkline Biologicals Sa | Saponin purification |
| EP4025587A1 (en) | 2019-09-04 | 2022-07-13 | University of Washington | Self-assembling protein nanostructures displaying paramyxovirus and/or pneumovirus f proteins and their use |
| NZ787680A (en) | 2019-10-24 | 2026-02-27 | Cedars Sinai Medical Center | Humanized antibodies to tnf-like ligand 1a (tl1a) and uses thereof |
| WO2021119497A1 (en) | 2019-12-11 | 2021-06-17 | The United States Of America, As Represented By The Secretary, Department Of Health And Human Services | Mumps and measles virus immunogens and their use |
| TWI874544B (zh) * | 2019-12-23 | 2025-03-01 | 日商田邊三菱製藥股份有限公司 | 變異型rsv f蛋白質及其利用 |
| US10953089B1 (en) | 2020-01-27 | 2021-03-23 | Novavax, Inc. | Coronavirus vaccine formulations |
| JP2023513073A (ja) * | 2020-01-30 | 2023-03-30 | モデルナティエックス インコーポレイテッド | 呼吸器系ウイルス免疫化組成物 |
| US12194089B2 (en) | 2020-02-04 | 2025-01-14 | CureVac SE | Coronavirus vaccine |
| WO2021222639A2 (en) * | 2020-04-29 | 2021-11-04 | The United States Of America, As Represented By The Secretary, Department Of Health And Human Services | Recombinant human metapneumovirus f proteins and their use |
| WO2021243122A2 (en) * | 2020-05-29 | 2021-12-02 | Board Of Regents, The University Of Texas System | Engineered coronavirus spike (s) protein and methods of use thereof |
| CA3170740A1 (en) | 2020-05-29 | 2021-12-02 | Curevac Ag | Nucleic acid based combination vaccines |
| WO2021249009A1 (en) * | 2020-06-10 | 2021-12-16 | Sichuan Clover Biopharmaceuticals, Inc. | Rsv vaccine compositions, methods, and uses thereof |
| JP2022023813A (ja) | 2020-07-27 | 2022-02-08 | ファイザー・インク | 組換え生産されたｒｓｖタンパク質の精製方法における陰イオン交換クロマトグラフィー用洗浄溶液の改良 |
| JP2022023814A (ja) | 2020-07-27 | 2022-02-08 | ファイザー・インク | 組換え生産された三量体型のｒｓｖタンパク質の精製方法 |
| CN112226444B (zh) * | 2020-08-25 | 2022-11-04 | 北京交通大学 | 呼吸道合胞病毒全长融合前融合糖蛋白核苷酸序列、重组腺病毒载体及其应用产品 |
| JP7822149B2 (ja) | 2020-10-02 | 2026-03-02 | ファイザー・インク | Ｒｓｖ ｆタンパク質生産のための細胞培養工程 |
| KR102860080B1 (ko) | 2020-10-09 | 2025-09-15 | 더 보드 오브 리젠츠 오브 더 유니버시티 오브 텍사스 시스템 | 융합전-안정화된 hmpv f 단백질 |
| AU2021367917A1 (en) | 2020-10-28 | 2023-06-22 | Sanofi Pasteur | Liposomes containing tlr4 agonist, preparation and uses thereof |
| CN112592928B (zh) * | 2020-12-31 | 2021-08-31 | 北京鼎成肽源生物技术有限公司 | 冠状病毒的融合基因、融合蛋白、重组载体、通用型dc疫苗及其制备方法 |
| WO2022175477A1 (en) * | 2021-02-19 | 2022-08-25 | Janssen Vaccines & Prevention B.V. | Stabilized pre-fusion rsv fb antigens |
| KR20240024044A (ko) | 2021-04-02 | 2024-02-23 | 유니베르시떼 드 베르사이유 쎙 깡뗑 앙 이브렝 | Al-MOF 포함 보강제 및 항원을 함유하는 면역원성 조성물 |
| US12304929B2 (en) * | 2021-04-12 | 2025-05-20 | Sk Bioscience Co., Ltd. | Recombinant RSV live vaccine strain and the preparing method thereof |
| US20240200099A1 (en) * | 2021-04-15 | 2024-06-20 | Merck Sharp & Dohme Llc | Rotavirus vectors for heterologous gene delivery |
| IL310628A (en) * | 2021-08-10 | 2024-04-01 | Icosavax Inc | Virus-like particle vaccine for respiratory syncytial virus |
| JP2024536236A (ja) * | 2021-09-29 | 2024-10-04 | エスケー バイオサイエンス カンパニー リミテッド | 組み換えられた弱毒化ｒｓｖ生ワクチン及びその製造方法 |
| WO2023091766A2 (en) * | 2021-11-19 | 2023-05-25 | RNAimmune, Inc. | Compositions and methods of ribonucleic acid respiratory syncytial virus (rsv) vaccines |
| KR102785012B1 (ko) * | 2021-12-14 | 2025-03-20 | 경희대학교 산학협력단 | Rsv 항원 단백질을 포함하는 바이러스 유사입자 및 이를 이용한 백신 |
| CN117715923A (zh) * | 2022-04-29 | 2024-03-15 | 北京新合睿恩生物医疗科技有限公司 | Rsv f蛋白突变体及其应用 |
| CN119452088A (zh) * | 2022-05-31 | 2025-02-14 | Vlp治疗日本公司 | 修饰疫苗设计开发 |
| US20260014242A1 (en) * | 2022-06-10 | 2026-01-15 | Glaxosmithkline Biologicals Sa | Rsv vaccination with trimeric rsv f fusion protein |
| WO2024041773A1 (en) * | 2022-08-22 | 2024-02-29 | Glaxosmithkline Biologicals Sa | Rsv-f proteins |
| WO2024069420A2 (en) | 2022-09-29 | 2024-04-04 | Pfizer Inc. | Immunogenic compositions comprising an rsv f protein trimer |
| CN116478296B (zh) * | 2022-10-17 | 2024-02-23 | 厦门大学 | 截短的呼吸道合胞病毒f蛋白及其用途 |
| WO2024089634A1 (en) | 2022-10-27 | 2024-05-02 | Pfizer Inc. | Immunogenic compositions against influenza and rsv |
| IL320459A (en) | 2022-10-27 | 2025-06-01 | Pfizer | Rna molecules encoding rsv-f and vaccines containing them |
| KR20250099727A (ko) * | 2022-11-04 | 2025-07-02 | 사노피 파스퇴르 인크 | 호흡기 세포융합 바이러스 rna 백신접종 |
| WO2024100196A1 (en) * | 2022-11-09 | 2024-05-16 | Nykode Therapeutics ASA | Co-expression of constructs and polypeptides |
| KR102531775B1 (ko) | 2022-11-11 | 2023-05-15 | 대한민국 | Rsv f 항체 또는 이의 항원 결합 단편 |
| CN116284266B (zh) * | 2022-11-21 | 2024-01-19 | 怡道生物科技(苏州)有限公司 | 突变型呼吸道合胞病毒融合前f蛋白及其应用 |
| WO2024115561A1 (en) * | 2022-12-01 | 2024-06-06 | Glaxosmithkline Biologicals Sa | Vaccination against rsv |
| JP2026500218A (ja) | 2022-12-11 | 2026-01-06 | ファイザー・インク | インフルエンザおよびｒｓｖに対する免疫原性組成物 |
| EP4652184A2 (en) * | 2023-01-17 | 2025-11-26 | The Scripps Research Institute | Engineered paramyxovirus soluble fusion (f) proteins and related vaccines |
| US20240252614A1 (en) | 2023-01-18 | 2024-08-01 | Pfizer Inc. | Vaccines against respiratory diseases |
| EP4658305A1 (en) * | 2023-02-03 | 2025-12-10 | Vernagen, LLC | Respiratory syncytial virus mrna vaccine |
| WO2024164020A2 (en) * | 2023-02-03 | 2024-08-08 | The Trustees Of Columbia University In The City Of New York | Methods of inhibiting paramyxoviridae fusion to a target cell |
| KR20250152090A (ko) * | 2023-02-21 | 2025-10-22 | 엠에스디 인터내셔널 비즈니스 게엠베하 | 이종 삼량체화 도메인이 없는 안정화된 삼량체 rsv 융합 단백질 |
| WO2024175040A1 (en) * | 2023-02-22 | 2024-08-29 | Everest Medicines (China) Co., Ltd. | RSV mRNA VACCINES |
| JP2026510670A (ja) * | 2023-03-17 | 2026-04-10 | 成都威斯克生物医▲薬▼有限公司 | 呼吸器合胞体ウイルス感染症に対するワクチン |
| CN116536357A (zh) * | 2023-04-17 | 2023-08-04 | 中国医学科学院输血研究所 | 构建CRISPR/Cas12a中sgRNA剪切活性筛选系统的方法 |
| CN118108812B (zh) * | 2023-05-04 | 2025-04-15 | 国药中生生物技术研究院有限公司 | Rsv f蛋白的突变体 |
| CN118994329A (zh) * | 2023-05-18 | 2024-11-22 | 北京微星生物科技有限公司 | 融合前rsv f蛋白及其应用 |
| CN117050149B (zh) * | 2023-05-19 | 2025-12-12 | 珠海丽凡达生物技术有限公司 | 包含人呼吸道合胞病毒抗原的免疫组合物及其制备方法和应用 |
| KR20260015203A (ko) | 2023-05-19 | 2026-02-02 | 글락소스미스클라인 바이오로지칼즈 에스.에이. | 호흡기 세포융합 바이러스 및 스트렙토코쿠스 뉴모니아에 감염에 대한 면역 반응을 유발하는 방법 |
| WO2024240267A1 (zh) * | 2023-05-25 | 2024-11-28 | 江苏瑞科生物技术股份有限公司 | 一种具有免疫原性的呼吸道合胞病毒(rsv)多肽 |
| CN121464149A (zh) * | 2023-06-07 | 2026-02-03 | 四川三叶草生物制药有限公司 | Rsv疫苗组合物、方法及其用途 |
| WO2024256637A1 (en) * | 2023-06-16 | 2024-12-19 | Glaxosmithkline Biologicals Sa | Cysteine-substituted rsv-f proteins |
| EP4736848A1 (en) | 2023-06-28 | 2026-05-06 | Shanghai Regenelead Therapies Co., Ltd. | Pharmaceutical composition containing cationic lipid and use thereof |
| TW202515531A (zh) | 2023-07-07 | 2025-04-16 | 美商輝瑞股份有限公司 | 兩親性ｔｌｒ７／８佐劑及其用途 |
| CN119431524A (zh) * | 2023-08-07 | 2025-02-14 | 北京新合睿恩生物医疗科技有限公司 | Rsv融合前构象f蛋白的突变体及其应用 |
| WO2025092933A1 (zh) * | 2023-10-31 | 2025-05-08 | 上海蓝鹊生物医药有限公司 | 一种rsv抗原、核酸、重组表达载体、药物组合物及其应用 |
| CN120022355A (zh) * | 2023-11-22 | 2025-05-23 | 长春百克生物科技股份公司 | 一种mRNA疫苗及其应用 |
| CN117304278B (zh) * | 2023-11-28 | 2024-04-16 | 江苏瑞科生物技术股份有限公司 | 一种重组rsv f蛋白及其应用 |
| WO2025126071A1 (en) | 2023-12-14 | 2025-06-19 | Pfizer Inc. | Rna molecules |
| WO2025127857A1 (ko) * | 2023-12-15 | 2025-06-19 | 에스케이바이오사이언스(주) | 변이 rsv 단백질 |
| KR102816014B1 (ko) | 2023-12-20 | 2025-06-02 | 에스케이바이오사이언스(주) | Rsv 의 가용성 f 단백질을 생성하기 위한 재조합 전구체 폴리펩티드 및 이의 이용 |
| CN117586425B (zh) * | 2024-01-19 | 2024-06-14 | 北京安百胜生物科技有限公司 | 一种重组呼吸道合胞病毒颗粒抗原其制备方法和应用 |
| CN117586357B (zh) * | 2024-01-19 | 2024-07-09 | 北京安百胜生物科技有限公司 | 一种具有免疫原性的呼吸道合胞病毒（rsv）多肽 |
| CN117567652B (zh) * | 2024-01-19 | 2024-05-14 | 北京安百胜生物科技有限公司 | 一种重组呼吸道合胞病毒颗粒抗原 |
| CN117586359A (zh) * | 2024-01-19 | 2024-02-23 | 北京安百胜生物科技有限公司 | 一种具有免疫原性的呼吸道合胞病毒（rsv）多肽 |
| CN117645655B (zh) * | 2024-01-26 | 2024-05-24 | 普大生物科技(泰州)有限公司 | 一种肺炎球菌多糖-rsv重组蛋白结合疫苗及其制备方法 |
| WO2025163460A2 (en) | 2024-01-30 | 2025-08-07 | Pfizer Inc. | Vaccines against respiratory diseases |
| WO2025186719A1 (en) | 2024-03-06 | 2025-09-12 | Pfizer Inc. | Immunogenic compositions and uses thereof |
| CN118440937B (zh) * | 2024-04-09 | 2025-02-25 | 嘉译生物医药(杭州)有限公司 | 新型的人合胞病毒RSV B mRNA疫苗 |
| CN118580323B (zh) * | 2024-05-22 | 2025-06-17 | 苏州聚微生物科技有限公司 | Rsv融合前f蛋白的突变体及其制备和应用 |
| CN118406159B (zh) * | 2024-05-22 | 2025-07-08 | 苏州聚微生物科技有限公司 | RSV pre-F截短体及其生产方法和应用 |
| CN118496324B (zh) * | 2024-05-22 | 2025-10-21 | 苏州聚微生物科技有限公司 | RSV pre-F突变体及其生产方法和用途 |
| CN118480560B (zh) * | 2024-07-09 | 2024-11-26 | 北京悦康科创医药科技股份有限公司 | 呼吸道合胞病毒mRNA疫苗及其制备方法和应用 |
| WO2026018181A1 (en) | 2024-07-17 | 2026-01-22 | Pfizer Inc. | Immunogenic compositions and uses thereof |
| WO2026038177A1 (en) | 2024-08-16 | 2026-02-19 | Pfizer Inc. | Immunogenic compositions and uses thereof |
| CN119074910A (zh) * | 2024-08-30 | 2024-12-06 | 中国医学科学院病原生物学研究所 | 以麻疹减毒活疫苗为载体的重组呼吸道合胞病毒疫苗及其制备方法 |
| CN118725053B (zh) * | 2024-09-03 | 2024-12-24 | 北京民海生物科技有限公司 | 呼吸道合胞病毒融合前f蛋白突变体及其应用 |
| CN119176859B (zh) * | 2024-11-26 | 2025-03-14 | 北京成大天和生物科技有限公司 | 呼吸道合胞病毒f蛋白突变体及其应用 |
| CN120248057B (zh) * | 2024-12-26 | 2025-12-02 | 北京华诺泰生物医药科技有限公司 | 一种呼吸道合胞病毒f蛋白突变体及其应用 |
Family Cites Families (109)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US472209A (en) | 1892-04-05 | Vacuum-pan | ||
| US4235871A (en) | 1978-02-24 | 1980-11-25 | Papahadjopoulos Demetrios P | Method of encapsulating biologically active materials in lipid vesicles |
| 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 |
| US4675189A (en) | 1980-11-18 | 1987-06-23 | Syntex (U.S.A.) Inc. | Microencapsulation of water soluble active polypeptides |
| 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 |
| US4722848A (en) | 1982-12-08 | 1988-02-02 | Health Research, Incorporated | Method for immunizing animals with synthetically modified vaccinia virus |
| 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 |
| US4501728A (en) | 1983-01-06 | 1985-02-26 | Technology Unlimited, Inc. | Masking of liposomes from RES recognition |
| JPS60100516A (ja) | 1983-11-04 | 1985-06-04 | Takeda Chem Ind Ltd | 徐放型マイクロカプセルの製造法 |
| US4957735A (en) | 1984-06-12 | 1990-09-18 | The University Of Tennessee Research Corporation | Target-sensitive immunoliposomes- preparation and characterization |
| CA1256638A (en) | 1984-07-06 | 1989-06-27 | Motoaki Tanaka | Polymer and its production |
| US5019369A (en) | 1984-10-22 | 1991-05-28 | Vestar, Inc. | Method of targeting tumors in humans |
| US4683195A (en) | 1986-01-30 | 1987-07-28 | Cetus Corporation | Process for amplifying, detecting, and/or-cloning nucleic acid sequences |
| JP2551756B2 (ja) | 1985-05-07 | 1996-11-06 | 武田薬品工業株式会社 | ポリオキシカルボン酸エステルおよびその製造法 |
| 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 |
| US5091309A (en) | 1986-01-16 | 1992-02-25 | Washington University | Sindbis virus vectors |
| US4877611A (en) | 1986-04-15 | 1989-10-31 | Ribi Immunochem Research Inc. | Vaccine containing tumor antigens and adjuvants |
| US4902505A (en) | 1986-07-30 | 1990-02-20 | Alkermes | Chimeric peptides for neuropeptide delivery through the blood-brain barrier |
| US4837028A (en) | 1986-12-24 | 1989-06-06 | Liposome Technology, Inc. | Liposomes with enhanced circulation time |
| US5057540A (en) | 1987-05-29 | 1991-10-15 | Cambridge Biotech Corporation | Saponin adjuvant |
| CA1331443C (en) | 1987-05-29 | 1994-08-16 | Charlotte A. Kensil | Saponin adjuvant |
| US5726292A (en) | 1987-06-23 | 1998-03-10 | Lowell; George H. | Immuno-potentiating systems for preparation of immunogenic materials |
| US5004697A (en) | 1987-08-17 | 1991-04-02 | Univ. Of Ca | Cationized antibodies for delivery through the blood-brain barrier |
| 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 |
| CA1336955C (en) * | 1988-09-20 | 1995-09-12 | Peter R. Paradiso | Respiratory syncytial virus: vaccines and diagnostic assays |
| US5217879A (en) | 1989-01-12 | 1993-06-08 | Washington University | Infectious Sindbis virus vectors |
| US5055303A (en) | 1989-01-31 | 1991-10-08 | Kv Pharmaceutical Company | Solid controlled release bioadherent emulsions |
| US5703055A (en) | 1989-03-21 | 1997-12-30 | Wisconsin Alumni Research Foundation | Generation of antibodies through lipid mediated DNA delivery |
| US5271961A (en) | 1989-11-06 | 1993-12-21 | Alkermes Controlled Therapeutics, Inc. | Method for producing protein microspheres |
| US5188837A (en) | 1989-11-13 | 1993-02-23 | Nova Pharmaceutical Corporation | Lipsopheres for controlled delivery of substances |
| US5268164A (en) | 1990-04-23 | 1993-12-07 | Alkermes, Inc. | Increasing blood-brain barrier permeability with permeabilizer peptides |
| US5254342A (en) | 1991-09-30 | 1993-10-19 | University Of Southern California | Compositions and methods for enhanced transepithelial and transendothelial transport or active agents |
| US5643578A (en) | 1992-03-23 | 1997-07-01 | University Of Massachusetts Medical Center | Immunization by inoculation of DNA transcription unit |
| DE69311538D1 (de) | 1992-03-12 | 1997-07-17 | Alkermes Inc | Acth enthaltende mikrokugeln mit gesteuerter abgabe |
| US5534496A (en) | 1992-07-07 | 1996-07-09 | University Of Southern California | Methods and compositions to enhance epithelial drug transport |
| EP0671926B1 (en) | 1992-08-11 | 2002-11-13 | President And Fellows Of Harvard College | Immunomodulatory peptides |
| US5593972A (en) | 1993-01-26 | 1997-01-14 | The Wistar Institute | Genetic immunization |
| US5776468A (en) | 1993-03-23 | 1998-07-07 | Smithkline Beecham Biologicals (S.A.) | Vaccine compositions containing 3-0 deacylated monophosphoryl lipid A |
| FR2705686B1 (fr) | 1993-05-28 | 1995-08-18 | Transgene Sa | Nouveaux adénovirus défectifs et lignées de complémentation correspondantes. |
| SK282843B6 (sk) | 1993-07-13 | 2002-12-03 | Rhone-Poulenc Rorer S. A. | Defektný rekombinantný adenovírus a farmaceutický prostriedok s jeho obsahom |
| US5514670A (en) | 1993-08-13 | 1996-05-07 | Pharmos Corporation | Submicron emulsions for delivery of peptides |
| US5961970A (en) | 1993-10-29 | 1999-10-05 | Pharmos Corporation | Submicron emulsions as vaccine adjuvants |
| PL181241B1 (pl) | 1993-11-17 | 2001-06-29 | Deutsche Om Arzneimittel Gmbh | Disacharydy beta(1 6)glukozoaminowe, sposób wytwarzania disacharydu beta(1 6) glukozoaminowego, zawierająca je kompozycja farmaceutyczna i środek immunomodulujący i/lub przeciwnowotworowy oraz szczepionka |
| WO1995016772A1 (en) | 1993-12-14 | 1995-06-22 | Cornell Research Foundation, Inc. | Adenovirus gene expression system |
| WO1995026204A1 (en) | 1994-03-25 | 1995-10-05 | Isis Pharmaceuticals, Inc. | Immune stimulation by phosphorothioate oligonucleotide analogs |
| US5851806A (en) | 1994-06-10 | 1998-12-22 | Genvec, Inc. | Complementary adenoviral systems and cell lines |
| ATE336587T1 (de) | 1994-06-10 | 2006-09-15 | Genvec Inc | Adenoviren-vektor systeme und zelllinien |
| EP1167379A3 (en) | 1994-07-15 | 2004-09-08 | University Of Iowa Research Foundation | Immunomodulatory oligonucleotides |
| AUPM873294A0 (en) | 1994-10-12 | 1994-11-03 | Csl Limited | Saponin preparations and use thereof in iscoms |
| IL116816A (en) | 1995-01-20 | 2003-05-29 | Rhone Poulenc Rorer Sa | Cell for the production of a defective recombinant adenovirus or an adeno-associated virus and the various uses thereof |
| 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 |
| US5837511A (en) | 1995-10-02 | 1998-11-17 | Cornell Research Foundation, Inc. | Non-group C adenoviral vectors |
| US5666153A (en) | 1995-10-03 | 1997-09-09 | Virtual Shopping, Inc. | Retractable teleconferencing apparatus |
| US6020182A (en) | 1996-07-12 | 2000-02-01 | Connaught Laboratories Limited | Subunit respiratory syncytial virus vaccine preparation |
| US5856462A (en) | 1996-09-10 | 1999-01-05 | Hybridon Incorporated | Oligonucleotides having modified CpG dinucleosides |
| US6113918A (en) | 1997-05-08 | 2000-09-05 | Ribi Immunochem Research, Inc. | Aminoalkyl glucosamine phosphate compounds and their use as adjuvants and immunoeffectors |
| US6764840B2 (en) | 1997-05-08 | 2004-07-20 | Corixa Corporation | Aminoalkyl glucosaminide 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 |
| GB9727262D0 (en) | 1997-12-24 | 1998-02-25 | Smithkline Beecham Biolog | Vaccine |
| AU7833298A (en) * | 1998-06-10 | 1999-12-30 | Incyte Pharmaceuticals, Inc. | New human carboxypeptidase inhibitor |
| US6113913A (en) | 1998-06-26 | 2000-09-05 | Genvec, Inc. | Recombinant adenovirus |
| 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 |
| WO2001046127A1 (fr) | 1999-12-22 | 2001-06-28 | Om Pharma | Pseudodipeptides acyles porteurs d'un bras auxiliaire fonctionnalise |
| US6764685B1 (en) | 2000-03-21 | 2004-07-20 | Medimmune Vaccines, Inc. | Recombinant parainfluenza virus expression systems and vaccines |
| ES2252261T3 (es) | 2000-06-28 | 2006-05-16 | Glycofi, Inc. | Metodos para producir glicoproteinas modificadas. |
| US20030232061A1 (en) | 2001-10-18 | 2003-12-18 | Fouchier Ronaldus Adrianus Maria | Recombinant parainfluenza virus expression systems and vaccines comprising heterologous antigens derived from metapneumovirus |
| 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 |
| US7524509B2 (en) | 2001-03-09 | 2009-04-28 | Id Biomedical Corporation Of Quebec | Proteosome-liposaccharide vaccine adjuvant |
| US7157465B2 (en) | 2001-04-17 | 2007-01-02 | Dainippon Simitomo Pharma Co., Ltd. | Adenine derivatives |
| JP2005503797A (ja) | 2001-09-13 | 2005-02-10 | ジェンベク、インコーポレイティッド | アデノウイルスベクター及び関連する系、並びに製造及び使用の方法 |
| WO2003029416A2 (en) | 2001-10-01 | 2003-04-10 | Uab Research Foundation | Recombinant respiratory syncytial viruses with deleted surface glycoprotein genes and uses thereof |
| EP1455700A4 (en) | 2001-11-16 | 2007-02-14 | 3M Innovative Properties Co | METHODS AND COMPOSITIONS RELATED TO MRI COMPOUNDS AND TO TOLL-TYPE RECEPTOR (TLR) PATHWAYS |
| EP1485468A4 (en) | 2002-02-21 | 2007-01-03 | Medimmune Vaccines Inc | RECOMBINANT PARAIN FLUENZAVIRUS EXPRESSION SYSTEMS AND VACCINES WITH ANTIGENS FROM METAPNEUMOVIRUS STEM-RELATED HETEROLOGISTS |
| MXPA05003978A (es) | 2002-10-16 | 2005-06-22 | Scripps Research Inst | Sintesis de glicoproteinas. |
| 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 |
| EP1622574A4 (en) | 2003-04-25 | 2006-10-18 | Medimmune Vaccines Inc | EXPRESSION SYSTEMS OF RECOMBINANT PARAINFLUENZA VIRUSES AND VACCINES COMPRISING HETEROLOGOUS ANTIGENS DERIVED FROM METAPNEUMOVIRUS |
| CN101410519B (zh) | 2003-04-25 | 2013-04-24 | 免疫医疗有限责任公司 | 间质肺病毒株及其在疫苗制剂中以及用作抗原性序列表达载体的用途和繁殖病毒的方法 |
| US8637234B2 (en) | 2004-04-16 | 2014-01-28 | Uab Research Foundation | Molecular scaffolds for HIV-1 epitopes |
| US8647818B2 (en) | 2005-02-18 | 2014-02-11 | UAB Research Foundation, University of Alabama—Birmingham | Molecular scaffolds for HIV-1 immunogens |
| CA2600484A1 (en) | 2005-03-10 | 2006-09-21 | Medimmune Vaccines, Inc. | Metapneumovirus strains and their use in vaccine formulations and as vectors for expression of antigenic sequences and methods for propagating virus |
| US7728106B2 (en) | 2005-07-01 | 2010-06-01 | University Of Maryland Biotechnology Institute | HIV-1 glycopeptides and derivatives; preparation and applications thereof |
| WO2007133855A2 (en) | 2006-03-27 | 2007-11-22 | University Of Maryland Biotechnology Institute | Glycoprotein synthesis and remodeling by enzymatic transglycosylation |
| EP2062180A2 (en) | 2006-08-25 | 2009-05-27 | The Government of the United States of America as Represented by The Department of Health and Human Services | Epitope-protein scaffolds and their use |
| EP1997830A1 (en) | 2007-06-01 | 2008-12-03 | AIMM Therapeutics B.V. | RSV specific binding molecules and means for producing them |
| US20090017517A1 (en) | 2007-07-13 | 2009-01-15 | Medimmune, Llc | Preparation of Negative-Stranded RNA Viruses by Electroporation |
| JP5711972B2 (ja) * | 2007-12-24 | 2015-05-07 | アイディー バイオメディカル コーポレイション オブ ケベック | 組換えｒｓｖ抗原 |
| SI2604695T1 (sl) | 2007-12-27 | 2023-03-31 | Universitaet Zuerich Prorektorat Forschung | Replikacijsko defektni arenavirusni vektorji |
| WO2010075491A2 (en) * | 2008-12-24 | 2010-07-01 | University Of Rochester | Recombinant expression of self-folding neutralizing epitope-bearing subdomains of the respiratory syncytial virus attachment and fusion proteins |
| US8609392B2 (en) | 2009-05-12 | 2013-12-17 | Transgene S.A. | Method for orthopoxvirus production and purification |
| EP2445527A2 (en) * | 2009-06-24 | 2012-05-02 | ID Biomedical Corporation of Quebec | Vaccine |
| HUE028085T2 (en) * | 2009-06-24 | 2016-11-28 | Glaxosmithkline Biologicals Sa | Recombinant RSV antigens |
| CA2768186A1 (en) | 2009-07-15 | 2011-01-20 | Novartis Ag | Rsv f protein compositions and methods for making same |
| US8568726B2 (en) | 2009-10-06 | 2013-10-29 | Medimmune Limited | RSV specific binding molecule |
| EP2486053B1 (en) | 2009-10-06 | 2017-01-18 | Medimmune Limited | Rsv-specific binding molecule |
| US20120315270A1 (en) | 2009-10-21 | 2012-12-13 | The United States Of America, As Represented By The | Rsv immunogens, antibodies and compositions thereof |
| CA2835644C (en) * | 2011-05-13 | 2021-06-15 | Novartis Ag | Pre-fusion rsv f antigens |
| CN102210860B (zh) | 2011-05-31 | 2012-11-21 | 昆明理工大学 | 一种结核分枝杆菌tb10．4-f1融合蛋白疫苗及制备方法 |
| ES2395677B1 (es) * | 2011-07-29 | 2013-12-26 | Instituto De Salud Carlos Iii | Proteína F del VRSH en conformación pre-fusión estabilizada y anticuerpos neutralizantes específicos frente a la misma. |
| AU2013301312A1 (en) | 2012-08-06 | 2015-03-19 | Glaxosmithkline Biologicals S.A. | Method for eliciting in infants an immune response against RSV and B. pertussis |
| EP2922570A1 (en) | 2012-11-20 | 2015-09-30 | GlaxoSmithKline Biologicals SA | Rsv f prefusion trimers |
| 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 |
| EP2970398B1 (en) * | 2013-03-13 | 2024-05-08 | The United States of America, as Represented by The Secretary, Department of Health and Human Services | Prefusion rsv f proteins and their use |
| EP2975052B1 (en) | 2013-03-15 | 2020-09-23 | Xiamen University | Epitope of rsv fusion protein and antibody identifying same |
| KR102236497B1 (ko) | 2013-04-25 | 2021-04-06 | 얀센 백신스 앤드 프리벤션 비.브이. | 안정화된 가용성 예비융합 ｒｓｖ ｆ 폴리펩타이드 |
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