CN114829407A - 利用哺乳动物展示筛选FcγR特异性结合Fc - Google Patents
利用哺乳动物展示筛选FcγR特异性结合Fc Download PDFInfo
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Classifications
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/46—Hybrid immunoglobulins
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N5/00—Undifferentiated human, animal or plant cells, e.g. cell lines; Tissues; Cultivation or maintenance thereof; Culture media therefor
Abstract
公开了将哺乳动物展示与流式分选术、二代测序等技术相结合,筛选与特定FcγR结合能力增强的Fc变体的方法,以及由此筛选获得的Fc变体。
Description
PCT国内申请,说明书已公开。
Claims (21)
- PCT国内申请,权利要求书已公开。
Applications Claiming Priority (3)
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CN201910898731 | 2019-09-23 | ||
PCT/CN2020/116868 WO2021057726A1 (zh) | 2019-09-23 | 2020-09-22 | 利用哺乳动物展示筛选FcγR特异性结合Fc |
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CN114703229A (zh) * | 2022-03-22 | 2022-07-05 | 重庆医科大学 | 一种基于人源细胞的表面展示技术及靶向hbv受体的多肽及其应用 |
Citations (8)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
CN101331223A (zh) * | 2005-10-14 | 2008-12-24 | 米迪缪尼有限公司 | 细胞展示抗体文库 |
US20090215639A1 (en) * | 2005-04-26 | 2009-08-27 | Bioren, Inc. | Method of Producing Human IgG Antibodies with Enhanced Effector Functions |
CN102027009A (zh) * | 2008-03-11 | 2011-04-20 | 健泰科生物技术公司 | 具有增强的adcc功能的抗体 |
CN102666874A (zh) * | 2009-10-07 | 2012-09-12 | 宏观基因有限公司 | 由于岩藻糖基化程度的改变而表现出改善的效应子功能的含Fc区的多肽及其使用方法 |
US20130338017A1 (en) * | 2007-12-21 | 2013-12-19 | Pdl Biopharma, Inc. | Methods of screening complex protein libraries to identify altered properties |
US20140377253A1 (en) * | 2013-03-15 | 2014-12-25 | Abbvie Biotherapeutics Inc. | Fc variants |
CN104736706A (zh) * | 2012-08-24 | 2015-06-24 | 中外制药株式会社 | FcγRIIb特异性Fc区变体 |
CN105163758A (zh) * | 2013-03-15 | 2015-12-16 | 法国血液分割暨生化制品实验室 | 包含富集主要电荷同工型的抗体组合物的新药物 |
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EP2646606B1 (en) * | 2010-12-01 | 2018-10-10 | Merck Sharp&Dohme Corp. | Surface-anchored fc-bait antibody display system |
BR112014013035A2 (pt) * | 2011-12-22 | 2018-10-09 | Hoffmann La Roche | métodos de seleção de células, conjuntos de expressão bicistrônica, células eucarióticas, vetores lentivirais, uso de vetor lentiviral, bibliotecas de ventores lentivirais e de células eucarióticas, métodos de seleção de células, fluxos de trabalho e uso de célula |
FR3024453B1 (fr) * | 2014-08-01 | 2018-06-29 | Lab Francais Du Fractionnement | Procede de production de variants ayant un fc presentant une sialylation amelioree |
ES2749716T3 (es) * | 2014-10-28 | 2020-03-23 | Merck Patent Gmbh | Métodos de despliegue de proteínas que contienen dominios Fc no covalentes sobre la superficie de células y métodos de selección de las mismas |
FR3038517B1 (fr) * | 2015-07-06 | 2020-02-28 | Laboratoire Francais Du Fractionnement Et Des Biotechnologies | Utilisation de fragments fc modifies en immunotherapie |
-
2020
- 2020-09-22 WO PCT/CN2020/116868 patent/WO2021057726A1/zh active Application Filing
- 2020-09-22 CN CN202080066466.5A patent/CN114829407A/zh active Pending
Patent Citations (9)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
US20090215639A1 (en) * | 2005-04-26 | 2009-08-27 | Bioren, Inc. | Method of Producing Human IgG Antibodies with Enhanced Effector Functions |
CN101331223A (zh) * | 2005-10-14 | 2008-12-24 | 米迪缪尼有限公司 | 细胞展示抗体文库 |
US20130338017A1 (en) * | 2007-12-21 | 2013-12-19 | Pdl Biopharma, Inc. | Methods of screening complex protein libraries to identify altered properties |
CN102027009A (zh) * | 2008-03-11 | 2011-04-20 | 健泰科生物技术公司 | 具有增强的adcc功能的抗体 |
CN102666874A (zh) * | 2009-10-07 | 2012-09-12 | 宏观基因有限公司 | 由于岩藻糖基化程度的改变而表现出改善的效应子功能的含Fc区的多肽及其使用方法 |
CN104736706A (zh) * | 2012-08-24 | 2015-06-24 | 中外制药株式会社 | FcγRIIb特异性Fc区变体 |
US20140377253A1 (en) * | 2013-03-15 | 2014-12-25 | Abbvie Biotherapeutics Inc. | Fc variants |
CN105143257A (zh) * | 2013-03-15 | 2015-12-09 | 艾伯维生物医疗股份有限公司 | Fc变体 |
CN105163758A (zh) * | 2013-03-15 | 2015-12-16 | 法国血液分割暨生化制品实验室 | 包含富集主要电荷同工型的抗体组合物的新药物 |
Non-Patent Citations (1)
Title |
---|
PETER SONDERMANN: "Molecular Basis for Immune Complex Recognition: A Comparison of Fc-Receptor Structures", JOURNAL OF MOLECULAR BIOLOGY, vol. 309, no. 3, pages 737 - 749, XP004626899, DOI: 10.1006/jmbi.2001.4670 * |
Cited By (1)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
CN114703229A (zh) * | 2022-03-22 | 2022-07-05 | 重庆医科大学 | 一种基于人源细胞的表面展示技术及靶向hbv受体的多肽及其应用 |
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