JP5754135B2 - 関心対象のタンパク質の細胞表面ディスプレイ、スクリーニング、および産生 - Google Patents
関心対象のタンパク質の細胞表面ディスプレイ、スクリーニング、および産生 Download PDFInfo
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Classifications
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- G01N33/00—Investigating or analysing materials by specific methods not covered by groups G01N1/00 - G01N31/00
- G01N33/48—Biological material, e.g. blood, urine; Haemocytometers
- 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
- G01N33/566—Immunoassay; Biospecific binding assay; Materials therefor using specific carrier or receptor proteins as ligand binding reagents where possible specific carrier or receptor proteins are classified with their target compounds
-
- 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
- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
- C12N15/09—Recombinant DNA-technology
- C12N15/10—Processes for the isolation, preparation or purification of DNA or RNA
- C12N15/1034—Isolating an individual clone by screening libraries
- C12N15/1037—Screening libraries presented on the surface of microorganisms, e.g. phage display, E. coli display
-
- C—CHEMISTRY; METALLURGY
- C40—COMBINATORIAL TECHNOLOGY
- C40B—COMBINATORIAL CHEMISTRY; LIBRARIES, e.g. CHEMICAL LIBRARIES
- C40B10/00—Directed molecular evolution of macromolecules, e.g. RNA, DNA or proteins
-
- C—CHEMISTRY; METALLURGY
- C40—COMBINATORIAL TECHNOLOGY
- C40B—COMBINATORIAL CHEMISTRY; LIBRARIES, e.g. CHEMICAL LIBRARIES
- C40B40/00—Libraries per se, e.g. arrays, mixtures
- C40B40/02—Libraries contained in or displayed by microorganisms, e.g. bacteria or animal cells; Libraries contained in or displayed by vectors, e.g. plasmids; Libraries containing only microorganisms or vectors
-
- C—CHEMISTRY; METALLURGY
- C40—COMBINATORIAL TECHNOLOGY
- C40B—COMBINATORIAL CHEMISTRY; LIBRARIES, e.g. CHEMICAL LIBRARIES
- C40B40/00—Libraries per se, e.g. arrays, mixtures
- C40B40/04—Libraries containing only organic compounds
- C40B40/06—Libraries containing nucleotides or polynucleotides, or derivatives thereof
- C40B40/08—Libraries containing RNA or DNA which encodes proteins, e.g. gene libraries
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/01—Fusion polypeptide containing a localisation/targetting motif
- C07K2319/035—Fusion polypeptide containing a localisation/targetting motif containing a signal for targeting to the external surface of a cell, e.g. to the outer membrane of Gram negative bacteria, GPI- anchored eukaryote proteins
-
- C—CHEMISTRY; METALLURGY
- C40—COMBINATORIAL TECHNOLOGY
- C40B—COMBINATORIAL CHEMISTRY; LIBRARIES, e.g. CHEMICAL LIBRARIES
- C40B30/00—Methods of screening libraries
- C40B30/04—Methods of screening libraries by measuring the ability to specifically bind a target molecule, e.g. antibody-antigen binding, receptor-ligand binding
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N2333/00—Assays involving biological materials from specific organisms or of a specific nature
- G01N2333/435—Assays involving biological materials from specific organisms or of a specific nature from animals; from humans
- G01N2333/705—Assays involving receptors, cell surface antigens or cell surface determinants
Landscapes
- Life Sciences & Earth Sciences (AREA)
- Health & Medical Sciences (AREA)
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- Organic Chemistry (AREA)
- Molecular Biology (AREA)
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- Biochemistry (AREA)
- Genetics & Genomics (AREA)
- Medicinal Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Biomedical Technology (AREA)
- General Chemical & Material Sciences (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Microbiology (AREA)
- Biotechnology (AREA)
- General Engineering & Computer Science (AREA)
- Zoology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Wood Science & Technology (AREA)
- Immunology (AREA)
- Physics & Mathematics (AREA)
- Urology & Nephrology (AREA)
- Hematology (AREA)
- Virology (AREA)
- Crystallography & Structural Chemistry (AREA)
- Biophysics (AREA)
- Plant Pathology (AREA)
- General Physics & Mathematics (AREA)
- Food Science & Technology (AREA)
- Analytical Chemistry (AREA)
- Cell Biology (AREA)
- Pathology (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Measuring Or Testing Involving Enzymes Or Micro-Organisms (AREA)
- Peptides Or Proteins (AREA)
- Enzymes And Modification Thereof (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
Applications Claiming Priority (9)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US92037507P | 2007-03-26 | 2007-03-26 | |
| US92037807P | 2007-03-26 | 2007-03-26 | |
| US60/920,375 | 2007-03-26 | ||
| US60/920,378 | 2007-03-26 | ||
| US95971907P | 2007-07-16 | 2007-07-16 | |
| US60/959,719 | 2007-07-16 | ||
| US484107P | 2007-12-01 | 2007-12-01 | |
| US61/004,841 | 2007-12-01 | ||
| PCT/US2008/003978 WO2008118476A2 (en) | 2007-03-26 | 2008-03-26 | Cell surface display, screening and production of proteins of interest |
Related Child Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP2013170132A Division JP2013233157A (ja) | 2007-03-26 | 2013-08-20 | 関心対象のタンパク質の細胞表面ディスプレイ、スクリーニング、および産生 |
Publications (3)
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| JP2010522561A JP2010522561A (ja) | 2010-07-08 |
| JP2010522561A5 JP2010522561A5 (https=) | 2012-05-10 |
| JP5754135B2 true JP5754135B2 (ja) | 2015-07-29 |
Family
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| JP2010500980A Expired - Fee Related JP5754135B2 (ja) | 2007-03-26 | 2008-03-26 | 関心対象のタンパク質の細胞表面ディスプレイ、スクリーニング、および産生 |
| JP2013170132A Withdrawn JP2013233157A (ja) | 2007-03-26 | 2013-08-20 | 関心対象のタンパク質の細胞表面ディスプレイ、スクリーニング、および産生 |
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| JP2013170132A Withdrawn JP2013233157A (ja) | 2007-03-26 | 2013-08-20 | 関心対象のタンパク質の細胞表面ディスプレイ、スクリーニング、および産生 |
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| Country | Link |
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| US (4) | US8709980B2 (https=) |
| EP (2) | EP2617827A1 (https=) |
| JP (2) | JP5754135B2 (https=) |
| WO (1) | WO2008118476A2 (https=) |
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| WO2008118476A2 (en) | 2007-03-26 | 2008-10-02 | Codon Devices, Inc. | Cell surface display, screening and production of proteins of interest |
| ES2475973T3 (es) * | 2008-06-27 | 2014-07-11 | Sapphire Energy, Inc. | Inducción de la floculaci�n en organismos fotosint�ticos |
| US8067339B2 (en) | 2008-07-09 | 2011-11-29 | Merck Sharp & Dohme Corp. | Surface display of whole antibodies in eukaryotes |
| US20110275535A1 (en) † | 2008-12-16 | 2011-11-10 | Novartis Ag | Yeast Display Systems |
| WO2010129485A2 (en) * | 2009-05-04 | 2010-11-11 | San Diego State University Foundation | Compositions and methods for identifying enzyme and transport protein inhibitors |
| WO2010129541A1 (en) * | 2009-05-04 | 2010-11-11 | Affomix Corporation | Emulsion selection of antibodies |
| ES2652340T3 (es) * | 2009-07-17 | 2018-02-01 | Bioatla Llc | Selección y evolución simultáneas e integradas de rendimiento y expresión de proteínas humanas en huéspedes de producción |
| SG181862A1 (en) | 2009-12-23 | 2012-07-30 | Affinity Biosciences Pty Ltd | Protein display |
| US9169312B2 (en) | 2010-09-21 | 2015-10-27 | San Diego State University Research Foundation | Compositions and methods for identifying enzyme and transport protein inhibitors |
| IL210093A0 (en) * | 2010-12-19 | 2011-06-30 | David Helman | Membrane bound reporter molecules and their use in cell sorting |
| DE102010056289A1 (de) | 2010-12-24 | 2012-06-28 | Geneart Ag | Verfahren zur Herstellung von Leseraster-korrekten Fragment-Bibliotheken |
| WO2013000023A1 (en) | 2011-06-29 | 2013-01-03 | Affinity Biosciences Pty Ltd | Method of protein display |
| EP2739733B1 (en) * | 2011-08-03 | 2017-11-22 | Texas Biomedical Research Insitute | Nucleic acid compositions, methods and kits for rapid pairing of affinity agents |
| EP2758565A4 (en) * | 2011-09-23 | 2015-03-04 | Merck Sharp & Dohme | Cell surface imaging of ligands for insulin and / or insulin growth factor 1 receptor and applications thereof |
| RU2746407C1 (ru) | 2012-02-23 | 2021-04-13 | Стейдж Селл Терапеутикс Гмбх | Хроматографическое выделение клеток и других сложных биологических материалов |
| US20150322479A1 (en) * | 2012-06-20 | 2015-11-12 | Cytospan Technologies Corporation | Apparatus and method for quantification of replicative lifespan and observation of senescene |
| EP3008094B1 (en) * | 2013-06-14 | 2018-12-26 | Pacific Biosciences Of California, Inc. | Bis-biotinylation tags |
| US10544449B2 (en) | 2013-06-14 | 2020-01-28 | Pacific Biosciences Of California, Inc. | Bis-biotinylation tags |
| EP3057989A1 (en) | 2013-10-17 | 2016-08-24 | ARSANIS Biosciences GmbH | Cross-reactive staphylococcus aureus antibody sequences |
| US10421958B2 (en) | 2014-02-05 | 2019-09-24 | Molecular Templates, Inc. | Methods of screening, selecting, and identifying cytotoxic recombinant polypeptides based on an interim diminution of ribotoxicity |
| BR112016024072B1 (pt) * | 2014-04-16 | 2021-02-09 | Juno Therapeutics Gmbh | método in vitro de estimular uma população de células |
| GB201410262D0 (en) * | 2014-06-10 | 2014-07-23 | Cambridge Entpr Ltd | Novel method |
| TWI695011B (zh) | 2014-06-18 | 2020-06-01 | 美商梅爾莎納醫療公司 | 抗ｈｅｒ２表位之單株抗體及其使用之方法 |
| AU2015341081A1 (en) | 2014-10-28 | 2017-06-08 | Merck Patent Gmbh | Methods for non-covalent Fc-domain-containing protein display on the surface of cells and methods of screening thereof |
| MX2017012775A (es) | 2015-04-17 | 2019-04-29 | Arsanis Biosciences Gmbh | Preparacion combinatoria de anticuerpos anti-staphylococcus aureus. |
| SG11201803330WA (en) | 2015-10-22 | 2018-05-30 | Juno Therapeutics Gmbh | Methods for culturing cells and kits and apparatus for same |
| JP7194020B2 (ja) | 2015-10-22 | 2022-12-21 | ジュノ セラピューティクス ゲーエムベーハー | 細胞の培養方法ならびにそのためのキットおよび装置 |
| US11248238B2 (en) | 2015-10-22 | 2022-02-15 | Juno Therapeutics Gmbh | Methods, kits, agents and apparatuses for transduction |
| ES2902682T3 (es) * | 2015-10-26 | 2022-03-29 | Buckman Laboratories Int Inc | Sondas de polímero de lignocelulosa y métodos |
| CN109310885B (zh) | 2016-03-15 | 2022-05-31 | 梅尔莎纳医疗公司 | NaPi2b靶向抗体-药物缀合物及其使用方法 |
| WO2018041740A1 (en) | 2016-09-01 | 2018-03-08 | Bayer Pharma Aktiengesellschaft | Non-covalent display system using fimgt/dsf |
| GB201704115D0 (en) * | 2017-03-15 | 2017-04-26 | Oxford Genetics Ltd | Method of selecting for antibodies |
| JP7339160B2 (ja) | 2017-04-27 | 2023-09-05 | ジュノ セラピューティクス ゲーエムベーハー | オリゴマー粒子試薬およびその使用方法 |
| WO2018213242A1 (en) * | 2017-05-15 | 2018-11-22 | University Of Maryland, Baltimore | Live salmonella typhi vectors engineered to express heterologous outer membrane protein antigens and methods of use thereof |
| CN113474450A (zh) | 2018-08-09 | 2021-10-01 | 朱诺治疗学股份有限公司 | 产生工程化细胞的方法以及所述工程化细胞的组合物 |
| EP3874024A1 (en) | 2018-10-31 | 2021-09-08 | Juno Therapeutics GmbH | Methods for selection and stimulation of cells and apparatus for same |
| WO2022190733A1 (ja) * | 2021-03-10 | 2022-09-15 | ソニーグループ株式会社 | 生体粒子分析方法及び生体粒子分析用試薬キット |
| WO2023051972A1 (en) | 2021-09-29 | 2023-04-06 | Miltenyi Biotec B.V. & Co. KG | Method for the generation and selection of a producer cell |
Family Cites Families (40)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US5223409A (en) | 1988-09-02 | 1993-06-29 | Protein Engineering Corp. | Directed evolution of novel binding proteins |
| US5252466A (en) | 1989-05-19 | 1993-10-12 | Biotechnology Research And Development Corporation | Fusion proteins having a site for in vivo post-translation modification and methods of making and purifying them |
| US5747334A (en) | 1990-02-15 | 1998-05-05 | The University Of North Carolina At Chapel Hill | Random peptide library |
| AU8740491A (en) | 1990-09-28 | 1992-04-28 | Protein Engineering Corporation | Proteinaceous anti-dental plaque agents |
| US20030036092A1 (en) | 1991-11-15 | 2003-02-20 | Board Of Regents, The University Of Texas System | Directed evolution of enzymes and antibodies |
| US5348867A (en) | 1991-11-15 | 1994-09-20 | George Georgiou | Expression of proteins on bacterial surface |
| US5866344A (en) | 1991-11-15 | 1999-02-02 | Board Of Regents, The University Of Texas System | Antibody selection methods using cell surface expressed libraries |
| RU95105899A (ru) | 1992-07-08 | 1997-03-20 | Унилевер Н.В. (NL) | Способ иммобилизации фермента, полинуклеотид, вектор, химерный блок, низшие эукариоты, способ осуществления ферментативного процесса |
| KR100306635B1 (ko) | 1992-10-21 | 2001-11-30 | 스테판밀테니 | 분비생성물에의한직접적인세포선별 |
| US7166423B1 (en) | 1992-10-21 | 2007-01-23 | Miltenyi Biotec Gmbh | Direct selection of cells by secretion product |
| EP0682710B1 (en) | 1993-02-10 | 2003-10-29 | Unilever Plc | Isolation process using immobilized proteins with specific binding capacities |
| DE69434520T3 (de) | 1993-07-30 | 2009-10-15 | Affymax, Inc., Palo Alto | Biotinylierung von proteinen |
| US6696251B1 (en) | 1996-05-31 | 2004-02-24 | Board Of Trustees Of The University Of Illinois | Yeast cell surface display of proteins and uses thereof |
| US6300065B1 (en) | 1996-05-31 | 2001-10-09 | Board Of Trustees Of The University Of Illinois | Yeast cell surface display of proteins and uses thereof |
| US6699658B1 (en) | 1996-05-31 | 2004-03-02 | Board Of Trustees Of The University Of Illinois | Yeast cell surface display of proteins and uses thereof |
| EP0934526B1 (en) | 1996-10-08 | 2003-01-08 | U-BISys B.V. | Methods and means for selecting peptides and proteins having specific affinity for a target |
| US6057098A (en) | 1997-04-04 | 2000-05-02 | Biosite Diagnostics, Inc. | Polyvalent display libraries |
| EP0985033A4 (en) | 1997-04-04 | 2005-07-13 | Biosite Inc | POLYVALENT AND POLYCLONAL LIBRARIES |
| US6555310B1 (en) | 1997-04-04 | 2003-04-29 | Biosite Diagnostics, Inc. | Polyclonal libraries |
| US6759243B2 (en) | 1998-01-20 | 2004-07-06 | Board Of Trustees Of The University Of Illinois | High affinity TCR proteins and methods |
| US6255075B1 (en) | 1998-10-20 | 2001-07-03 | Smithkline Beecham Corporation | Bira |
| US7223533B2 (en) | 1999-09-10 | 2007-05-29 | Cadus Technologies, Inc. | Cell surface proteins and use thereof as indicators of activation of cellular signal transduction pathways |
| US6686168B1 (en) | 1999-11-04 | 2004-02-03 | Zymogenetics, Inc. | Cell surface display of proteins by recombinant host cells |
| GB2383045A (en) | 2000-07-26 | 2003-06-18 | Korea Res Inst Of Bioscience | Novel cell wall anchor proteins derived from yeast, genes thereof and cell surface expression systems using the same |
| US20020142355A1 (en) | 2000-11-14 | 2002-10-03 | Baylor College Of Medicine | Methods for the in vivo biotin labeling of polypeptides |
| EP1340088B1 (en) | 2000-11-17 | 2007-01-17 | University Of Rochester | In vitro methods of producing and identifying immunoglobulin molecules in eukaryotic cells |
| WO2002057423A2 (en) | 2001-01-16 | 2002-07-25 | Regeneron Pharmaceuticals, Inc. | Isolating cells expressing secreted proteins |
| DK1380592T3 (da) | 2001-04-19 | 2009-01-26 | Kansai Chem Eng | Celleoverfladelagsbindende protein og anvendelse heraf |
| GB0118337D0 (en) | 2001-07-27 | 2001-09-19 | Lonza Biologics Plc | Method for selecting antibody expressing cells |
| DK1438400T3 (da) | 2001-10-01 | 2009-10-05 | Dyax Corp | Flerkædede eukaryote display-vektorer og anvendelser deraf |
| GB0202018D0 (en) | 2002-01-29 | 2002-03-13 | Sense Proteomic Ltd | Tag and method |
| EP1367125A1 (en) | 2002-05-30 | 2003-12-03 | Centre National De La Recherche Scientifique (Cnrs) | Vectors for expression of biotinylated proteins in mammalian cells, and their use for identification of protein-nucleic acid interactions in vivo |
| US20040132133A1 (en) | 2002-07-08 | 2004-07-08 | Invitrogen Corporation | Methods and compositions for the production, identification and purification of fusion proteins |
| US20040033603A1 (en) | 2002-08-19 | 2004-02-19 | Lin Zhang | Biotinylation of proteins |
| FI20031663A0 (fi) | 2003-11-14 | 2003-11-14 | Jyvaeskylaen Yliopisto | Avidiinin mutantteja |
| US7795411B2 (en) | 2006-10-05 | 2010-09-14 | Fred Hutchinson Cancer Research Center | Vectors for expressing in vivo biotinylated recombinant proteins |
| JP5571955B2 (ja) | 2006-10-13 | 2014-08-13 | アーチャー−ダニエルズ−ミッドランド カンパニー | 酵母細胞触媒支持体における細胞表面ディスプレイの使用 |
| WO2008067547A2 (en) | 2006-11-30 | 2008-06-05 | Research Development Foundation | Improved immunoglobulin libraries |
| WO2008118476A2 (en) | 2007-03-26 | 2008-10-02 | Codon Devices, Inc. | Cell surface display, screening and production of proteins of interest |
| US8043830B2 (en) | 2008-02-01 | 2011-10-25 | The Regents Of The University Of California | Biotin-ligase system for secretion of biotinylated protein |
-
2008
- 2008-03-26 WO PCT/US2008/003978 patent/WO2008118476A2/en not_active Ceased
- 2008-03-26 EP EP12154795.4A patent/EP2617827A1/en not_active Withdrawn
- 2008-03-26 JP JP2010500980A patent/JP5754135B2/ja not_active Expired - Fee Related
- 2008-03-26 US US12/056,264 patent/US8709980B2/en not_active Expired - Fee Related
- 2008-03-26 EP EP08727167.2A patent/EP2137308B1/en not_active Not-in-force
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2009
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2013
- 2013-08-20 JP JP2013170132A patent/JP2013233157A/ja not_active Withdrawn
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2014
- 2014-03-26 US US14/226,114 patent/US9645146B2/en not_active Expired - Fee Related
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2017
- 2017-03-28 US US15/471,604 patent/US20170261506A1/en not_active Abandoned
Also Published As
| Publication number | Publication date |
|---|---|
| EP2617827A1 (en) | 2013-07-24 |
| US20170261506A1 (en) | 2017-09-14 |
| EP2137308B1 (en) | 2016-08-03 |
| WO2008118476A2 (en) | 2008-10-02 |
| US20100267057A1 (en) | 2010-10-21 |
| US8722586B2 (en) | 2014-05-13 |
| US9645146B2 (en) | 2017-05-09 |
| JP2013233157A (ja) | 2013-11-21 |
| US20090005264A1 (en) | 2009-01-01 |
| WO2008118476A3 (en) | 2008-11-13 |
| JP2010522561A (ja) | 2010-07-08 |
| EP2137308A2 (en) | 2009-12-30 |
| US20140357508A1 (en) | 2014-12-04 |
| US8709980B2 (en) | 2014-04-29 |
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