CA2382483A1 - Techniques et compositions permettant de construire et d'utiliser des bibliotheques de fusion - Google Patents
Techniques et compositions permettant de construire et d'utiliser des bibliotheques de fusion Download PDFInfo
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Classifications
-
- 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
-
- 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
- C12N15/1075—Isolating an individual clone by screening libraries by coupling phenotype to genotype, not provided for in other groups of this subclass
Landscapes
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Genetics & Genomics (AREA)
- Chemical & Material Sciences (AREA)
- Engineering & Computer Science (AREA)
- Organic Chemistry (AREA)
- Zoology (AREA)
- Wood Science & Technology (AREA)
- Biomedical Technology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Biotechnology (AREA)
- General Engineering & Computer Science (AREA)
- Molecular Biology (AREA)
- Plant Pathology (AREA)
- Biophysics (AREA)
- Microbiology (AREA)
- Physics & Mathematics (AREA)
- Crystallography & Structural Chemistry (AREA)
- Biochemistry (AREA)
- General Health & Medical Sciences (AREA)
- Bioinformatics & Computational Biology (AREA)
- Measuring Or Testing Involving Enzymes Or Micro-Organisms (AREA)
- Peptides Or Proteins (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Enzymes And Modification Thereof (AREA)
Abstract
L'invention concerne des bibliothèques d'acides nucléiques de fusion, chacune comprenant des acides nucléiques codant pour un enzyme de modification d'acide nucléique (NAM), et un acide nucléique codant pour une protéine candidate. L'invention concerne également une bibliothèque de polypeptides de fusion comprenant un enzyme de modification d'acide nucléique (NAM), et une protéine candidate, notamment une bibliothèque de vecteurs d'expression, chaque vecteur comprenant i) un acide nucléique de fusion renfermant un acide nucléique codant pour un enzyme de modification d'acide nucléique (NAM), et un acide nucléique codant pour une protéine candidate, et ii) une séquence de fixation d'enzyme (EAS). Il existe au moins deux protéines candidates différentes. L'enzyme NAM est, de préférence, une protéine Rep, et EAS est, de préférence, plus long que 20 nucléotides. De même, des modes de réalisation préférés utilisent des acides nucléiques de fusion comprenant des acides nucléiques codant pour des structures de présentation, des acides nucléiques codant pour des marqueurs, ou des acides nucléiques codant pour des séquences cibles. L'invention concerne également des bibliothèques de conjugués d'acide nucléique/protéine (NAP), chacun renfermant un polypeptide de fusion comprenant un enzyme NAM et une protéine candidate. Les conjugués NAP comprennent également un vecteur d'expression comprenant un acide nucléique de fusion renfermant un acide nucléique codant pour un enzyme NAM, un acide nucléique codant pour une protéine candidate, et une séquence de fixation d'enzyme (EAS) reconnue par l'enzyme NAM. Les enzymes EAS et NAM sont fixés de manière covalente. L'invention concerne enfin des bibliothèques de cellules hôtes et des procédés de criblage.
Applications Claiming Priority (5)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US15000499P | 1999-08-20 | 1999-08-20 | |
| US60/150,004 | 1999-08-20 | ||
| US20913000P | 2000-06-02 | 2000-06-02 | |
| US60/209,130 | 2000-06-02 | ||
| PCT/US2000/022906 WO2001014539A2 (fr) | 1999-08-20 | 2000-08-18 | Techniques et compositions permettant de construire et d'utiliser des bibliotheques de fusion |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| CA2382483A1 true CA2382483A1 (fr) | 2001-03-01 |
Family
ID=26847232
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CA002382483A Abandoned CA2382483A1 (fr) | 1999-08-20 | 2000-08-18 | Techniques et compositions permettant de construire et d'utiliser des bibliotheques de fusion |
Country Status (7)
| Country | Link |
|---|---|
| EP (1) | EP1212411A2 (fr) |
| JP (1) | JP2003507063A (fr) |
| KR (1) | KR20020059370A (fr) |
| CN (1) | CN1378593A (fr) |
| AU (1) | AU781478B2 (fr) |
| CA (1) | CA2382483A1 (fr) |
| WO (1) | WO2001014539A2 (fr) |
Families Citing this family (53)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| DE69935248T2 (de) | 1998-12-02 | 2007-11-08 | Adnexus Therapeutics, Inc., Waltham | Dna-protein fusionen sowie anwendungen derselben |
| US20030036643A1 (en) * | 2000-09-14 | 2003-02-20 | Jin Cheng He | Methods and compositions for the construction and use of fusion libraries |
| WO2002022826A2 (fr) * | 2000-09-14 | 2002-03-21 | Xencor, Inc. | Methodes et compositions de construction et d'utilisation de bibliotheques de fusion |
| AU2002255451A1 (en) * | 2000-12-14 | 2002-09-04 | Xencor | Procaryotic libraries and uses |
| US20030049647A1 (en) * | 2001-02-22 | 2003-03-13 | Bassil Dahiyat | Use of nucleic acid libraries to create toxicological profiles |
| AU2002251999A1 (en) * | 2001-02-22 | 2002-09-12 | Xencor | Methods and compositions for the construction and use of fusion libraries using computational protein design methods |
| US20020168640A1 (en) * | 2001-02-22 | 2002-11-14 | Min Li | Biochips comprising nucleic acid/protein conjugates |
| NZ532635A (en) | 2001-11-13 | 2007-05-31 | Univ Pennsylvania | A method of identifying unknown adeno-associated virus (AAV) sequences and a kit for the method |
| WO2003100100A1 (fr) * | 2002-05-24 | 2003-12-04 | Somagenics, Inc. | Procedes et compositions de production de bibliotheques dirigees de sequences |
| US20090010920A1 (en) | 2003-03-03 | 2009-01-08 | Xencor, Inc. | Fc Variants Having Decreased Affinity for FcyRIIb |
| US9714282B2 (en) | 2003-09-26 | 2017-07-25 | Xencor, Inc. | Optimized Fc variants and methods for their generation |
| US8883147B2 (en) | 2004-10-21 | 2014-11-11 | Xencor, Inc. | Immunoglobulins insertions, deletions, and substitutions |
| US8399618B2 (en) | 2004-10-21 | 2013-03-19 | Xencor, Inc. | Immunoglobulin insertions, deletions, and substitutions |
| EP1701772A4 (fr) | 2003-11-21 | 2012-03-28 | Univ Johns Hopkins | Motifs de separation biomoleculaire et utilisations |
| WO2005086679A2 (fr) | 2004-03-05 | 2005-09-22 | Medical College Of Ohio | Procedes et compositions pour l'evaluation d'acides nucleiques et d'alleles |
| WO2005106036A2 (fr) | 2004-04-12 | 2005-11-10 | Medical College Of Ohio | Methodes et compositions pour analyser des analytes |
| DK1817340T3 (da) | 2004-11-12 | 2012-08-13 | Xencor Inc | Fc-varianter med ændret binding til fcrn |
| US8367805B2 (en) | 2004-11-12 | 2013-02-05 | Xencor, Inc. | Fc variants with altered binding to FcRn |
| WO2007008943A2 (fr) | 2005-07-08 | 2007-01-18 | Xencor, Inc. | Proteines optimisees qui ciblent la molecule ep-cam |
| WO2007041635A2 (fr) | 2005-10-03 | 2007-04-12 | Xencor, Inc. | Variants de fc dotés de propriétés de liaison aux récepteurs fc optimisées |
| SI3093345T1 (sl) * | 2007-07-26 | 2019-08-30 | Uniqure Ip B.V. | Bakulovirusni vektorji, ki vsebujejo ponavljajoča kodirna zaporedja z različnimi kodonskimi preferencami |
| RU2529951C2 (ru) | 2007-12-26 | 2014-10-10 | Ксенкор, Инк. | ВАРИАНТЫ Fc С ИЗМЕНЕННЫМ СВЯЗЫВАНИЕМ C FcRn |
| US12492253B1 (en) | 2008-02-25 | 2025-12-09 | Xencor, Inc. | Anti-human C5 antibodies |
| US9493578B2 (en) | 2009-09-02 | 2016-11-15 | Xencor, Inc. | Compositions and methods for simultaneous bivalent and monovalent co-engagement of antigens |
| GB2505237A (en) * | 2012-08-24 | 2014-02-26 | Stefan Grimm | Method of screening for therapeutic agents using cell lines including a reference cell line |
| WO2015191508A1 (fr) | 2014-06-09 | 2015-12-17 | Voyager Therapeutics, Inc. | Capsides chimériques |
| SG11201703148TA (en) | 2014-11-05 | 2017-05-30 | Voyager Therapeutics Inc | Aadc polynucleotides for the treatment of parkinson's disease |
| CN119876138A (zh) | 2014-11-14 | 2025-04-25 | 沃雅戈治疗公司 | 调节性多核苷酸 |
| CA3193811A1 (fr) | 2014-11-14 | 2016-05-19 | Voyager Therapeutics, Inc. | Compositions et methodes de traitement de la sclerose laterale amyotrophique (sla) |
| HK1245326A1 (zh) | 2014-12-12 | 2018-08-24 | Voyager Therapeutics, Inc. | 用於生产scaav的组合物和方法 |
| ES2938072T3 (es) * | 2015-05-11 | 2023-04-04 | Illumina Inc | Plataforma para el descubrimiento y análisis de agentes terapéuticos |
| WO2017096162A1 (fr) | 2015-12-02 | 2017-06-08 | Voyager Therapeutics, Inc. | Dosages pour la détection d'anticorps neutralisants de vaa |
| EP3448987A4 (fr) | 2016-04-29 | 2020-05-27 | Voyager Therapeutics, Inc. | Compositions pour le traitement de maladies |
| EP3448874A4 (fr) | 2016-04-29 | 2020-04-22 | Voyager Therapeutics, Inc. | Compositions pour le traitement de maladies |
| CA3024448C (fr) | 2016-05-18 | 2025-09-09 | Voyager Therapeutics, Inc. | Polynucleotides modulateurs |
| CA3024449A1 (fr) | 2016-05-18 | 2017-11-23 | Voyager Therapeutics, Inc. | Compositions et methodes de traitement de la maladie de huntington |
| WO2018044933A1 (fr) | 2016-08-30 | 2018-03-08 | The Regents Of The University Of California | Procédés de ciblage et d'administration biomédicaux, et dispositifs et systèmes pour la mise en œuvre de ceux-ci |
| GB201702938D0 (en) | 2017-02-23 | 2017-04-12 | Univ Southampton | Methods of generating and screening compartmentalised peptides libraries |
| JP2020518259A (ja) | 2017-05-05 | 2020-06-25 | ボイジャー セラピューティクス インコーポレイテッドVoyager Therapeutics,Inc. | ハンチントン病治療組成物および方法 |
| EP3618839A4 (fr) | 2017-05-05 | 2021-06-09 | Voyager Therapeutics, Inc. | Compositions et méthodes de traitement de la sclérose latérale amyotrophique (sla) |
| JOP20190269A1 (ar) | 2017-06-15 | 2019-11-20 | Voyager Therapeutics Inc | بولي نوكليوتيدات aadc لعلاج مرض باركنسون |
| JP7229989B2 (ja) | 2017-07-17 | 2023-02-28 | ボイジャー セラピューティクス インコーポレイテッド | 軌道アレイガイドシステム |
| JP7221275B2 (ja) | 2017-08-03 | 2023-02-13 | ボイジャー セラピューティクス インコーポレイテッド | Aavを送達するための組成物および方法 |
| US20200263199A1 (en) | 2017-09-29 | 2020-08-20 | Voyager Therapeutics, Inc. | Rescue of central and peripheral neurological phenotype of friedreich's ataxia by intravenous delivery |
| TW202413649A (zh) | 2017-10-16 | 2024-04-01 | 美商航海家醫療公司 | 肌萎縮性脊髓側索硬化症(als)之治療 |
| WO2019079242A1 (fr) | 2017-10-16 | 2019-04-25 | Voyager Therapeutics, Inc. | Traitement de la sclérose latérale amyotrophique (sla) |
| SG11202011296VA (en) | 2018-05-15 | 2020-12-30 | Voyager Therapeutics Inc | Compositions and methods for the treatment of parkinson's disease |
| US12281321B2 (en) | 2018-09-28 | 2025-04-22 | Voyager Therapeutics, Inc. | Frataxin expression constructs having engineered promoters and methods of use thereof |
| EP3956467A1 (fr) * | 2019-04-16 | 2022-02-23 | F. Hoffmann-La Roche AG | Dosage cellulaire de criblage de petites molécules utilisant des billes modifiées |
| CN110452303B (zh) * | 2019-08-08 | 2022-03-04 | 中国科学院武汉病毒研究所 | 共价连接核酸和肽或蛋白的方法及应用 |
| JP7765290B2 (ja) * | 2019-12-13 | 2025-11-06 | 中外製薬株式会社 | 細胞外プリン受容体リガンドを検出するシステムおよび当該システムを導入した非ヒト動物 |
| CN111704655A (zh) * | 2020-04-24 | 2020-09-25 | 吉林农业大学 | 一种可以诱导鹅胚成纤维细胞凋亡的鹅细小病毒蛋白及其制备方法 |
| CN120424229B (zh) * | 2025-03-20 | 2026-03-31 | 重庆医科大学附属第二医院 | 一种荧光融合蛋白及其应用 |
Family Cites Families (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US5270170A (en) * | 1991-10-16 | 1993-12-14 | Affymax Technologies N.V. | Peptide library and screening method |
| US5856090A (en) * | 1994-09-09 | 1999-01-05 | The Scripps Research Institute | DNA-methylase linking reaction |
| WO1998023781A1 (fr) * | 1996-11-26 | 1998-06-04 | Johns Hopkins University | Systeme de detection de ligands et procedes d'utilisation associes |
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- 2000-08-18 JP JP2001518853A patent/JP2003507063A/ja active Pending
- 2000-08-18 EP EP00955779A patent/EP1212411A2/fr not_active Withdrawn
- 2000-08-18 WO PCT/US2000/022906 patent/WO2001014539A2/fr not_active Ceased
- 2000-08-18 AU AU67925/00A patent/AU781478B2/en not_active Ceased
- 2000-08-18 CN CN00814124A patent/CN1378593A/zh active Pending
- 2000-08-18 KR KR1020027002204A patent/KR20020059370A/ko not_active Abandoned
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| WO2001014539A3 (fr) | 2001-09-27 |
| KR20020059370A (ko) | 2002-07-12 |
| WO2001014539A2 (fr) | 2001-03-01 |
| AU781478B2 (en) | 2005-05-26 |
| JP2003507063A (ja) | 2003-02-25 |
| CN1378593A (zh) | 2002-11-06 |
| EP1212411A2 (fr) | 2002-06-12 |
| AU6792500A (en) | 2001-03-19 |
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