RU2270865C2 - Иммуногенный полипептид, вызывающий защитный иммунный ответ против bacillus anthracis (варианты), способ его получения, нуклеиновая кислота, кодирующая его, вектор для экспрессии (варианты), способ и вакцина для предупреждения инфекции, вызванной bacillus anthracis - Google Patents
Иммуногенный полипептид, вызывающий защитный иммунный ответ против bacillus anthracis (варианты), способ его получения, нуклеиновая кислота, кодирующая его, вектор для экспрессии (варианты), способ и вакцина для предупреждения инфекции, вызванной bacillus anthracis Download PDFInfo
- Publication number
- RU2270865C2 RU2270865C2 RU2003103779/13A RU2003103779A RU2270865C2 RU 2270865 C2 RU2270865 C2 RU 2270865C2 RU 2003103779/13 A RU2003103779/13 A RU 2003103779/13A RU 2003103779 A RU2003103779 A RU 2003103779A RU 2270865 C2 RU2270865 C2 RU 2270865C2
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- Russia
- Prior art keywords
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- immunogenic polypeptide
- nucleic acid
- anthracis
- variants
- Prior art date
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Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/195—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria
- C07K14/32—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria from Bacillus (G)
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P31/00—Antiinfectives, i.e. antibiotics, antiseptics, chemotherapeutics
- A61P31/04—Antibacterial agents
-
- 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
- C12N15/63—Introduction of foreign genetic material using vectors; Vectors; Use of hosts therefor; Regulation of expression
- C12N15/70—Vectors or expression systems specially adapted for E. coli
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- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K39/00—Medicinal preparations containing antigens or antibodies
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
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- Biotechnology (AREA)
- Biomedical Technology (AREA)
- Gastroenterology & Hepatology (AREA)
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- Veterinary Medicine (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Peptides Or Proteins (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| GB0016702.3 | 2000-07-08 | ||
| GBGB0016702.3A GB0016702D0 (en) | 2000-07-08 | 2000-07-08 | Expression system |
Related Child Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| RU2004134341/13A Division RU2385348C2 (ru) | 2000-07-08 | 2001-07-06 | Экспрессирующая система |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| RU2003103779A RU2003103779A (ru) | 2004-08-20 |
| RU2270865C2 true RU2270865C2 (ru) | 2006-02-27 |
Family
ID=9895205
Family Applications (2)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| RU2003103779/13A RU2270865C2 (ru) | 2000-07-08 | 2001-07-06 | Иммуногенный полипептид, вызывающий защитный иммунный ответ против bacillus anthracis (варианты), способ его получения, нуклеиновая кислота, кодирующая его, вектор для экспрессии (варианты), способ и вакцина для предупреждения инфекции, вызванной bacillus anthracis |
| RU2004134341/13A RU2385348C2 (ru) | 2000-07-08 | 2001-07-06 | Экспрессирующая система |
Family Applications After (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| RU2004134341/13A RU2385348C2 (ru) | 2000-07-08 | 2001-07-06 | Экспрессирующая система |
Country Status (10)
| Country | Link |
|---|---|
| US (3) | US7537771B2 (https=) |
| EP (2) | EP1301606A1 (https=) |
| JP (2) | JP2004502460A (https=) |
| CN (2) | CN101012458A (https=) |
| AU (1) | AU2007201553B8 (https=) |
| CA (2) | CA2413045C (https=) |
| GB (1) | GB0016702D0 (https=) |
| RU (2) | RU2270865C2 (https=) |
| WO (1) | WO2002004646A1 (https=) |
| ZA (1) | ZA200210206B (https=) |
Cited By (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| RU2633508C1 (ru) * | 2016-12-27 | 2017-10-12 | Федеральное государственное учреждение "Федеральный исследовательский центр "Фундаментальные основы биотехнологии" Российской академии наук (ФИЦ Биотехнологии РАН) | Штамм E. coli - продуцент изолированного домена 1 протективного антигена Bacillus anthracis в форме вирусоподобных частиц |
| RU2633504C1 (ru) * | 2016-12-27 | 2017-10-12 | Федеральное государственное учреждение "Федеральный исследовательский центр "Фундаментальные основы биотехнологии" Российской академии наук (ФИЦ Биотехнологии РАН) | Штамм E.coli - продуцент полноразмерного протективного антигена Bacillus anthracis в форме вирусоподобных частиц |
| RU2821917C1 (ru) * | 2023-03-07 | 2024-06-27 | Федеральное государственное бюджетное образовательное учреждение высшего образования "Московский государственный университет имени М.В.Ломоносова" (МГУ) | Рекомбинантная вакцина против сибирской язвы на основе вирусов растений |
Families Citing this family (29)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| GB0016702D0 (en) | 2000-07-08 | 2000-08-23 | Secr Defence Brit | Expression system |
| US7601351B1 (en) | 2002-06-26 | 2009-10-13 | Human Genome Sciences, Inc. | Antibodies against protective antigen |
| EP1575505A4 (en) * | 2002-09-10 | 2007-01-24 | Vical Inc | CODON OPTIMIZATION-BASED POLYNUCLEOTIDE VACCINES AGAINST BACILLUS ANTHRACIS INFECTION |
| US9453251B2 (en) | 2002-10-08 | 2016-09-27 | Pfenex Inc. | Expression of mammalian proteins in Pseudomonas fluorescens |
| EP1572977B1 (en) | 2002-11-15 | 2010-03-03 | Gen-Probe Incorporated | Assay and compositions for detection of bacillus anthracis nucleic acid |
| EP1670505B1 (en) | 2003-09-18 | 2012-11-14 | GOVERNMENT OF THE UNITED STATES OF AMERICA, as represented by THE SECRETARY, DEPARTMENT OF HEALTH AND HUMAN SERVICES | Dna promoters and anthrax vaccines |
| FR2860005A1 (fr) * | 2003-09-23 | 2005-03-25 | Univ Aix Marseille Ii | Methode de detection d'agents bacteriens ou viraux de bioterrorisme |
| WO2005030991A1 (fr) * | 2003-09-23 | 2005-04-07 | Universite De La Mediterranee (Aix-Marseille Ii) | Methode de detection d’agents bacteriens ou viraux de bioterrorisme |
| GB0401036D0 (en) * | 2004-01-17 | 2004-02-18 | Royal Holloway University Of L | Improvements in or relating to vaccination |
| US8101735B2 (en) | 2004-06-16 | 2012-01-24 | Health Protection Agency | Preparation of protective antigen |
| US7355027B2 (en) * | 2004-06-16 | 2008-04-08 | Dynport Vaccine Company Llc | Bacillus anthracis protective antigen |
| US8603824B2 (en) | 2004-07-26 | 2013-12-10 | Pfenex, Inc. | Process for improved protein expression by strain engineering |
| CN100336908C (zh) * | 2004-09-10 | 2007-09-12 | 中国人民解放军军事医学科学院微生物流行病研究所 | 一种制备重组炭疽保护性抗原的方法及其专用表达质粒 |
| WO2006068647A1 (en) * | 2004-12-20 | 2006-06-29 | United States Army Medical Research And Materiel Command | Internal positive control for probe-based nucleic acid molecule assays and methods of making and using thereof |
| GB0504940D0 (en) * | 2005-03-10 | 2005-04-20 | Secr Defence | Vaccine formulation |
| EP1954307A4 (en) | 2005-11-14 | 2009-12-02 | Univ Maryland Biotech Inst | ORAL VACCINES AGAINST MILZBRAND ON SALMONELLA BASE |
| GB0525213D0 (en) * | 2005-12-12 | 2006-01-18 | Secr Defence | Vaccine |
| US20070202117A1 (en) * | 2005-12-22 | 2007-08-30 | Herman Groen | Compositions and Methods Of Modulating the Immune Response |
| GB0607462D0 (en) | 2006-04-13 | 2006-05-24 | Avecia Ltd | Assay |
| JP2008231063A (ja) * | 2007-03-22 | 2008-10-02 | Takano Foods Kk | 納豆菌ワクチン |
| JP5444553B2 (ja) | 2007-04-27 | 2014-03-19 | フェネックス インコーポレイテッド | 微生物宿主を迅速にスクリーニングして、異種タンパク質発現の収率および／または質が改善されている特定の株を同定する方法 |
| US9580719B2 (en) | 2007-04-27 | 2017-02-28 | Pfenex, Inc. | Method for rapidly screening microbial hosts to identify certain strains with improved yield and/or quality in the expression of heterologous proteins |
| AU2009299615B2 (en) | 2008-10-02 | 2015-07-16 | Pharmathene Inc. | Anthrax vaccine formulation and uses thereof |
| WO2010080188A2 (en) * | 2008-10-14 | 2010-07-15 | The Regents Of The University Of Michigan | Epitope targeted anthrax vaccine |
| US20100183675A1 (en) * | 2009-01-22 | 2010-07-22 | Allan Watkinson | Stable vaccine compositions and methods of use |
| US8187611B2 (en) * | 2009-10-29 | 2012-05-29 | Albert Einstein College Of Medicine Of Yeshiva University | Anti-peptide antibodies that cross react with protective antigen of Bacillus anthracis and uses thereof |
| US20110110968A1 (en) * | 2009-11-12 | 2011-05-12 | Stanley Goldman | Human optimized Bacillus anthracis protective antigen |
| CN101798565B (zh) * | 2010-02-26 | 2013-08-07 | 中国人民解放军军事医学科学院生物工程研究所 | 能在芽孢表面展示pa20蛋白的炭疽芽孢杆菌及其应用 |
| WO2020116686A1 (ko) * | 2018-12-06 | 2020-06-11 | 고려대학교 산학협력단 | 인간 항-antxr 키메라 항원 수용체 및 이의 용도 |
Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US5677274A (en) * | 1993-02-12 | 1997-10-14 | The Government Of The United States As Represented By The Secretary Of The Department Of Health And Human Services | Anthrax toxin fusion proteins and related methods |
| RU2115433C1 (ru) * | 1992-08-28 | 1998-07-20 | Научно-исследовательский институт микробиологии МО РФ | Вакцина сибиреязвенная комбинированная |
Family Cites Families (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| RU2110575C1 (ru) * | 1995-07-19 | 1998-05-10 | Государственное Федеральное предприятие Государственный научный центр прикладной микробиологии | Рекомбинантная плазмидная днк pro pf 5, определяющая синтез капсульного антигена fi возбудителя чумы и протективного антигена возбудителя сибирской язвы, и способ конструирования рекомбинантной плазмидной днк pro pf5 |
| DE69940157D1 (en) * | 1998-07-10 | 2009-02-05 | U S Medical Res Inst Of Infect | Anthrax-impfstoff |
| GB0016702D0 (en) | 2000-07-08 | 2000-08-23 | Secr Defence Brit | Expression system |
-
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- 2000-07-08 GB GBGB0016702.3A patent/GB0016702D0/en not_active Ceased
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- 2001-07-06 US US10/332,282 patent/US7537771B2/en not_active Expired - Fee Related
- 2001-07-06 EP EP01947659A patent/EP1301606A1/en not_active Withdrawn
- 2001-07-06 CA CA2413045A patent/CA2413045C/en not_active Expired - Lifetime
- 2001-07-06 CA CA002658217A patent/CA2658217A1/en not_active Abandoned
- 2001-07-06 JP JP2002509500A patent/JP2004502460A/ja active Pending
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- 2001-07-06 EP EP07005671.8A patent/EP1808489B1/en not_active Expired - Lifetime
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- 2007-04-05 AU AU2007201553A patent/AU2007201553B8/en not_active Ceased
-
2011
- 2011-08-22 JP JP2011180293A patent/JP2012010706A/ja active Pending
-
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- 2012-09-26 US US13/627,071 patent/US9346860B2/en not_active Expired - Fee Related
Patent Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| RU2115433C1 (ru) * | 1992-08-28 | 1998-07-20 | Научно-исследовательский институт микробиологии МО РФ | Вакцина сибиреязвенная комбинированная |
| US5677274A (en) * | 1993-02-12 | 1997-10-14 | The Government Of The United States As Represented By The Secretary Of The Department Of Health And Human Services | Anthrax toxin fusion proteins and related methods |
Non-Patent Citations (1)
| Title |
|---|
| BROSSIER F. et. al. Role of toxin functional domains in anthrax pathogenesis, Infection and Immunity, 2000,68,4, p.1781-1786. * |
Cited By (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| RU2633508C1 (ru) * | 2016-12-27 | 2017-10-12 | Федеральное государственное учреждение "Федеральный исследовательский центр "Фундаментальные основы биотехнологии" Российской академии наук (ФИЦ Биотехнологии РАН) | Штамм E. coli - продуцент изолированного домена 1 протективного антигена Bacillus anthracis в форме вирусоподобных частиц |
| RU2633504C1 (ru) * | 2016-12-27 | 2017-10-12 | Федеральное государственное учреждение "Федеральный исследовательский центр "Фундаментальные основы биотехнологии" Российской академии наук (ФИЦ Биотехнологии РАН) | Штамм E.coli - продуцент полноразмерного протективного антигена Bacillus anthracis в форме вирусоподобных частиц |
| RU2821917C1 (ru) * | 2023-03-07 | 2024-06-27 | Федеральное государственное бюджетное образовательное учреждение высшего образования "Московский государственный университет имени М.В.Ломоносова" (МГУ) | Рекомбинантная вакцина против сибирской язвы на основе вирусов растений |
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| US20130164823A1 (en) | 2013-06-27 |
| EP1808489A1 (en) | 2007-07-18 |
| US9346860B2 (en) | 2016-05-24 |
| RU2004134341A (ru) | 2006-05-10 |
| US20030170263A1 (en) | 2003-09-11 |
| GB0016702D0 (en) | 2000-08-23 |
| AU2007201553B8 (en) | 2010-06-03 |
| CA2413045A1 (en) | 2002-01-17 |
| AU2007201553B2 (en) | 2010-04-22 |
| AU2007201553A1 (en) | 2007-05-03 |
| CN101012458A (zh) | 2007-08-08 |
| CA2413045C (en) | 2016-06-21 |
| CN1322134C (zh) | 2007-06-20 |
| JP2004502460A (ja) | 2004-01-29 |
| WO2002004646A1 (en) | 2002-01-17 |
| EP1301606A1 (en) | 2003-04-16 |
| JP2012010706A (ja) | 2012-01-19 |
| US8313928B2 (en) | 2012-11-20 |
| CA2658217A1 (en) | 2002-01-17 |
| ZA200210206B (en) | 2004-03-17 |
| EP1808489B1 (en) | 2016-03-23 |
| AU6930501A (en) | 2002-01-21 |
| US20100266639A1 (en) | 2010-10-21 |
| RU2385348C2 (ru) | 2010-03-27 |
| CN1440459A (zh) | 2003-09-03 |
| US7537771B2 (en) | 2009-05-26 |
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