AU2002314358C1 - Mycobacterial antigens expressed during latency - Google Patents
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- AU2002314358C1 AU2002314358C1 AU2002314358A AU2002314358A AU2002314358C1 AU 2002314358 C1 AU2002314358 C1 AU 2002314358C1 AU 2002314358 A AU2002314358 A AU 2002314358A AU 2002314358 A AU2002314358 A AU 2002314358A AU 2002314358 C1 AU2002314358 C1 AU 2002314358C1
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- 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
-
- 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
- A61P31/06—Antibacterial agents for tuberculosis
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
-
- 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
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- General Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Medicinal Chemistry (AREA)
- Oncology (AREA)
- Veterinary Medicine (AREA)
- Biophysics (AREA)
- Molecular Biology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Biochemistry (AREA)
- Genetics & Genomics (AREA)
- Communicable Diseases (AREA)
- Gastroenterology & Hepatology (AREA)
- Chemical Kinetics & Catalysis (AREA)
- General Chemical & Material Sciences (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Pharmacology & Pharmacy (AREA)
- Animal Behavior & Ethology (AREA)
- Public Health (AREA)
- Pulmonology (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
- Peptides Or Proteins (AREA)
- Measuring Or Testing Involving Enzymes Or Micro-Organisms (AREA)
- Enzymes And Modification Thereof (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Medicines Containing Material From Animals Or Micro-Organisms (AREA)
- Investigating Or Analysing Biological Materials (AREA)
Priority Applications (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| AU2002314358A AU2002314358C1 (en) | 2001-07-04 | 2002-07-04 | Mycobacterial antigens expressed during latency |
| AU2008243118A AU2008243118A1 (en) | 2001-07-04 | 2008-11-05 | Mycobacterial antigens expressed during latency |
Applications Claiming Priority (6)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| GB0116385.6 | 2001-07-04 | ||
| GB0116385A GB0116385D0 (en) | 2001-07-04 | 2001-07-04 | Mycobacterial antigens expressed during latency |
| GB0123993A GB0123993D0 (en) | 2001-10-05 | 2001-10-05 | Mycobacterial antigens expressed during latency |
| GB0123993.8 | 2001-10-05 | ||
| PCT/GB2002/003052 WO2003004520A2 (en) | 2001-07-04 | 2002-07-04 | Mycobacterial antigens expressed during latency |
| AU2002314358A AU2002314358C1 (en) | 2001-07-04 | 2002-07-04 | Mycobacterial antigens expressed during latency |
Related Child Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| AU2008243118A Division AU2008243118A1 (en) | 2001-07-04 | 2008-11-05 | Mycobacterial antigens expressed during latency |
Publications (3)
| Publication Number | Publication Date |
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| AU2002314358A1 AU2002314358A1 (en) | 2003-05-22 |
| AU2002314358B2 AU2002314358B2 (en) | 2008-08-14 |
| AU2002314358C1 true AU2002314358C1 (en) | 2009-03-26 |
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Family Applications (2)
| Application Number | Title | Priority Date | Filing Date |
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| AU2002314358A Ceased AU2002314358C1 (en) | 2001-07-04 | 2002-07-04 | Mycobacterial antigens expressed during latency |
| AU2008243118A Abandoned AU2008243118A1 (en) | 2001-07-04 | 2008-11-05 | Mycobacterial antigens expressed during latency |
Family Applications After (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| AU2008243118A Abandoned AU2008243118A1 (en) | 2001-07-04 | 2008-11-05 | Mycobacterial antigens expressed during latency |
Country Status (6)
| Country | Link |
|---|---|
| US (3) | US7393540B2 (https=) |
| EP (2) | EP2196473A1 (https=) |
| JP (1) | JP2005508613A (https=) |
| AU (2) | AU2002314358C1 (https=) |
| CA (1) | CA2453173C (https=) |
| WO (1) | WO2003004520A2 (https=) |
Families Citing this family (37)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| GB9806093D0 (en) * | 1998-03-20 | 1998-05-20 | Taylor John Hermon | Diagnostics and vaccines for mycobacterial infections of animals and humans |
| JP2005504523A (ja) | 2001-06-22 | 2005-02-17 | ヘルス プロテクション エージェンシー | 低酸素圧下で発現するマイコバクテリア抗原 |
| EP2196473A1 (en) | 2001-07-04 | 2010-06-16 | Health Protection Agency | Mycobacterial antigens expressed during latency |
| GB0125535D0 (en) * | 2001-10-24 | 2001-12-12 | Microbiological Res Authority | Mycobacterial genes down-regulated during latency |
| AU2003242504A1 (en) * | 2002-07-13 | 2004-02-02 | Statens Serum Institut | Therapeutic tuberculosis vaccines |
| WO2004067718A2 (en) * | 2003-01-24 | 2004-08-12 | Emory University | Necrosis-deficient mutants of tuberculosis bacteria |
| ES2231037B1 (es) | 2003-10-31 | 2005-12-16 | Archivel Technologies, Sl | Agente inmunoterapico util para el tratamiento combinado de la tuberculosis en asociacion con otros farmacos. |
| CN101203239B (zh) * | 2005-03-31 | 2014-09-17 | 莱顿大学医药中心 | 诊断、预防和治疗分枝杆菌感染和结核疾病的方法和装置 |
| CA2606962A1 (en) * | 2005-04-29 | 2006-11-09 | Fusion Antibodies Limited | Assays for diagnosis of tuberculosis and uses thereof |
| CA2612900C (en) | 2005-06-23 | 2016-08-09 | Claus Aagaard | Improved tuberculosis vaccines |
| US7968694B2 (en) | 2005-07-01 | 2011-06-28 | Forsyth Dental Infirmary For Children | Tuberculosis antigen detection assays and vaccines |
| ATE466876T1 (de) * | 2005-08-09 | 2010-05-15 | Hav Vaccines Ltd | Immunogene konstrukte |
| US7601357B2 (en) * | 2005-12-07 | 2009-10-13 | University Of Central Florida Research Foundation, Inc. | Targeting of long chain triacylglycerol hydrolase gene for tuberculosis treatment |
| CN101378764A (zh) * | 2005-12-09 | 2009-03-04 | 贝勒研究院 | 通过血液白细胞微阵列分析对系统性红斑狼疮的诊断、预后和疾病发展的监测 |
| EP1996732A4 (en) * | 2006-03-02 | 2010-03-31 | Uab Research Foundation | RECOGNITION AND TREATMENT AND DISCOVERY OF REMEDIES AGAINST MYCOBACTERIAL DISEASES |
| ES2307402B1 (es) | 2006-10-30 | 2009-09-30 | Archivel Farma, S.L. | Vacuna profilactica contra la tuberculosis. |
| AP2011005546A0 (en) * | 2008-06-25 | 2011-02-28 | Baylor Res Intitute | Blood transcriptional signature of mycobacterium tuberculosis infection. |
| US20110129817A1 (en) * | 2009-11-30 | 2011-06-02 | Baylor Research Institute | Blood transcriptional signature of active versus latent mycobacterium tuberculosis infection |
| US20100015171A1 (en) | 2008-07-15 | 2010-01-21 | Statens Serum Institute | Vaccines comprising tb 10.4 |
| ES2335177B1 (es) | 2008-09-19 | 2011-02-28 | Archivel Farma, S.L. | Agente inmunoterapeutico apropiado para la profilaxis primaria de la tuberculosis. |
| WO2011063283A2 (en) | 2009-11-20 | 2011-05-26 | Oregon Health & Science University | Methods for detecting a mycobacterium tuberculosis infection |
| GB201008512D0 (en) * | 2010-05-21 | 2010-07-07 | Health Prot Agency | Mycobacterial antigen composition |
| ITRM20100411A1 (it) * | 2010-07-23 | 2012-01-24 | Massimo Amicosante | Uso di sequenze amminoacidiche da mycobacterium tuberculosis o dei loro corrispondenti acidi nucleici per la diagnosi e la prevenzione di infezione tubercolare, relativo kit diagnostico e vaccino. |
| EP2471511A1 (en) | 2011-01-04 | 2012-07-04 | Archivel Farma, SL | Liposome formulation suitable for treating or preventing tuberculosis |
| EP2661253B1 (en) | 2011-01-04 | 2017-04-19 | Archivel Farma, SL | Liposome formulation suitable for treating or preventing tuberculosis |
| WO2012138754A2 (en) * | 2011-04-04 | 2012-10-11 | Beth Israel Deaconess Medical Center, Inc. | Mycobacterial vaccine vectors and methods of using the same |
| JP2014531896A (ja) * | 2011-08-30 | 2014-12-04 | ザ ユーエービー リサーチ ファンデーション | ヒト型結核菌ポリンおよび毒素ならびに関連方法 |
| US10703784B2 (en) * | 2011-09-30 | 2020-07-07 | La Jolla Institute For Allergy And Immunology | Antigens and epitopes derived from Mycobacterium tuberculosis |
| US20140349320A1 (en) * | 2011-12-15 | 2014-11-27 | The Trustees Of The University Of Pennsylvania | Using Adaptive Immunity to Detect Drug Resistance |
| CN104640564B (zh) | 2012-07-10 | 2020-08-04 | 特兰斯吉恩股份有限公司 | 分枝杆菌抗原疫苗 |
| WO2014210327A1 (en) * | 2013-06-27 | 2014-12-31 | The Brigham And Women's Hospital, Inc. | Methods and systems for determining m. tuberculosis infection |
| EP3092000A1 (en) | 2014-01-09 | 2016-11-16 | Transgene SA | Fusion of heterooligomeric mycobacterial antigens |
| GB201400819D0 (en) * | 2014-01-17 | 2014-03-05 | Sec Dep For Health The | Mycobacterial antigen composition |
| US10295538B2 (en) | 2014-08-15 | 2019-05-21 | Oxford Immunotec Limited | Mycobacterium tuberculosis proteins |
| CN108267588B (zh) * | 2016-12-30 | 2020-10-23 | 首都医科大学附属北京胸科医院 | 结核分枝杆菌蛋白在制备诊断结核潜伏感染者和/或活动性肺结核产品中的用途 |
| EP3877519B1 (en) | 2018-11-09 | 2026-03-11 | Ginkgo Bioworks, Inc. | Biosynthesis of mogrosides |
| CN110129465B (zh) * | 2019-05-22 | 2023-08-22 | 杭州优思达生物技术股份有限公司 | 一种海分枝杆菌核酸的快速检测方法及其试剂盒 |
Family Cites Families (25)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| GB9024320D0 (en) | 1990-11-08 | 1990-12-19 | Univ London | Treatment of uveitis |
| DE4221858A1 (de) | 1992-07-03 | 1994-01-05 | Becker Carl Chemie Gmbh | Addukte von 0,0-Dialkyldithiophosphorsäuren an ungesättigte Verbindungen, Verfahren zu ihrer Herstellung und ihre Verwendung als Schmiermitteladditive |
| US6583266B1 (en) * | 1993-08-19 | 2003-06-24 | Genome Therapeutics Corporation | Nucleic acid and amino acid sequences relating to mycobacterium tuberculosis and leprae for diagnostics and therapeutics |
| US5783386A (en) | 1994-02-24 | 1998-07-21 | Agresearch, New Zealand Pastoral Agriculture Research Institute Ltd. | Mycobacteria virulence factors and a novel method for their identification |
| KR20060099543A (ko) | 1994-12-09 | 2006-09-19 | 임페리얼 컬리지 이노베이션스 리미티드 | 유전자의 동정 |
| US6572865B1 (en) * | 1995-06-15 | 2003-06-03 | University Of Victoria Innovation And Development Corporation | Mycobacterium tuberculosis DNA sequences encoding immunostimulatory peptides and methods for using same |
| US5998194A (en) * | 1995-12-21 | 1999-12-07 | Abbott Laboratories | Polyketide-associated sugar biosynthesis genes |
| CA2197524A1 (en) * | 1996-02-22 | 1997-08-22 | Bradley Stuart Dehoff | Polyketide synthase genes |
| WO1997035611A1 (en) | 1996-03-27 | 1997-10-02 | The Johns-Hopkins University | Stationary phase, stress response sigma factor from mycobacterium tuberculosis, and regulation thereof |
| CZ126699A3 (cs) | 1996-10-11 | 1999-09-15 | Corixa Corporation | Polypeptid obsahující antigenní část rozpustného antigenu M. tuberculosis nebo variantu uvedeného antigenu, molekula DNA kódující tento polypeptid, expresivní vektor, hostitelská buňka, způsoby diagnostiky infekce M. tuberculosis a diagnostické kity |
| US6555653B2 (en) | 1997-05-20 | 2003-04-29 | Corixa Corporation | Compounds for diagnosis of tuberculosis and methods for their use |
| GB9711389D0 (en) | 1997-06-04 | 1997-07-30 | Univ Wales The | Bacterial pheromones and uses therefor |
| EP1003870A1 (en) | 1997-07-16 | 2000-05-31 | Institut Pasteur | A polynucleotide functionally coding for the lhp protein from mycobacterium tuberculosis, its biologically active derivative fragments, as well as methods using the same |
| WO1999010536A1 (en) | 1997-08-22 | 1999-03-04 | Yale University | A process to study changes in gene expression in granulocytic cells |
| GB9723630D0 (en) | 1997-11-07 | 1998-01-07 | Stanford Rook Ltd | M.vaccae preparation and its use |
| US6183957B1 (en) * | 1998-04-16 | 2001-02-06 | Institut Pasteur | Method for isolating a polynucleotide of interest from the genome of a mycobacterium using a BAC-based DNA library application to the detection of mycobacteria |
| EP1075485A4 (en) | 1998-05-05 | 2004-12-15 | Gene Logic Inc | METHOD FOR EXAMINING GENE EXPRESSION IN T LYMPHOCYTES |
| US6892139B2 (en) * | 1999-01-29 | 2005-05-10 | The Regents Of The University Of California | Determining the functions and interactions of proteins by comparative analysis |
| GB9904773D0 (en) | 1999-03-02 | 1999-04-28 | Microbiological Res Authority | Culture of mycobacteria |
| US6573361B1 (en) * | 1999-12-06 | 2003-06-03 | Monsanto Technology Llc | Antifungal proteins and methods for their use |
| US6613553B1 (en) * | 2000-02-04 | 2003-09-02 | St. Jude Children's Research Hospital | Enoyl reductases and methods of use thereof |
| AU2002306849A1 (en) | 2001-03-21 | 2002-10-08 | Elitra Pharmaceuticals, Inc. | Identification of essential genes in microorganisms |
| JP2005504523A (ja) | 2001-06-22 | 2005-02-17 | ヘルス プロテクション エージェンシー | 低酸素圧下で発現するマイコバクテリア抗原 |
| EP2196473A1 (en) | 2001-07-04 | 2010-06-16 | Health Protection Agency | Mycobacterial antigens expressed during latency |
| GB0125535D0 (en) | 2001-10-24 | 2001-12-12 | Microbiological Res Authority | Mycobacterial genes down-regulated during latency |
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2002
- 2002-07-04 EP EP10150877A patent/EP2196473A1/en not_active Withdrawn
- 2002-07-04 JP JP2003510686A patent/JP2005508613A/ja active Pending
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- 2002-07-04 WO PCT/GB2002/003052 patent/WO2003004520A2/en not_active Ceased
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Also Published As
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| US7393540B2 (en) | 2008-07-01 |
| AU2008243118A1 (en) | 2008-11-27 |
| US20090082296A1 (en) | 2009-03-26 |
| US8399650B2 (en) | 2013-03-19 |
| AU2002314358B2 (en) | 2008-08-14 |
| WO2003004520A2 (en) | 2003-01-16 |
| EP1404706A2 (en) | 2004-04-07 |
| US8003776B2 (en) | 2011-08-23 |
| US20120034689A1 (en) | 2012-02-09 |
| EP2196473A1 (en) | 2010-06-16 |
| JP2005508613A (ja) | 2005-04-07 |
| CA2453173A1 (en) | 2003-01-16 |
| WO2003004520A3 (en) | 2003-10-16 |
| US20040241826A1 (en) | 2004-12-02 |
| CA2453173C (en) | 2013-12-10 |
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