KR102106762B1 - 에를리히아 항체의 검출을 위한 펩티드, 장치, 그리고 방법 - Google Patents
에를리히아 항체의 검출을 위한 펩티드, 장치, 그리고 방법 Download PDFInfo
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- KR102106762B1 KR102106762B1 KR1020157010378A KR20157010378A KR102106762B1 KR 102106762 B1 KR102106762 B1 KR 102106762B1 KR 1020157010378 A KR1020157010378 A KR 1020157010378A KR 20157010378 A KR20157010378 A KR 20157010378A KR 102106762 B1 KR102106762 B1 KR 102106762B1
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Citations (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2000032745A2 (en) | 1998-11-30 | 2000-06-08 | Research Development Foundation | Homologous 28-kilodalton immunodominant protein genes of ehrlichia canis and uses thereof |
| US20030103991A1 (en) | 1998-09-18 | 2003-06-05 | Yasuko Rikihisa | Outer membrane protein of Ehrlichia canis and Ehrlichia chaffeensis |
| WO2008137881A2 (en) | 2007-05-04 | 2008-11-13 | The Ohio State University Research Foundation | Ehrlichia ewingii proteins, nucleic acids, and methods of their use |
| US20110124125A1 (en) * | 2009-11-20 | 2011-05-26 | Abaxis, Inc. | Peptides, devices, and methods for the detection of ehrlichia antibodies |
Family Cites Families (40)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4366246A (en) | 1977-11-08 | 1982-12-28 | Genentech, Inc. | Method for microbial polypeptide expression |
| US4617262A (en) * | 1983-07-22 | 1986-10-14 | Cooperbiomedical, Inc. | Assaying for circulating immune complexes with labeled protein A |
| US6284238B1 (en) | 1995-06-06 | 2001-09-04 | Aquila Biopharmaceuticals, Inc. | Cell lines infected with granulocytic ehrlichia, vaccines, diagnostics and methods |
| US6451315B1 (en) | 1996-10-01 | 2002-09-17 | Corixa Corporation | Compounds and methods for the diagnosis and treatment of B. microti infection |
| US6593147B1 (en) * | 1996-10-17 | 2003-07-15 | University Of Florida Research Foundation, Inc. | Nucleic acid vaccines against rickettsial diseases and methods of use |
| US6653128B2 (en) | 1996-10-17 | 2003-11-25 | University Of Florida | Nucleic acid vaccines against rickettsial diseases and methods of use |
| US6207169B1 (en) | 1997-03-21 | 2001-03-27 | Corixa Corporation | Compounds and methods for the diagnosis and treatment of Ehrlichia infection |
| US6231869B1 (en) | 1997-03-21 | 2001-05-15 | Corixa Corporation | Compounds and methods for the diagnosis and treatment of ehrlichia infection |
| DE69841037D1 (de) | 1997-04-25 | 2009-09-17 | Antigenics Inc | Charakterisierung von granulozytischer ehrlichia und methoden für ihre verwendung. |
| AU748357B2 (en) | 1997-09-19 | 2002-06-06 | Ohio State Research Foundation, The | Outer membrane protein of ehrlichia canis and ehrlichia chaffeensis |
| AU1197799A (en) * | 1998-07-28 | 2000-02-21 | Aquila Biopharmaceuticals, Inc. | Granulocytic ehrlichia genes and uses thereof |
| US6043085A (en) | 1998-08-27 | 2000-03-28 | Research Development Foundation | Ehrlichia canis 120-kDa immunodominant antigenic protein and gene |
| US6544517B1 (en) | 1998-09-18 | 2003-04-08 | The Ohio State University Research Foundation | Outer membrane protein of Ehrlichia canis and Ehrlichia chaffeensis |
| US7888491B2 (en) | 1998-09-18 | 2011-02-15 | The Ohio State University Research Foundation | Outer membrane protein of Ehrlichia canis and Ehrlichia chaffeensis |
| US6392023B1 (en) | 1999-03-03 | 2002-05-21 | Research Development Foundation | Homologous 28-kilodalton immunodominant protein genes of Ehrlicha canis and uses thereof |
| BR0012556A (pt) | 1999-07-21 | 2002-07-02 | Cornell Res Foundation Inc | Genes e vacinas de ehrlichia canis |
| US6355777B1 (en) | 2000-04-28 | 2002-03-12 | Research Development Foundation | P43 antigen for the immunodiagnosis of canine ehrlichiosis and uses thereof |
| US7087372B2 (en) | 2001-01-18 | 2006-08-08 | Idexx Laboratories, Inc. | Compositions and methods for detection of Ehrlichia canis and Ehrlichia chaffeensis antibodies |
| US20030194756A1 (en) | 2002-04-12 | 2003-10-16 | O'connor Thomas Patrick | Peptides for detection of antibody to Ehrlichia equi |
| US7407770B2 (en) | 2001-01-18 | 2008-08-05 | Idexx Corporation | Compositions and methods for detection of Ehrlichia canis and Ehrlichia chaffeensis antibodies |
| US7183060B2 (en) | 2005-02-22 | 2007-02-27 | Idexx Laboratories, Inc. | Peptides for detection of antibody to Ehrlichia ewingii |
| US7172873B2 (en) | 2001-03-28 | 2007-02-06 | Heska Corporation | Methods of detecting early renal disease in animals |
| US20030129161A1 (en) | 2001-09-17 | 2003-07-10 | Hsien-Jue Chu | Interleukin-12 as a veterinary vaccine adjuvant |
| CN101294162B (zh) | 2002-11-04 | 2011-03-30 | 研究发展基金会 | 用于犬和人埃利希病的免疫诊断的p156抗原及其用途 |
| WO2004084841A2 (en) | 2003-03-27 | 2004-10-07 | Heska Corporation | Novel anti-feline albumin antibodies and methods of detecting early renal disease |
| US7304139B2 (en) | 2003-10-28 | 2007-12-04 | University Of Florida Research Foundation, Inc. | Polynucleotides and polypeptides of Anaplasma phagocytophilum and methods of using the same |
| US20050202046A1 (en) | 2004-03-11 | 2005-09-15 | Wyeth | Canine vaccine for protection against ehrlichiosis |
| US20060046310A1 (en) | 2004-08-25 | 2006-03-02 | Zong-Li Xia | Amplification method for solid phase immunoassays |
| US7842474B2 (en) | 2005-04-04 | 2010-11-30 | Idexx Laboratories, Inc. | Ehrlichia canis DIVA (differentiate infected from vaccinated animals) |
| ES2550140T3 (es) | 2005-04-04 | 2015-11-04 | Idexx Laboratories, Inc. | Antígenos DIVA (de Diferenciación entre Animales Vacunados e Infectados) de Erlichia canis |
| USRE46254E1 (en) | 2005-06-16 | 2016-12-27 | Research Development Foundation | Immunoreactive protein orthologs of Ehrlichia canis and E. chaffeensis |
| US20090176208A1 (en) | 2006-01-04 | 2009-07-09 | Simon Brodie | Methods for detecting, identifying and reporting the presence of animal pathological agents |
| US7776618B2 (en) | 2007-03-01 | 2010-08-17 | Church & Dwight Co., Inc. | Diagnostic detection device |
| US7507789B2 (en) | 2007-04-09 | 2009-03-24 | Idexx Laboratories, Inc. | Detection of Anaplasma platys |
| BRPI0816437B8 (pt) | 2007-09-21 | 2021-05-25 | Idexx Lab Inc | polipeptídeos purificados e métodos para a detecção de ehrlichia chaffeensis em uma amostra teste |
| BRPI0817202B1 (pt) * | 2007-09-21 | 2018-11-21 | Idexx Laboratories, Inc. | polipeptídeo purificado e método de detecção de anticorpos que se ligam especificamente a um polipeptídio do ehrlichia chaffeensis em uma amostra em teste |
| ES2913324T3 (es) | 2007-10-31 | 2022-06-01 | Idexx Lab Inc | DIVA de Ehrlichia canis (que diferencia animales infectados de vacunados) |
| ES2668863T3 (es) | 2012-10-11 | 2018-05-22 | Abaxis, Inc. | Péptidos, dispositivos y métodos para la detección de anticuerpos de Ehrlichia |
| CN103060468B (zh) | 2013-01-30 | 2014-02-12 | 扬州大学 | 一种埃里希氏菌的荧光定量pcr检测和分型的引物、探针及试剂盒 |
| US9442112B2 (en) | 2014-04-04 | 2016-09-13 | Abaxis, Inc. | Compositions and methods for identifying Ehrlichia species |
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Patent Citations (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US20030103991A1 (en) | 1998-09-18 | 2003-06-05 | Yasuko Rikihisa | Outer membrane protein of Ehrlichia canis and Ehrlichia chaffeensis |
| WO2000032745A2 (en) | 1998-11-30 | 2000-06-08 | Research Development Foundation | Homologous 28-kilodalton immunodominant protein genes of ehrlichia canis and uses thereof |
| WO2008137881A2 (en) | 2007-05-04 | 2008-11-13 | The Ohio State University Research Foundation | Ehrlichia ewingii proteins, nucleic acids, and methods of their use |
| US20110124125A1 (en) * | 2009-11-20 | 2011-05-26 | Abaxis, Inc. | Peptides, devices, and methods for the detection of ehrlichia antibodies |
Non-Patent Citations (2)
| Title |
|---|
| Asiyaa Gusa et al, Journal of Clinical Microbiology (2011), vol 39, no 11, pp 3871-3876. |
| Zhang Chunbin et al, Clinical and Vaccine Immunology (2008), vol 15, no 3, pp 402-411. |
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