ES2447843T3 - Polip�ptidos de Lutzomyia longipalpis y m�todos de uso - Google Patents
Polip�ptidos de Lutzomyia longipalpis y m�todos de uso Download PDFInfo
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- ES2447843T3 ES2447843T3 ES09158294T ES09158294T ES2447843T3 ES 2447843 T3 ES2447843 T3 ES 2447843T3 ES 09158294 T ES09158294 T ES 09158294T ES 09158294 T ES09158294 T ES 09158294T ES 2447843 T3 ES2447843 T3 ES 2447843T3
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- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/18—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans
- C07K16/20—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans from protozoa
-
- 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
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- A—HUMAN NECESSITIES
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- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K39/00—Medicinal preparations containing antigens or antibodies
- A61K2039/51—Medicinal preparations containing antigens or antibodies comprising whole cells, viruses or DNA/RNA
- A61K2039/53—DNA (RNA) vaccination
-
- 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
- A61K2039/57—Medicinal preparations containing antigens or antibodies characterised by the type of response, e.g. Th1, Th2
-
- 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
- A61K2039/57—Medicinal preparations containing antigens or antibodies characterised by the type of response, e.g. Th1, Th2
- A61K2039/575—Medicinal preparations containing antigens or antibodies characterised by the type of response, e.g. Th1, Th2 humoral response
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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
- A61K2039/58—Medicinal preparations containing antigens or antibodies raising an immune response against a target which is not the antigen used for immunisation
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/20—Immunoglobulins specific features characterized by taxonomic origin
- C07K2317/21—Immunoglobulins specific features characterized by taxonomic origin from primates, e.g. man
-
- Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y02—TECHNOLOGIES OR APPLICATIONS FOR MITIGATION OR ADAPTATION AGAINST CLIMATE CHANGE
- Y02A—TECHNOLOGIES FOR ADAPTATION TO CLIMATE CHANGE
- Y02A50/00—TECHNOLOGIES FOR ADAPTATION TO CLIMATE CHANGE in human health protection, e.g. against extreme weather
- Y02A50/30—Against vector-borne diseases, e.g. mosquito-borne, fly-borne, tick-borne or waterborne diseases whose impact is exacerbated by climate change
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- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
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- General Health & Medical Sciences (AREA)
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- Molecular Biology (AREA)
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- Chemical Kinetics & Catalysis (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Peptides Or Proteins (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
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| US42230302P | 2002-10-29 | 2002-10-29 |
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| ES (1) | ES2447843T3 (enExample) |
| MX (1) | MXPA05004714A (enExample) |
| WO (1) | WO2004039958A2 (enExample) |
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| US7741437B2 (en) | 2002-09-19 | 2010-06-22 | The United States Of America As Represented By The Department Of Health And Human Services | P. ariasi polypeptides, p. perniciosus polypeptides and methods of use |
| EP1572968B1 (en) * | 2002-10-29 | 2009-04-22 | The Government Of The United States Of America As Represented By The Secretary Of The Department Of Health And Human Services | Lutzomyia longipalpis polypeptides and methods of use |
| US8968749B2 (en) | 2006-07-21 | 2015-03-03 | Universidade Federal De Minas Gerais—Ufmg | Vaccine composition and immunization method |
| BRPI0603490B1 (pt) * | 2006-07-21 | 2018-04-24 | Universidade Federal De Minas Gerais | Vacina recombinante contra a leishmaniose visceral canina |
| GB0717864D0 (en) | 2007-09-13 | 2007-10-24 | Peptcell Ltd | Peptide sequences and compositions |
| EP2283035B1 (en) * | 2008-05-08 | 2015-07-29 | Merial Limited | Leishmania vaccine using sand fly salivary immunogen |
| WO2010021940A1 (en) * | 2008-08-18 | 2010-02-25 | The United States Of America, As Represented By The Secretary, Department Of Health And Human Services | Insect proteins as adjuvants to accelerate the immune response |
| JP5590986B2 (ja) | 2010-06-23 | 2014-09-17 | 株式会社シマノ | 釣り用リールのワンウェイクラッチ |
| UY37753A (es) | 2017-06-02 | 2018-11-30 | Amgen Inc | Antagonistas de péptido pac1 |
Family Cites Families (51)
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| US2909462A (en) | 1955-12-08 | 1959-10-20 | Bristol Myers Co | Acrylic acid polymer laxative compositions |
| US4036945A (en) | 1976-05-03 | 1977-07-19 | The Massachusetts General Hospital | Composition and method for determining the size and location of myocardial infarcts |
| US4444487A (en) | 1979-07-02 | 1984-04-24 | Xerox Corporation | Multiple-flash fuser |
| US4331647A (en) | 1980-03-03 | 1982-05-25 | Goldenberg Milton David | Tumor localization and therapy with labeled antibody fragments specific to tumor-associated markers |
| US4722848A (en) | 1982-12-08 | 1988-02-02 | Health Research, Incorporated | Method for immunizing animals with synthetically modified vaccinia virus |
| US4603112A (en) | 1981-12-24 | 1986-07-29 | Health Research, Incorporated | Modified vaccinia virus |
| GB8308235D0 (en) | 1983-03-25 | 1983-05-05 | Celltech Ltd | Polypeptides |
| US4816567A (en) | 1983-04-08 | 1989-03-28 | Genentech, Inc. | Recombinant immunoglobin preparations |
| US4745051A (en) | 1983-05-27 | 1988-05-17 | The Texas A&M University System | Method for producing a recombinant baculovirus expression vector |
| DE3584341D1 (de) | 1984-08-24 | 1991-11-14 | Upjohn Co | Rekombinante dna-verbindungen und expression von polypeptiden wie tpa. |
| US4745055A (en) | 1985-05-07 | 1988-05-17 | California Biotechnology Inc. | Fused protein for enzyme immunoassay system |
| EP0256654B1 (en) | 1986-07-07 | 1996-09-18 | Centocor, Inc. | Chimeric murine/human immunoglobulin specific for tumour-associated 17-1A Antigen |
| US4946778A (en) | 1987-09-21 | 1990-08-07 | Genex Corporation | Single polypeptide chain binding molecules |
| EP0260148A3 (en) | 1986-09-12 | 1989-06-07 | Genentech, Inc. | Improved recombinant expression method, vector and transformed cells |
| IL84154A0 (en) | 1986-10-16 | 1988-03-31 | Microgenesys Inc | Polypeptides derived from the envelope gene of human immunodeficiency virus in recombinant baculovirus infected insect cells and vaccines against acquired immune deficiency syndrome containing the same |
| GB8626412D0 (en) | 1986-11-05 | 1986-12-03 | Clark M R | Antibodies |
| GB8717430D0 (en) | 1987-07-23 | 1987-08-26 | Celltech Ltd | Recombinant dna product |
| CA1323293C (en) | 1987-12-11 | 1993-10-19 | Keith C. Backman | Assay using template-dependent nucleic acid probe reorganization |
| DE3743138A1 (de) | 1987-12-18 | 1989-09-14 | Mayr Christian Gmbh & Co Kg | Schleifringlose, elektromagnetische ueberlastkupplung |
| JP2955759B2 (ja) | 1988-07-20 | 1999-10-04 | セゲブ・ダイアグノスティックス・インコーポレイテッド | 核酸配列を増幅及び検出する方法 |
| CA2003300A1 (en) | 1988-11-21 | 1990-05-21 | Franklin Volvovitz | Skin test and test kit for aids |
| US5703055A (en) | 1989-03-21 | 1997-12-30 | Wisconsin Alumni Research Foundation | Generation of antibodies through lipid mediated DNA delivery |
| US5397772A (en) * | 1989-06-29 | 1995-03-14 | The President And Fellows Of Harvard College | Vasodilatory peptides from the salivary gland of the sand fly Lutzomyia longipalpis |
| US5270202A (en) | 1989-11-03 | 1993-12-14 | Syamal Raychaudhuri | Anti-idiotypic antibodies to human melanoma-associated proteoglycan antigen |
| US5427930A (en) | 1990-01-26 | 1995-06-27 | Abbott Laboratories | Amplification of target nucleic acids using gap filling ligase chain reaction |
| EP0438803B1 (en) | 1990-01-26 | 1997-03-12 | Immunomedics, Inc. | Vaccines against cancer and infectious diseases |
| AU672359B2 (en) | 1991-03-07 | 1996-10-03 | Virogenetics Corporation | Genetically engineered vaccine strain |
| DE69225710T3 (de) | 1991-07-25 | 2004-10-14 | Idec Pharmaceuticals Corp., San Diego | Anregung von antworten zytotoxischer t-lymphozyten |
| US5709860A (en) | 1991-07-25 | 1998-01-20 | Idec Pharmaceuticals Corporation | Induction of cytotoxic T-lymphocyte responses |
| US5643578A (en) | 1992-03-23 | 1997-07-01 | University Of Massachusetts Medical Center | Immunization by inoculation of DNA transcription unit |
| US5662907A (en) | 1992-08-07 | 1997-09-02 | Cytel Corporation | Induction of anti-tumor cytotoxic T lymphocytes in humans using synthetic peptide epitopes |
| CA2142007C (en) | 1992-08-11 | 2007-10-30 | Robert Glen Urban | Immunomodulatory peptides |
| US5593972A (en) | 1993-01-26 | 1997-01-14 | The Wistar Institute | Genetic immunization |
| WO1995006729A1 (en) | 1993-09-03 | 1995-03-09 | Mcgill University | Differentially expressed leishmania genes and proteins |
| FR2712603B1 (fr) | 1993-11-18 | 1996-02-09 | Centre Nat Rech Scient | Virus recombinants, préparation et utilisation en thérapie génique. |
| US5529780A (en) | 1994-03-30 | 1996-06-25 | Virogenetics Corporation | Nucleotide and amino acid sequences of canine herpesvirus gB and gC |
| US5648211A (en) | 1994-04-18 | 1997-07-15 | Becton, Dickinson And Company | Strand displacement amplification using thermophilic enzymes |
| WO1996002668A1 (en) | 1994-07-15 | 1996-02-01 | Azco Nobel N.V. | Use of rna polymerase to improve nucleic acid amplification process |
| EP0826063A1 (en) | 1995-04-25 | 1998-03-04 | Vical Incorporated | Single-vial formulations of dna/lipid complexes |
| AT402203B (de) | 1995-06-13 | 1997-03-25 | Himmler Gottfried Dipl Ing Dr | Verfahren zur transkriptionsfreien amplifizierung von nucleinsäuren |
| EP0803573A1 (en) | 1996-04-25 | 1997-10-29 | Gesellschaft für Biotechnologische Forschung mbH (GBF) | Polycistronic expression construct with cytokines for multivalent vaccines |
| FR2750865B1 (fr) | 1996-06-27 | 1998-12-04 | Rhone Merieux | Vaccin vivant recombinant a base d'herpesvirus canin, notamment contre la maladie de carre, la rage ou le virus parainfluenza de type 2 |
| US6090393A (en) | 1996-07-03 | 2000-07-18 | Merial | Recombinant canine adenoviruses, method for making and uses thereof |
| US6156567A (en) | 1996-07-03 | 2000-12-05 | Merial | Truncated transcriptionally active cytomegalovirus promoters |
| AU737243B2 (en) | 1996-07-03 | 2001-08-16 | Merial, Inc. | Recombinant canine adenovirus (CAV) containing exogenous DNA |
| ATE292980T1 (de) | 1996-10-11 | 2005-04-15 | Univ California | Immunostimulierende oligonucleotidekonjugate |
| US6017537A (en) | 1998-12-18 | 2000-01-25 | Connaught Laboratories, Inc. | Formyl methionyl peptide vaccine adjuvant |
| US6645740B1 (en) | 1999-06-10 | 2003-11-11 | Merial Limited | Nucleic acids encodings equine GM-CSF |
| AU2002347464A1 (en) | 2001-06-19 | 2003-01-02 | The Gouvernment Of The United States Of America, As Represented By The Secretary Department Of Healt | Anti-arthropod vector vaccines methods of selecting and uses thereof |
| US7741437B2 (en) | 2002-09-19 | 2010-06-22 | The United States Of America As Represented By The Department Of Health And Human Services | P. ariasi polypeptides, p. perniciosus polypeptides and methods of use |
| EP1572968B1 (en) * | 2002-10-29 | 2009-04-22 | The Government Of The United States Of America As Represented By The Secretary Of The Department Of Health And Human Services | Lutzomyia longipalpis polypeptides and methods of use |
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2003
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- 2003-10-29 WO PCT/US2003/034453 patent/WO2004039958A2/en not_active Ceased
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2009
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- 2009-12-17 JP JP2009285970A patent/JP2010142226A/ja not_active Withdrawn
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2013
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2015
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2016
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2018
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| US9382302B2 (en) | 2016-07-05 |
| US10314900B2 (en) | 2019-06-11 |
| AU2003287267A1 (en) | 2004-05-25 |
| WO2004039958A3 (en) | 2005-12-08 |
| EP1572968B1 (en) | 2009-04-22 |
| EP2085467A2 (en) | 2009-08-05 |
| US20140093531A1 (en) | 2014-04-03 |
| DE60327366D1 (de) | 2009-06-04 |
| EP1572968A2 (en) | 2005-09-14 |
| JP2010142226A (ja) | 2010-07-01 |
| WO2004039958A2 (en) | 2004-05-13 |
| EP2085467B1 (en) | 2013-12-11 |
| US20150315254A1 (en) | 2015-11-05 |
| US9120867B2 (en) | 2015-09-01 |
| MXPA05004714A (es) | 2006-03-17 |
| JP2006516187A (ja) | 2006-06-29 |
| ATE429487T1 (de) | 2009-05-15 |
| US20090117139A1 (en) | 2009-05-07 |
| BR0315872A (pt) | 2006-07-18 |
| AU2003287267A8 (en) | 2004-05-25 |
| EP2085467A3 (en) | 2009-10-14 |
| EP1572968A4 (en) | 2006-07-19 |
| US9884100B2 (en) | 2018-02-06 |
| US8628780B2 (en) | 2014-01-14 |
| US7485306B2 (en) | 2009-02-03 |
| US20160279211A1 (en) | 2016-09-29 |
| US20060051364A1 (en) | 2006-03-09 |
| US20180147269A1 (en) | 2018-05-31 |
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