ES2346116T3 - Epitopos artificiales de celulas t ayudadoras como estimuladores inmunes para peptidos sinteticos inmunogenos. - Google Patents
Epitopos artificiales de celulas t ayudadoras como estimuladores inmunes para peptidos sinteticos inmunogenos. Download PDFInfo
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- ES2346116T3 ES2346116T3 ES99928826T ES99928826T ES2346116T3 ES 2346116 T3 ES2346116 T3 ES 2346116T3 ES 99928826 T ES99928826 T ES 99928826T ES 99928826 T ES99928826 T ES 99928826T ES 2346116 T3 ES2346116 T3 ES 2346116T3
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Classifications
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- A61P9/10—Drugs for disorders of the cardiovascular system for treating ischaemic or atherosclerotic diseases, e.g. antianginal drugs, coronary vasodilators, drugs for myocardial infarction, retinopathy, cerebrovascula insufficiency, renal arteriosclerosis
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/005—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from viruses
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
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- C07K14/44—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from protozoa
- C07K14/445—Plasmodium
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
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- C07K14/46—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates
- C07K14/47—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/575—Hormones
- C07K14/655—Somatostatins
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/705—Receptors; Cell surface antigens; Cell surface determinants
- C07K14/70503—Immunoglobulin superfamily
- C07K14/70514—CD4
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K7/00—Peptides having 5 to 20 amino acids in a fully defined sequence; Derivatives thereof
- C07K7/04—Linear peptides containing only normal peptide links
- C07K7/23—Luteinising hormone-releasing hormone [LHRH]; Related peptides
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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
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/50—Immunoglobulins specific features characterized by immunoglobulin fragments
- C07K2317/52—Constant or Fc region; Isotype
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- 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
- C12N2740/00—Reverse transcribing RNA viruses
- C12N2740/00011—Details
- C12N2740/10011—Retroviridae
- C12N2740/16011—Human Immunodeficiency Virus, HIV
- C12N2740/16111—Human Immunodeficiency Virus, HIV concerning HIV env
- C12N2740/16122—New viral proteins or individual genes, new structural or functional aspects of known viral proteins or genes
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- 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
- C12N2770/00—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA ssRNA viruses positive-sense
- C12N2770/00011—Details
- C12N2770/32011—Picornaviridae
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- C12N2770/32122—New viral proteins or individual genes, new structural or functional aspects of known viral proteins or genes
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- 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
Landscapes
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- Peptides Or Proteins (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
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| US10041298A | 1998-06-20 | 1998-06-20 | |
| US100412 | 1998-06-20 |
Publications (1)
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| ES2346116T3 true ES2346116T3 (es) | 2010-10-08 |
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| ES99928826T Expired - Lifetime ES2346116T3 (es) | 1998-06-20 | 1999-06-21 | Epitopos artificiales de celulas t ayudadoras como estimuladores inmunes para peptidos sinteticos inmunogenos. |
| ES09179823T Expired - Lifetime ES2369055T3 (es) | 1998-06-20 | 1999-06-21 | Epítopos de células t auxiliares como estimulantes inmunitarios para inmunógenos peptídicos sintéticos. |
Family Applications After (1)
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|---|---|---|---|
| ES09179823T Expired - Lifetime ES2369055T3 (es) | 1998-06-20 | 1999-06-21 | Epítopos de células t auxiliares como estimulantes inmunitarios para inmunógenos peptídicos sintéticos. |
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| JP (2) | JP3993387B2 (enExample) |
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| EP0885244B2 (en) | 1996-03-01 | 2008-04-16 | Novartis AG | Peptide immunogens for vaccination against and treatment of allergy |
| TWI229679B (en) * | 1998-06-20 | 2005-03-21 | United Biomedical Inc | Artificial T helper cell epitopes as immune stimulators for synthetic peptide immunogens |
| US6025468A (en) * | 1998-06-20 | 2000-02-15 | United Biomedical, Inc. | Artificial T helper cell epitopes as immune stimulators for synthetic peptide immunogens including immunogenic LHRH peptides |
| TWI227241B (en) * | 1998-06-20 | 2005-02-01 | United Biomedical Inc | IgE-CH3 domain antigen peptide, peptide conjugate containing the same, and pharmaceutical composition for treating allergies containing the peptide conjugate |
| US6911527B1 (en) | 1999-01-11 | 2005-06-28 | The United States Of America As Represented By The Secretary Of The Department Of Health And Human Services | HIV related peptides |
| AU2603100A (en) * | 1999-01-11 | 2000-08-01 | Government Of The United States Of America, As Represented By The Secretary Of The Department Of Health And Human Services, The | Novel hiv related peptides |
| EP1195161A3 (en) * | 2000-08-30 | 2002-07-24 | Pfizer Products Inc. | Anti-IgE vaccines |
| US6906169B2 (en) * | 2001-05-25 | 2005-06-14 | United Biomedical, Inc. | Immunogenic peptide composition comprising measles virus Fprotein Thelper cell epitope (MUFThl-16) and N-terminus of β-amyloid peptide |
| US8088388B2 (en) | 2002-02-14 | 2012-01-03 | United Biomedical, Inc. | Stabilized synthetic immunogen delivery system |
| US7335359B2 (en) * | 2003-02-06 | 2008-02-26 | Tripep Ab | Glycosylated specificity exchangers |
| WO2004069873A2 (en) | 2003-02-06 | 2004-08-19 | Tripep Ab | Antigen/antibody or ligand/receptor glycosylated specificity exchangers |
| US20040202673A1 (en) * | 2003-04-08 | 2004-10-14 | Jen-Pin Huang | Constructs of branched synthetic peptide immunogens with artificial T helper cell epitopes coupled to B cell epitopes |
| CA2583113C (en) * | 2004-10-05 | 2015-11-10 | Diversa Corporation | Compositions comprising an antigen and a promiscuous t-cell epitope |
| AT501621A1 (de) * | 2005-03-15 | 2006-10-15 | Mattner Frank Dr | Zusammensetzungen zur verwendung bei der vorbeugung und behandlung der alzheimer- erkrankung |
| CN101193654A (zh) * | 2005-06-14 | 2008-06-04 | 赛托斯生物技术公司 | 抗原偶联物及其用途 |
| EP2012122A1 (en) * | 2007-07-06 | 2009-01-07 | Medigene AG | Mutated parvovirus structural proteins as vaccines |
| SG190562A1 (en) | 2008-04-18 | 2013-06-28 | Vaxinnate Corp | Deletion mutants of flagellin and methods of use |
| FR2945290A1 (fr) * | 2009-05-07 | 2010-11-12 | Maan Zrein | Anticorps biomarqueur et dispositif de diagnostic pour la detection de certaines maladies auto-immunes |
| CA2793959C (en) | 2010-03-25 | 2019-06-04 | Oregon Health & Science University | Cmv glycoproteins and recombinant vectors |
| CA2804604C (en) * | 2010-07-08 | 2023-10-03 | United Biomedical, Inc. | Designer peptide-based pcv2 vaccine |
| KR102190180B1 (ko) | 2011-04-15 | 2020-12-11 | 고꾸리쯔 다이가꾸 호우징 오사까 다이가꾸 | Ｄｎａ 백신 |
| PT2691530T (pt) | 2011-06-10 | 2018-05-10 | Univ Oregon Health & Science | Glicoproteínas e vectores recombinantes cmv |
| EP2568289A3 (en) | 2011-09-12 | 2013-04-03 | International AIDS Vaccine Initiative | Immunoselection of recombinant vesicular stomatitis virus expressing hiv-1 proteins by broadly neutralizing antibodies |
| EP2586461A1 (en) | 2011-10-27 | 2013-05-01 | Christopher L. Parks | Viral particles derived from an enveloped virus |
| WO2013101195A1 (en) | 2011-12-30 | 2013-07-04 | United Biomedical, Inc. | Synthetic peptide-based marker vaccine and diagnostic system for effective control of porcine reproductive and respiratory syndrome (prrs) |
| ES2631608T3 (es) | 2012-06-27 | 2017-09-01 | International Aids Vaccine Initiative | Variante de la glicoproteína Env del VIH-1 |
| CN102775478B (zh) * | 2012-08-10 | 2013-06-19 | 申联生物医药（上海）有限公司 | 口蹄疫病毒抗原多肽及疫苗 |
| JP6001974B2 (ja) | 2012-09-21 | 2016-10-05 | アンジェスＭｇ株式会社 | アポリポプロテイン（ａ）の特異的エピトープを含むＤＮＡワクチン |
| BR112015010756B1 (pt) | 2012-11-16 | 2022-04-12 | United Biomedical, Inc | Composições de vacina para a doença do pé-e-boca (fmd),e uso das mesmas |
| US9102752B2 (en) | 2013-03-15 | 2015-08-11 | United Biomedical, Inc. | Peptide vaccine for prevention and immunotherapy of dementia of the Alzheimer's type |
| US20150065381A1 (en) | 2013-09-05 | 2015-03-05 | International Aids Vaccine Initiative | Methods of identifying novel hiv-1 immunogens |
| EP2873423B1 (en) | 2013-10-07 | 2017-05-31 | International Aids Vaccine Initiative | Soluble hiv-1 envelope glycoprotein trimers |
| WO2016014071A1 (en) * | 2014-07-25 | 2016-01-28 | United Biomedical, Inc | Immunogenic lhrh composition and use thereof in pigs |
| US10174292B2 (en) | 2015-03-20 | 2019-01-08 | International Aids Vaccine Initiative | Soluble HIV-1 envelope glycoprotein trimers |
| US9931394B2 (en) | 2015-03-23 | 2018-04-03 | International Aids Vaccine Initiative | Soluble HIV-1 envelope glycoprotein trimers |
| CN105418738B (zh) * | 2015-07-03 | 2019-04-19 | 申联生物医药（上海）有限公司 | 口蹄疫病毒a型抗原多肽、融合抗原多肽及疫苗 |
| CN105176897A (zh) * | 2015-07-29 | 2015-12-23 | 中国药科大学 | 一种表达GnRH/M2融合多肽的重组工程菌株及其构建和应用 |
| JP2017141234A (ja) * | 2017-03-01 | 2017-08-17 | ユナイテッド・バイオメディカル・インコーポレーテッドＵｎｉｔｅｄ Ｂｉｏｍｅｄｉｃａｌ Ｉｎｃｏｒｐｏｒａｔｅｄ | ブタ生殖器呼吸器症候群（ｐｒｒｓ）の有効な制御のための合成ペプチドベースのマーカーワクチン及び診断システム |
| WO2019061297A1 (zh) * | 2017-09-29 | 2019-04-04 | 苏州工业园区唯可达生物科技有限公司 | 一种cd4辅助性t细胞表位融合肽及其疫苗 |
| CN107703294B (zh) * | 2017-10-12 | 2019-06-04 | 华派生物工程集团有限公司 | 一种用于检测鸡血清中cLHRH抗体效价的ELISA方法 |
| CA3085318A1 (en) * | 2017-12-11 | 2019-06-20 | Ubi Ip Holdings | Peptide immunogens of il-31 and formulations thereof for the treatment and/or prevention of atopic dermatitis |
| JP7497293B2 (ja) | 2018-03-16 | 2024-06-10 | ゾエティス・サービシーズ・エルエルシー | インターロイキン－３１に対するペプチドワクチン |
| CA3099296A1 (en) * | 2018-05-04 | 2019-11-07 | Ubi Ip Holdings | Artificial promiscuous t helper cell epitopes that facilitate targeted antibody production with limited t cell inflammatory response |
| PE20212156A1 (es) * | 2018-12-19 | 2021-11-09 | United Biomedical Inc | Epitopos artificiales promiscuos de linfocitos t colaboradores como estimuladores inmunes para inmunogenos peptidicos inteticos |
| CN117003898B (zh) * | 2023-09-27 | 2023-12-29 | 贝格探索(成都)科技有限公司 | 一种lhrh4-crm197-lf多聚重组蛋白及其制备方法和应用 |
| CN118812726B (zh) * | 2024-06-26 | 2025-05-16 | 西北民族大学 | 脑心肌炎多抗原表位重组蛋白及其在制备脑心肌炎疫苗中的应用 |
Family Cites Families (10)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| AU634153B2 (en) | 1988-02-01 | 1993-02-18 | Wyeth Holdings Corporation | T-cell epitope as carriers molecule for conjugate vaccines |
| IT1237764B (it) | 1989-11-10 | 1993-06-17 | Eniricerche Spa | Peptidi sintetici utili come carriers universali per la preparazione di coniugati immunogenici e loro impiego per lo sviluppo di vaccini sintetici. |
| US5759551A (en) * | 1993-04-27 | 1998-06-02 | United Biomedical, Inc. | Immunogenic LHRH peptide constructs and synthetic universal immune stimulators for vaccines |
| AU8091694A (en) | 1993-10-26 | 1995-05-22 | United Biomedical Inc. | Structured synthetic antigen libraries as diagnostics, vaccines and therapeutics |
| AU4826799A (en) * | 1998-06-20 | 2000-01-10 | United Biomedical Inc. | Synthetic somatostatin immunogen for growth promotion in farm animals |
| TWI227241B (en) * | 1998-06-20 | 2005-02-01 | United Biomedical Inc | IgE-CH3 domain antigen peptide, peptide conjugate containing the same, and pharmaceutical composition for treating allergies containing the peptide conjugate |
| TWI229679B (en) * | 1998-06-20 | 2005-03-21 | United Biomedical Inc | Artificial T helper cell epitopes as immune stimulators for synthetic peptide immunogens |
| US6107021A (en) * | 1998-06-20 | 2000-08-22 | United Biomedical, Inc. | Synthetic peptide vaccines for foot-and-mouth disease |
| US6090388A (en) * | 1998-06-20 | 2000-07-18 | United Biomedical Inc. | Peptide composition for prevention and treatment of HIV infection and immune disorders |
| US6025468A (en) * | 1998-06-20 | 2000-02-15 | United Biomedical, Inc. | Artificial T helper cell epitopes as immune stimulators for synthetic peptide immunogens including immunogenic LHRH peptides |
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1999
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- 1999-06-21 DK DK99928826.9T patent/DK1089760T3/da active
- 1999-06-21 EP EP09179823A patent/EP2181715B1/en not_active Expired - Lifetime
- 1999-06-21 BR BRPI9912177A patent/BRPI9912177B8/pt not_active IP Right Cessation
- 1999-06-21 AT AT99928826T patent/ATE463255T1/de active
- 1999-06-21 DK DK09179823.1T patent/DK2181715T3/da active
- 1999-06-21 ES ES99928826T patent/ES2346116T3/es not_active Expired - Lifetime
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| EP2181715A1 (en) | 2010-05-05 |
| JP2002518463A (ja) | 2002-06-25 |
| EP1089760A1 (en) | 2001-04-11 |
| ES2369055T3 (es) | 2011-11-24 |
| HK1143950A1 (en) | 2011-01-21 |
| HK1037860A1 (en) | 2002-02-22 |
| US6713301B1 (en) | 2004-03-30 |
| TWI229679B (en) | 2005-03-21 |
| AU4580899A (en) | 2000-01-10 |
| BRPI9912177B8 (pt) | 2021-05-25 |
| BR9912177A (pt) | 2001-04-10 |
| BRPI9912177B1 (pt) | 2016-07-26 |
| ATE510563T1 (de) | 2011-06-15 |
| JP3993387B2 (ja) | 2007-10-17 |
| JP2005112860A (ja) | 2005-04-28 |
| EP1089760B1 (en) | 2010-04-07 |
| EP2181715B1 (en) | 2011-05-25 |
| CN1201819C (zh) | 2005-05-18 |
| ATE463255T1 (de) | 2010-04-15 |
| DE69942225D1 (de) | 2010-05-20 |
| CA2329772C (en) | 2011-02-22 |
| DK2181715T3 (da) | 2011-09-05 |
| JP3993605B2 (ja) | 2007-10-17 |
| CN1306439A (zh) | 2001-08-01 |
| AU763543B2 (en) | 2003-07-24 |
| CA2329772A1 (en) | 1999-12-29 |
| WO1999066957A2 (en) | 1999-12-29 |
| EP1089760A4 (en) | 2005-01-12 |
| DK1089760T3 (da) | 2010-07-19 |
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