BE1022949B1 - Composition immunogene - Google Patents
Composition immunogene Download PDFInfo
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- BE1022949B1 BE1022949B1 BE2015/5390A BE201505390A BE1022949B1 BE 1022949 B1 BE1022949 B1 BE 1022949B1 BE 2015/5390 A BE2015/5390 A BE 2015/5390A BE 201505390 A BE201505390 A BE 201505390A BE 1022949 B1 BE1022949 B1 BE 1022949B1
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- seq
- cdtb
- protein
- cdta
- difficile
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- A61K2039/555—Medicinal preparations containing antigens or antibodies characterised by a specific combination antigen/adjuvant
- A61K2039/55511—Organic adjuvants
- A61K2039/55555—Liposomes; Vesicles, e.g. nanoparticles; Spheres, e.g. nanospheres; Polymers
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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
- A61K2039/555—Medicinal preparations containing antigens or antibodies characterised by a specific combination antigen/adjuvant
- A61K2039/55511—Organic adjuvants
- A61K2039/55572—Lipopolysaccharides; Lipid A; Monophosphoryl lipid A
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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
- A61K2039/555—Medicinal preparations containing antigens or antibodies characterised by a specific combination antigen/adjuvant
- A61K2039/55511—Organic adjuvants
- A61K2039/55577—Saponins; Quil A; QS21; ISCOMS
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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
- A61K2039/70—Multivalent vaccine
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| GBGB1411306.2A GB201411306D0 (en) | 2014-06-25 | 2014-06-25 | Immunogenic composition |
| GB201411371A GB201411371D0 (en) | 2014-06-26 | 2014-06-26 | Immunogenic composition |
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| BE1022949A1 BE1022949A1 (fr) | 2016-10-21 |
| BE1022949B1 true BE1022949B1 (fr) | 2016-10-21 |
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| US11123419B2 (en) * | 2017-03-15 | 2021-09-21 | Novavax, Inc. | Methods and compositions for inducing immune responses against Clostridium difficile |
| WO2019243307A1 (en) | 2018-06-19 | 2019-12-26 | Glaxosmithkline Biologicals Sa | Immunogenic composition |
| GB202205833D0 (en) | 2022-04-21 | 2022-06-08 | Glaxosmithkline Biologicals Sa | Bacteriophage |
Citations (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2005004791A2 (en) * | 2002-11-08 | 2005-01-20 | President And Fellows Of Harvard College | Compounds and methods for the treatment and prevention of bacterial infection |
| WO2013112867A1 (en) * | 2012-01-27 | 2013-08-01 | Merck Sharp & Dohme Corp. | Vaccines against clostridium difficile comprising recombinant toxins |
| WO2014086787A1 (en) * | 2012-12-05 | 2014-06-12 | Glaxosmithkline Biologicals S.A. | Immunogenic composition |
| WO2014096393A1 (en) * | 2012-12-23 | 2014-06-26 | Glaxosmithkline Biologicals S.A. | Immunogenic composition comprising elements of c. difficile cdtb and/or cdta proteins |
Family Cites Families (17)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4235877A (en) | 1979-06-27 | 1980-11-25 | Merck & Co., Inc. | Liposome particle containing viral or bacterial antigenic subunit |
| US4436727A (en) | 1982-05-26 | 1984-03-13 | Ribi Immunochem Research, Inc. | Refined detoxified endotoxin product |
| US4866034A (en) | 1982-05-26 | 1989-09-12 | Ribi Immunochem Research Inc. | Refined detoxified endotoxin |
| US4751180A (en) | 1985-03-28 | 1988-06-14 | Chiron Corporation | Expression using fused genes providing for protein product |
| US4935233A (en) | 1985-12-02 | 1990-06-19 | G. D. Searle And Company | Covalently linked polypeptide cell modulators |
| US4877611A (en) | 1986-04-15 | 1989-10-31 | Ribi Immunochem Research Inc. | Vaccine containing tumor antigens and adjuvants |
| AU614755B2 (en) | 1987-06-05 | 1991-09-12 | United States of America, as represented by the Secretary, U.S. Department of Commerce, The | Autocrine motility factors in cancer diagnosis and management |
| US4912094B1 (en) | 1988-06-29 | 1994-02-15 | Ribi Immunochem Research Inc. | Modified lipopolysaccharides and process of preparation |
| ATE115862T1 (de) | 1989-02-04 | 1995-01-15 | Akzo Nobel Nv | Tocole als impfstoffadjuvans. |
| SK279188B6 (sk) | 1992-06-25 | 1998-07-08 | Smithkline Beecham Biologicals S.A. | Vakcínová kompozícia spôsob jej prípravy a použiti |
| ES2162139T5 (es) | 1993-03-23 | 2008-05-16 | Smithkline Beecham Biologicals S.A. | Composiciones de vacuna que contienen monofosforil-lipido a 3-o-desacilado. |
| NZ337543A (en) | 1994-10-24 | 2002-06-28 | Allergan Inc | Composition comprising avian antitoxin against clostridial neurotoxin protein and method for producing recombinant antitoxin proteins are provided for |
| UA56132C2 (uk) | 1995-04-25 | 2003-05-15 | Смітклайн Бічем Байолоджікалс С.А. | Композиція вакцини (варіанти), спосіб стабілізації qs21 відносно гідролізу (варіанти), спосіб приготування композиції вакцини |
| CA2220530A1 (en) | 1995-06-02 | 1996-12-05 | Incyte Pharmaceuticals, Inc. | Improved method for obtaining full-length cdna sequences |
| EP1169456B1 (en) | 1999-04-09 | 2012-07-11 | Intercell USA, Inc. | Recombinant production of Clostridium difficile Toxin A or Toxin B |
| WO2001073030A2 (en) | 2000-03-28 | 2001-10-04 | Diadexus, Inc. | Compositions and methods of diagnosing, monitoring, staging, imaging and treating colon cancer |
| JP6084631B2 (ja) * | 2011-12-08 | 2017-02-22 | ノバルティス アーゲー | Ｃｌｏｓｔｒｉｄｉｕｍｄｉｆｆｉｃｉｌｅ毒素ベースのワクチン |
-
2015
- 2015-06-25 LT LT15733404T patent/LT3160500T/lt unknown
- 2015-06-25 HU HUE15733404A patent/HUE045936T2/hu unknown
- 2015-06-25 WO PCT/EP2015/064324 patent/WO2015197737A1/en not_active Ceased
- 2015-06-25 PT PT157334046T patent/PT3160500T/pt unknown
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- 2015-06-25 BE BE2015/5390A patent/BE1022949B1/fr active
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2019
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Patent Citations (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2005004791A2 (en) * | 2002-11-08 | 2005-01-20 | President And Fellows Of Harvard College | Compounds and methods for the treatment and prevention of bacterial infection |
| WO2013112867A1 (en) * | 2012-01-27 | 2013-08-01 | Merck Sharp & Dohme Corp. | Vaccines against clostridium difficile comprising recombinant toxins |
| WO2014086787A1 (en) * | 2012-12-05 | 2014-06-12 | Glaxosmithkline Biologicals S.A. | Immunogenic composition |
| WO2014096393A1 (en) * | 2012-12-23 | 2014-06-26 | Glaxosmithkline Biologicals S.A. | Immunogenic composition comprising elements of c. difficile cdtb and/or cdta proteins |
Non-Patent Citations (4)
| Title |
|---|
| KAISER E. ET AL.: "Membrane Translocation of Binary Actin-ADP-Ribosylating Toxins from Clostridium difficile and Clostridium perfringens Is Facilitated by Cyclophilin A and Hsp90", INFECT. IMMUN., vol. 79, no. 10, October 2011 (2011-10-01), pages 3913 - 3921, XP055222411 * |
| NEUMEYER T. ET AL.: "Clostridium botulinum C2 Toxin: Identification of the binding site for chloroquine and related compounds and influence of the binding site on properties of the C2II channel", J. BIOL. CHEM., vol. 283, no. 7, 11 December 2007 (2007-12-11), pages 3904 - 3914, XP055207643 * |
| SRISUCHARITPANIT K. ET AL.: "Expression and purification of the active soluble form of binary toxin for structural analysis", PROT. EXPR. PURIF., vol. 82, no. 2, 20 February 2012 (2012-02-20), pages 368 - 372, XP028477061 * |
| SUNDRIYAL A. ET AL.: "Expression, purification and cell cytotoxicity of actin-modifying binary toxin from Clostridium difficile", PROT. EXPR. PURIF., vol. 74, no. 1, November 2010 (2010-11-01), pages 42 - 48, XP027226634 * |
Also Published As
| Publication number | Publication date |
|---|---|
| BR112016030096A8 (pt) | 2021-07-06 |
| BR112016030096B1 (pt) | 2023-10-03 |
| JP2020100625A (ja) | 2020-07-02 |
| BE1022949A1 (fr) | 2016-10-21 |
| EP3160500A1 (en) | 2017-05-03 |
| DK3160500T3 (da) | 2019-11-11 |
| WO2015197737A1 (en) | 2015-12-30 |
| JP6688233B2 (ja) | 2020-04-28 |
| LT3160500T (lt) | 2019-10-25 |
| PL3160500T3 (pl) | 2020-02-28 |
| HUE045936T2 (hu) | 2020-01-28 |
| HRP20191864T1 (hr) | 2020-01-10 |
| CN106536544A (zh) | 2017-03-22 |
| MX2016017094A (es) | 2017-05-03 |
| EP3636278A3 (en) | 2020-07-15 |
| EP3636278A2 (en) | 2020-04-15 |
| CN106536544B (zh) | 2020-04-07 |
| MX374380B (es) | 2025-03-06 |
| US20170218031A1 (en) | 2017-08-03 |
| BR112016030096A2 (pt) | 2017-08-22 |
| ES2749701T3 (es) | 2020-03-23 |
| CA2952118A1 (en) | 2015-12-30 |
| PT3160500T (pt) | 2019-11-11 |
| EP3160500B1 (en) | 2019-08-21 |
| JP2017520573A (ja) | 2017-07-27 |
| SI3160500T1 (sl) | 2019-11-29 |
| CY1122145T1 (el) | 2020-11-25 |
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