RU2322451C2 - Молекулярные миметики эпитопов менингококка в, которые вызывают выработку функционально активных антител - Google Patents
Молекулярные миметики эпитопов менингококка в, которые вызывают выработку функционально активных антител Download PDFInfo
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- RU2322451C2 RU2322451C2 RU2003133300/13A RU2003133300A RU2322451C2 RU 2322451 C2 RU2322451 C2 RU 2322451C2 RU 2003133300/13 A RU2003133300/13 A RU 2003133300/13A RU 2003133300 A RU2003133300 A RU 2003133300A RU 2322451 C2 RU2322451 C2 RU 2322451C2
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Applications Claiming Priority (4)
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| US28455401P | 2001-04-17 | 2001-04-17 | |
| US60/284,554 | 2001-04-17 | ||
| US32683801P | 2001-10-03 | 2001-10-03 | |
| US60/326,838 | 2001-10-03 |
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| RU2006146886/13A Division RU2355704C2 (ru) | 2001-04-17 | 2002-04-11 | Моноклональное антитело, направленное против gna33 пептида, и его применение |
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| RU2003133300A RU2003133300A (ru) | 2005-04-20 |
| RU2322451C2 true RU2322451C2 (ru) | 2008-04-20 |
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| EP (1) | EP1379272B1 (https=) |
| JP (3) | JP2004529643A (https=) |
| CN (1) | CN1306956C (https=) |
| AT (1) | ATE455793T1 (https=) |
| AU (1) | AU2002252638A1 (https=) |
| CA (1) | CA2439428C (https=) |
| DE (1) | DE60235155D1 (https=) |
| RU (1) | RU2322451C2 (https=) |
| WO (1) | WO2002083711A2 (https=) |
Families Citing this family (29)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CA2371994C (en) * | 1999-02-26 | 2010-09-28 | Guido Grandi | Enhancement of bactericidal activity of neisseria antigens with oligonucleotides containing cg motifs |
| US6977245B2 (en) | 1999-04-12 | 2005-12-20 | The United States Of America As Represented By The Department Of Health And Human Services | Oligodeoxynucleotide and its use to induce an immune response |
| NZ515935A (en) | 1999-05-19 | 2004-01-30 | Chiron S | Combination Neisserial compositions and vaccines for the prevention of infections due to Neisseria bacteria such as meningococcal meningitis |
| AU2001227889A1 (en) | 2000-01-14 | 2001-07-24 | The United States of America, represented by The Secretary, Department of Health & Human Services | Oligodeoxynucleotide and its use to induce an immune response |
| US7527797B1 (en) | 2000-09-01 | 2009-05-05 | The United States Of America As Represented By The Secretary Of The Department Of Health And Human Services | Vibrio cholerae 0139 conjugate vaccines |
| GB0024200D0 (en) * | 2000-10-03 | 2000-11-15 | Smithkline Beecham Sa | Component vaccine |
| US7666674B2 (en) | 2001-07-27 | 2010-02-23 | The United States Of America As Represented By The Secretary Of The Department Of Health And Human Services | Use of sterically stabilized cationic liposomes to efficiently deliver CPG oligonucleotides in vivo |
| WO2003020884A2 (en) * | 2001-08-14 | 2003-03-13 | The Government Of The United States Of America As Represented By The Secretary Of Health And Human Services | Method for rapid generation of mature dendritic cells |
| MX339524B (es) | 2001-10-11 | 2016-05-30 | Wyeth Corp | Composiciones inmunogenicas novedosas para la prevencion y tratamiento de enfermedad meningococica. |
| WO2003054161A2 (en) | 2001-12-20 | 2003-07-03 | The Government Of The United States Of America As Represented By The Secretary Of The Department Of Health And Human Services | USE OF CpG OLIGODEOXYNUCLEOTIDES TO INDUCE ANGIOGENESIS |
| US8466116B2 (en) | 2001-12-20 | 2013-06-18 | The Unites States Of America As Represented By The Secretary Of The Department Of Health And Human Services | Use of CpG oligodeoxynucleotides to induce epithelial cell growth |
| US8263091B2 (en) * | 2002-09-18 | 2012-09-11 | The United States Of America As Represented By The Secretary Of The Department Of Health And Human Services | Method of treating and preventing infections in immunocompromised subjects with immunostimulatory CpG oligonucleotides |
| WO2005023295A2 (en) * | 2003-09-10 | 2005-03-17 | De Staat Der Nederlanden, Vert. Door De Minister Van Vws | Naturally processed immunodominant peptides derived from neisseria meningitidis porin a protein and their use |
| US20070134263A1 (en) * | 2004-02-18 | 2007-06-14 | Anderson Annaliesa S | Polypeptides for inducing a protective immune response against staphyloococcus aureus |
| DE102004023906A1 (de) * | 2004-05-13 | 2005-12-22 | GESELLSCHAFT FüR BIOTECHNOLOGISCHE FORSCHUNG MBH (GBF) | Verfahren zur Herstellung von chemischen Mikroarrays |
| CA2631292C (en) * | 2005-11-30 | 2014-05-06 | International Institute Of Cancer Immunology, Inc. | Derivatised wt1 cancer antigen peptides and their use |
| GB0611914D0 (en) * | 2006-06-15 | 2006-07-26 | Teti Giuseppe | Peptides that mimic non-human cross-reactive protective epitopes of the group Bmeningococcal capsulsar polysaccharide |
| AR064642A1 (es) | 2006-12-22 | 2009-04-15 | Wyeth Corp | Polinucleotido vector que lo comprende celula recombinante que comprende el vector polipeptido , anticuerpo , composicion que comprende el polinucleotido , vector , celula recombinante polipeptido o anticuerpo , uso de la composicion y metodo para preparar la composicion misma y preparar una composi |
| US10527329B2 (en) | 2008-04-18 | 2020-01-07 | Denso Corporation | Ejector-type refrigeration cycle device |
| CN107913396B (zh) | 2010-08-23 | 2022-03-08 | 惠氏有限责任公司 | 脑膜炎萘瑟氏菌rLP2086抗原的稳定制剂 |
| AU2011300409B2 (en) | 2010-09-10 | 2015-03-26 | Wyeth Llc | Non-lipidated variants of Neisseria meningitidis ORF2086 antigens |
| US10598666B2 (en) * | 2012-03-08 | 2020-03-24 | Glaxosmithkline Biologicals Sa | In vitro potency assay for protein-based meningococcal vaccines |
| SA115360586B1 (ar) | 2012-03-09 | 2017-04-12 | فايزر انك | تركيبات لعلاج الالتهاب السحائي البكتيري وطرق لتحضيرها |
| MY198910A (en) | 2012-03-09 | 2023-10-02 | Pfizer | Neisseria meningitidis compositions and methods thereof |
| WO2014136064A2 (en) | 2013-03-08 | 2014-09-12 | Pfizer Inc. | Immunogenic fusion polypeptides |
| RU2662968C2 (ru) | 2013-09-08 | 2018-07-31 | Пфайзер Инк. | Иммуногенная композиция против neisseria meningitidis (варианты) |
| WO2016132294A1 (en) | 2015-02-19 | 2016-08-25 | Pfizer Inc. | Neisseria meningitidis compositions and methods thereof |
| AU2018215585B2 (en) | 2017-01-31 | 2022-03-17 | Pfizer Inc. | Neisseria meningitidis compositions and methods thereof |
| WO2021059181A1 (en) | 2019-09-27 | 2021-04-01 | Pfizer Inc. | Neisseria meningitidis compositions and methods thereof |
Citations (5)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| SU1708846A1 (ru) * | 1989-11-22 | 1992-01-30 | Научно-исследовательский институт вакцин и сывороток им.И.И.Мечникова | Штамм бактерий NeISSeRIa меNINGIтIDIS серогруппы В - продуцент капсульного полисахарида и полисахаридно-белкового комплекса |
| RU2068270C1 (ru) * | 1993-01-13 | 1996-10-27 | Научно-исследовательский институт вакцин и сывороток им.И.И.Мечникова | Антиген менингококков группы в |
| US5597572A (en) * | 1987-07-30 | 1997-01-28 | Centro Nacional De Biopreparados | Method of producing Neisseria meningitidis B vaccine, and vaccine produced by method |
| RU2105568C1 (ru) * | 1989-12-14 | 1998-02-27 | Нэшнл Рисерч Каунсл Оф Канада | Полисахарид neisseria meningitidis с модифицированной группой b, конъюгированный антиген, вакцина против менингита группы b и способ индукции ответа антител к менингиту группы b |
| WO2000066791A1 (en) * | 1999-04-30 | 2000-11-09 | Chiron Corporation | Neisseria genomic sequences and methods of their use |
Family Cites Families (17)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4356170A (en) * | 1981-05-27 | 1982-10-26 | Canadian Patents & Development Ltd. | Immunogenic polysaccharide-protein conjugates |
| JPH0720878B2 (ja) | 1983-11-21 | 1995-03-08 | ザ ウエルカム フアウンデ−シヨン リミテツド | 改善された複合体、それらの製造法および該複合体を含有する製剤 |
| US4727136A (en) * | 1985-10-01 | 1988-02-23 | Canadian Patents And Development Ltd. | Modified meningococcal group B polysaccharide for conjugate vaccine |
| US4970070A (en) * | 1986-02-07 | 1990-11-13 | Genetic Systems Corporation | Protective monoclonal antibody compositions for infections due to group B streptococcus |
| EP0449958B9 (en) | 1988-12-19 | 2003-05-28 | American Cyanamid Company | Meningococcal class 1 outer-membrane protein vaccine |
| US5128460A (en) * | 1989-04-04 | 1992-07-07 | Genelabs Incorporated | Recombinant trichosanthin and coding sequence |
| US5399346A (en) | 1989-06-14 | 1995-03-21 | The United States Of America As Represented By The Department Of Health And Human Services | Gene therapy |
| US5510264A (en) * | 1993-09-28 | 1996-04-23 | Insight Biotech Inc. | Antibodies which bind meningitis related homologous antigenic sequences |
| GB9422096D0 (en) | 1994-11-02 | 1994-12-21 | Biocine Spa | Combined meningitis vaccine |
| US5811102A (en) * | 1995-06-07 | 1998-09-22 | National Research Council Of Canada | Modified meningococcal polysaccharide conjugate vaccines |
| JP4150082B2 (ja) * | 1996-08-27 | 2008-09-17 | カイロン コーポレイション | 独特の髄膜炎菌性ｂエピトープを規定するモノクローナル抗体およびワクチン組成物の調製におけるそれらの使用 |
| ES2166097T5 (es) | 1996-08-27 | 2007-03-16 | Novartis Vaccines And Diagnostics, Inc. | Glicoconjugados de neisseria meningitidis de serogrupo b y procedimientos para usarlos. |
| ATE421527T1 (de) * | 1997-08-27 | 2009-02-15 | Novartis Vaccines & Diagnostic | Molekular-mimetika von meningokokkus b epitopen |
| EP2261338A3 (en) * | 1998-05-01 | 2012-01-04 | Novartis Vaccines and Diagnostics, Inc. | Neisseria meningitidis antigens and compositions |
| CA2371994C (en) | 1999-02-26 | 2010-09-28 | Guido Grandi | Enhancement of bactericidal activity of neisseria antigens with oligonucleotides containing cg motifs |
| WO2000066741A2 (en) * | 1999-04-30 | 2000-11-09 | Chiron S.P.A. | Conserved neisserial antigens |
| NZ521531A (en) * | 2000-02-28 | 2005-12-23 | Chiron S | Heterologous expression of neisserial proteins |
-
2002
- 2002-04-11 EP EP02721722A patent/EP1379272B1/en not_active Expired - Lifetime
- 2002-04-11 CA CA2439428A patent/CA2439428C/en not_active Expired - Fee Related
- 2002-04-11 DE DE60235155T patent/DE60235155D1/de not_active Expired - Lifetime
- 2002-04-11 US US10/121,456 patent/US7534444B2/en not_active Expired - Fee Related
- 2002-04-11 AT AT02721722T patent/ATE455793T1/de not_active IP Right Cessation
- 2002-04-11 CN CNB028081668A patent/CN1306956C/zh not_active Expired - Fee Related
- 2002-04-11 RU RU2003133300/13A patent/RU2322451C2/ru not_active IP Right Cessation
- 2002-04-11 WO PCT/US2002/011501 patent/WO2002083711A2/en not_active Ceased
- 2002-04-11 JP JP2002581466A patent/JP2004529643A/ja not_active Withdrawn
- 2002-04-11 AU AU2002252638A patent/AU2002252638A1/en not_active Abandoned
-
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- 2008-03-21 JP JP2008074708A patent/JP2008259503A/ja not_active Withdrawn
-
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- 2009-10-15 JP JP2009238784A patent/JP5215275B2/ja not_active Expired - Fee Related
Patent Citations (5)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US5597572A (en) * | 1987-07-30 | 1997-01-28 | Centro Nacional De Biopreparados | Method of producing Neisseria meningitidis B vaccine, and vaccine produced by method |
| SU1708846A1 (ru) * | 1989-11-22 | 1992-01-30 | Научно-исследовательский институт вакцин и сывороток им.И.И.Мечникова | Штамм бактерий NeISSeRIa меNINGIтIDIS серогруппы В - продуцент капсульного полисахарида и полисахаридно-белкового комплекса |
| RU2105568C1 (ru) * | 1989-12-14 | 1998-02-27 | Нэшнл Рисерч Каунсл Оф Канада | Полисахарид neisseria meningitidis с модифицированной группой b, конъюгированный антиген, вакцина против менингита группы b и способ индукции ответа антител к менингиту группы b |
| RU2068270C1 (ru) * | 1993-01-13 | 1996-10-27 | Научно-исследовательский институт вакцин и сывороток им.И.И.Мечникова | Антиген менингококков группы в |
| WO2000066791A1 (en) * | 1999-04-30 | 2000-11-09 | Chiron Corporation | Neisseria genomic sequences and methods of their use |
Non-Patent Citations (1)
| Title |
|---|
| М. PIZZA et al. Identification of Vaccine Candidates Against Serogroup В Meningococcus by Whole-Genome Sequencing, Science, 10.03.2000, vol.287, p.p.1816-1820. * |
Also Published As
| Publication number | Publication date |
|---|---|
| CN1602204A (zh) | 2005-03-30 |
| US20040013686A1 (en) | 2004-01-22 |
| CN1306956C (zh) | 2007-03-28 |
| JP5215275B2 (ja) | 2013-06-19 |
| WO2002083711A3 (en) | 2003-11-06 |
| WO2002083711A2 (en) | 2002-10-24 |
| EP1379272A4 (en) | 2005-12-14 |
| ATE455793T1 (de) | 2010-02-15 |
| JP2008259503A (ja) | 2008-10-30 |
| EP1379272B1 (en) | 2010-01-20 |
| DE60235155D1 (de) | 2010-03-11 |
| RU2003133300A (ru) | 2005-04-20 |
| JP2010011868A (ja) | 2010-01-21 |
| US7534444B2 (en) | 2009-05-19 |
| CA2439428C (en) | 2012-01-24 |
| EP1379272A2 (en) | 2004-01-14 |
| JP2004529643A (ja) | 2004-09-30 |
| CA2439428A1 (en) | 2002-10-24 |
| AU2002252638A1 (en) | 2002-10-28 |
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