NO330491B1 - Rekombinant polynukleotid som koder for et polypeptid, eller antigent fragment derav, som indusere en immunrespons som er spesifikk for gruppe B streptococcus, vektor omfattende polynukleotidet, vertscelle transfektert med vektoren, fremgangsmate for fremstilling av polypeptidet, isolert polypeptid, vaksinesammensetning som omfatter polypeptidet,anvendelse av polypeptid ifolge oppfinnelsen for fremstilling av en vaksinesammensetning, isolert antistoff, eller antigenbindende fragment derav, som spesifikt binder til polypeptidet, fremgangsmate for pavisning av gruppe B Streptococcus i en biologisk prove, fremgangsmate for pavisning av et antistoff som spesifikt binder til polypeptidet. - Google Patents
Rekombinant polynukleotid som koder for et polypeptid, eller antigent fragment derav, som indusere en immunrespons som er spesifikk for gruppe B streptococcus, vektor omfattende polynukleotidet, vertscelle transfektert med vektoren, fremgangsmate for fremstilling av polypeptidet, isolert polypeptid, vaksinesammensetning som omfatter polypeptidet,anvendelse av polypeptid ifolge oppfinnelsen for fremstilling av en vaksinesammensetning, isolert antistoff, eller antigenbindende fragment derav, som spesifikt binder til polypeptidet, fremgangsmate for pavisning av gruppe B Streptococcus i en biologisk prove, fremgangsmate for pavisning av et antistoff som spesifikt binder til polypeptidet. Download PDFInfo
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- NO330491B1 NO330491B1 NO20004161A NO20004161A NO330491B1 NO 330491 B1 NO330491 B1 NO 330491B1 NO 20004161 A NO20004161 A NO 20004161A NO 20004161 A NO20004161 A NO 20004161A NO 330491 B1 NO330491 B1 NO 330491B1
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- polypeptide
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- amino acid
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- C—CHEMISTRY; METALLURGY
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- C07K—PEPTIDES
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- C07K14/195—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria
- C07K14/315—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria from Streptococcus (G), e.g. Enterococci
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- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P31/00—Antiinfectives, i.e. antibiotics, antiseptics, chemotherapeutics
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Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US7542598P | 1998-02-20 | 1998-02-20 | |
| PCT/CA1999/000114 WO1999042588A2 (en) | 1998-02-20 | 1999-02-17 | Group b streptococcus antigens |
Publications (3)
| Publication Number | Publication Date |
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| NO20004161D0 NO20004161D0 (no) | 2000-08-18 |
| NO20004161L NO20004161L (no) | 2000-10-19 |
| NO330491B1 true NO330491B1 (no) | 2011-05-02 |
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| NO20004161A NO330491B1 (no) | 1998-02-20 | 2000-08-18 | Rekombinant polynukleotid som koder for et polypeptid, eller antigent fragment derav, som indusere en immunrespons som er spesifikk for gruppe B streptococcus, vektor omfattende polynukleotidet, vertscelle transfektert med vektoren, fremgangsmate for fremstilling av polypeptidet, isolert polypeptid, vaksinesammensetning som omfatter polypeptidet,anvendelse av polypeptid ifolge oppfinnelsen for fremstilling av en vaksinesammensetning, isolert antistoff, eller antigenbindende fragment derav, som spesifikt binder til polypeptidet, fremgangsmate for pavisning av gruppe B Streptococcus i en biologisk prove, fremgangsmate for pavisning av et antistoff som spesifikt binder til polypeptidet. |
| NO20101682A NO20101682L (no) | 1998-02-20 | 2010-11-30 | Gruppe B streptococcus antigener |
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| NO20101682A NO20101682L (no) | 1998-02-20 | 2010-11-30 | Gruppe B streptococcus antigener |
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| EP (3) | EP1054971B1 (de) |
| JP (2) | JP4637350B2 (de) |
| KR (1) | KR100771148B1 (de) |
| CN (2) | CN1944652A (de) |
| AP (1) | AP2000001886A0 (de) |
| AT (1) | ATE347600T1 (de) |
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| ID (1) | ID27482A (de) |
| IL (3) | IL137921A0 (de) |
| NO (2) | NO330491B1 (de) |
| NZ (1) | NZ529854A (de) |
| OA (1) | OA11686A (de) |
| TR (1) | TR200002437T2 (de) |
| WO (1) | WO1999042588A2 (de) |
| ZA (1) | ZA991325B (de) |
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| TR200002437T2 (tr) * | 1998-02-20 | 2000-11-21 | Biochem Pharma Inc. | B grubu streptococcus antijenleri. |
| US7098182B2 (en) | 1998-07-27 | 2006-08-29 | Microbial Technics Limited | Nucleic acids and proteins from group B streptococcus |
| WO2000006736A2 (en) * | 1998-07-27 | 2000-02-10 | Microbial Technics Limited | Nucleic acids and proteins from group b streptococcus |
| GB0105922D0 (en) * | 2001-03-09 | 2001-04-25 | Microscience Ltd | Genes and proteins, and their use |
| US6890539B2 (en) | 1998-12-22 | 2005-05-10 | Microscience, Ltd. | Genes and proteins, and their use |
| ES2281977T3 (es) | 1998-12-22 | 2007-10-01 | Microscience Limited | Proteinas de estreptococo del grupo b y su utilizacion. |
| US7128918B1 (en) | 1998-12-23 | 2006-10-31 | Id Biomedical Corporation | Streptococcus antigens |
| US6833356B1 (en) | 1999-08-25 | 2004-12-21 | Medimmune, Inc. | Pneumococcal protein homologs and fragments for vaccines |
| CA2382795A1 (en) * | 1999-08-25 | 2001-03-01 | Medimmune, Inc. | Homologs of a pneumococcal protein and fragments for vaccines |
| CA2411919C (en) | 2000-06-12 | 2012-07-31 | University Of Saskatchewan | Immunization of dairy cattle with chimeric gapc protein against streptococcus infection |
| EP1332155B1 (de) * | 2000-06-12 | 2006-10-25 | University of Saskatchewan | Immunisation von milchvieh mit gapc protein gegen streptococcus infektion |
| US6833134B2 (en) | 2000-06-12 | 2004-12-21 | University Of Saskacthewan | Immunization of dairy cattle with GapC protein against Streptococcus infection |
| US6866855B2 (en) | 2000-06-12 | 2005-03-15 | University Of Saskatchewan | Immunization of dairy cattle with GapC protein against Streptococcus infection |
| EP1734050A3 (de) * | 2000-06-12 | 2012-12-05 | University Of Saskatchewan | Immunisation von Milchvieh mit GapC Protein gegen Streptococcusinfektion |
| ES2382893T3 (es) * | 2000-10-13 | 2012-06-14 | Id Biomedical Corporation | Antígenos BVH-A2 y BVH-3 de streptococcus del grupo B |
| MX357775B (es) | 2000-10-27 | 2018-07-20 | J Craig Venter Inst Inc | Acidos nucleicos y proteinas de los grupos a y b de estreptococos. |
| EP1343895B1 (de) * | 2000-12-21 | 2008-06-18 | ID Biomedical Corporation | Antigene aus streptococcus pyogenes und zugehörige dna-fragmente |
| FR2824074A1 (fr) * | 2001-04-26 | 2002-10-31 | Pasteur Institut | Sequence du genome streptococcus agalactiae, application au developpement de vaccins, d'outils de diagnostic, et a l'identification de cibles therapeutiques |
| WO2003068813A2 (en) * | 2002-02-11 | 2003-08-21 | Shire Biochem Inc | Group b streptococcus antigen |
| GB0210128D0 (en) * | 2002-05-02 | 2002-06-12 | Chiron Spa | Nucleic acids and proteins from streptococcus groups A & B |
| EP1648500B1 (de) | 2003-07-31 | 2014-07-09 | Novartis Vaccines and Diagnostics, Inc. | Immunogene zusammensetzungen für streptococcus pyogenes |
| US8945589B2 (en) | 2003-09-15 | 2015-02-03 | Novartis Vaccines And Diagnostics, Srl | Immunogenic compositions for Streptococcus agalactiae |
| US20060165716A1 (en) | 2004-07-29 | 2006-07-27 | Telford John L | Immunogenic compositions for gram positive bacteria such as streptococcus agalactiae |
| EP1807446A2 (de) | 2004-10-08 | 2007-07-18 | Novartis Vaccines and Diagnostics, Inc. | Immunogene und therapeutische zusammensetzungen für pyogene streptokokken |
| JP2008530021A (ja) * | 2005-02-08 | 2008-08-07 | アイディー バイオメディカル コーポレイション オブ ケベック シー．オー．ビー． アズ グラクソスミスクライン バイオロジカルズ ノース アメリカ | 医薬組成物 |
| GB0605247D0 (en) * | 2006-03-15 | 2006-04-26 | Chiron Srl | Compositions and methods for immunisation |
| AU2008299376B2 (en) | 2007-09-12 | 2013-02-28 | Glaxosmithkline Biologicals S.A. | GAS57 mutant antigens and GAS57 antibodies |
| KR101773114B1 (ko) | 2007-12-21 | 2017-08-30 | 노파르티스 아게 | 스트렙토라이신 ｏ의 돌연변이 형태 |
| CN102304185A (zh) * | 2011-09-02 | 2012-01-04 | 黑龙江八一农垦大学 | 预防奶牛乳房炎的融合蛋白sip-trap及制备方法和应用 |
| EP2949340A1 (de) * | 2014-05-30 | 2015-12-02 | IDT Biologika GmbH | Impfstoffzusammensetzung gegen Streptococcus Suis-Infektion |
Family Cites Families (19)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4431739A (en) | 1979-11-05 | 1984-02-14 | Genentech, Inc. | Transformant bacterial culture capable of expressing heterologous protein |
| US4425437A (en) | 1979-11-05 | 1984-01-10 | Genentech, Inc. | Microbial polypeptide expression vehicle |
| US5302386A (en) * | 1986-04-16 | 1994-04-12 | Brigham And Women's Hospital, Inc. | Bacterial antigens, antibodies, vaccines and methods of manufacture |
| US5472696A (en) * | 1988-02-26 | 1995-12-05 | Univ. Of Florida Research Foundation, Inc. | Antigen of group B streptococci |
| US5648241A (en) * | 1989-09-15 | 1997-07-15 | The General Hospital Corporation | Conjugate vaccine against group B streptococcus |
| US5679768A (en) * | 1991-02-15 | 1997-10-21 | Uab Research Foundation | Epitopic regions of pneumococcal surface protein A |
| US5225331A (en) * | 1991-04-25 | 1993-07-06 | National Research Council Of Canada | Immunoassay for detecting group b streptococcus |
| SG47049A1 (en) | 1993-03-19 | 1998-03-20 | Gunnar Lindahl | Protein rib a cell surface protein that confers immunity to manu strains of the group b strepto-ccus process for purification of the protein reagent kit |
| US5595740A (en) * | 1994-05-16 | 1997-01-21 | University Of Florida | Cloning of non-IgA FC binding forms of the group B streptococcal beta antigens |
| AU706304B2 (en) * | 1994-11-01 | 1999-06-10 | Kirin Pharma Kabushiki Kaisha | Peptide sequence that forms mucin sugar chain and technique for modifying protein to be linked with mucin sugar chain |
| EP0942983B2 (de) * | 1996-10-31 | 2014-09-10 | Human Genome Sciences, Inc. | Streptococcus pneumoniae antigene und impfstoffe |
| TR200002437T2 (tr) * | 1998-02-20 | 2000-11-21 | Biochem Pharma Inc. | B grubu streptococcus antijenleri. |
| US6248329B1 (en) * | 1998-06-01 | 2001-06-19 | Ramaswamy Chandrashekar | Parasitic helminth cuticlin nucleic acid molecules and uses thereof |
| WO2000006736A2 (en) | 1998-07-27 | 2000-02-10 | Microbial Technics Limited | Nucleic acids and proteins from group b streptococcus |
| AU776828B2 (en) | 1998-12-21 | 2004-09-23 | Medimmune, Llc | Streptococcus pneumoniae proteins and immunogenic fragments for vaccines |
| BR9916477A (pt) | 1998-12-23 | 2004-06-22 | Shire Biochem Inc | Polinucleotìdeo isolado, polinucleotìdeo quimérico, composição de vacina e uso desta composição compreendendo os polinucleotìdeos |
| US7128918B1 (en) * | 1998-12-23 | 2006-10-31 | Id Biomedical Corporation | Streptococcus antigens |
| GB9921125D0 (en) | 1999-09-07 | 1999-11-10 | Microbial Technics Limited | Proteins |
| WO2003068813A2 (en) | 2002-02-11 | 2003-08-21 | Shire Biochem Inc | Group b streptococcus antigen |
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