DK175788B1 - Vaccine imod meningococcussygdomme, deri indgående komponenter, disses anvendelse og rekombinanter, som eksprimerer dem - Google Patents
Vaccine imod meningococcussygdomme, deri indgående komponenter, disses anvendelse og rekombinanter, som eksprimerer dem Download PDFInfo
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- DK175788B1 DK175788B1 DK199101174A DK117491A DK175788B1 DK 175788 B1 DK175788 B1 DK 175788B1 DK 199101174 A DK199101174 A DK 199101174A DK 117491 A DK117491 A DK 117491A DK 175788 B1 DK175788 B1 DK 175788B1
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- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K39/00—Medicinal preparations containing antigens or antibodies
- A61K39/02—Bacterial antigens
- A61K39/095—Neisseria
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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
- A61P31/04—Antibacterial agents
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/195—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria
- C07K14/22—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria from Neisseriaceae (F)
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/195—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria
- C07K14/24—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria from Enterobacteriaceae (F), e.g. Citrobacter, Serratia, Proteus, Providencia, Morganella, Yersinia
- C07K14/255—Salmonella (G)
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/12—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from bacteria
- C07K16/1203—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from bacteria from Gram-negative bacteria
- C07K16/1217—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from bacteria from Gram-negative bacteria from Neisseriaceae (F)
-
- 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
- A61K2039/60—Medicinal preparations containing antigens or antibodies characteristics by the carrier linked to the antigen
- A61K2039/6031—Proteins
- A61K2039/6037—Bacterial toxins, e.g. diphteria toxoid [DT], tetanus toxoid [TT]
-
- 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
- A61K2039/60—Medicinal preparations containing antigens or antibodies characteristics by the carrier linked to the antigen
- A61K2039/6031—Proteins
- A61K2039/6068—Other bacterial proteins, e.g. OMP
-
- 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
- A61K2039/60—Medicinal preparations containing antigens or antibodies characteristics by the carrier linked to the antigen
- A61K2039/6031—Proteins
- A61K2039/6081—Albumin; Keyhole limpet haemocyanin [KLH]
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/30—Immunoglobulins specific features characterized by aspects of specificity or valency
- C07K2317/34—Identification of a linear epitope shorter than 20 amino acid residues or of a conformational epitope defined by amino acid residues
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/01—Fusion polypeptide containing a localisation/targetting motif
- C07K2319/035—Fusion polypeptide containing a localisation/targetting motif containing a signal for targeting to the external surface of a cell, e.g. to the outer membrane of Gram negative bacteria, GPI- anchored eukaryote proteins
Landscapes
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Life Sciences & Earth Sciences (AREA)
- General Health & Medical Sciences (AREA)
- Medicinal Chemistry (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Molecular Biology (AREA)
- Genetics & Genomics (AREA)
- Biophysics (AREA)
- Biochemistry (AREA)
- Immunology (AREA)
- Veterinary Medicine (AREA)
- Public Health (AREA)
- Animal Behavior & Ethology (AREA)
- Pharmacology & Pharmacy (AREA)
- Microbiology (AREA)
- Mycology (AREA)
- Epidemiology (AREA)
- Gastroenterology & Hepatology (AREA)
- General Chemical & Material Sciences (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Oncology (AREA)
- Communicable Diseases (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
- Peptides Or Proteins (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Medicinal Preparation (AREA)
Applications Claiming Priority (8)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| NL8803111A NL8803111A (nl) | 1988-12-19 | 1988-12-19 | Multivalent meningococcen klasse i buitenmembraaneiwit vaccin. |
| NL8803111 | 1988-12-19 | ||
| NL8900036 | 1989-01-06 | ||
| NL8900036A NL8900036A (nl) | 1988-12-19 | 1989-01-06 | Multivalent meningococcen klasse 1 buitenmembraaneiwit vaccin. |
| NL8901612A NL8901612A (nl) | 1988-12-19 | 1989-06-26 | Multivalent meningococcen klasse i buitenmembraaneiwit vaccin. |
| NL8901612 | 1989-06-26 | ||
| PCT/US1989/005678 WO1990006696A2 (fr) | 1988-12-19 | 1989-12-19 | Vaccin meningocoque de la proteine de la membrane externe de la classe 1 |
| US8905678 | 1989-12-19 |
Publications (3)
| Publication Number | Publication Date |
|---|---|
| DK117491D0 DK117491D0 (da) | 1991-06-18 |
| DK117491A DK117491A (da) | 1991-08-15 |
| DK175788B1 true DK175788B1 (da) | 2005-02-21 |
Family
ID=27352237
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| DK199101174A DK175788B1 (da) | 1988-12-19 | 1991-06-18 | Vaccine imod meningococcussygdomme, deri indgående komponenter, disses anvendelse og rekombinanter, som eksprimerer dem |
Country Status (10)
| Country | Link |
|---|---|
| EP (1) | EP0449958B9 (fr) |
| JP (1) | JP3436756B2 (fr) |
| AT (1) | ATE120093T1 (fr) |
| AU (1) | AU640118B2 (fr) |
| DE (1) | DE68921895T3 (fr) |
| DK (1) | DK175788B1 (fr) |
| ES (1) | ES2070312T5 (fr) |
| FI (1) | FI113009B (fr) |
| NO (1) | NO305463B1 (fr) |
| WO (1) | WO1990006696A2 (fr) |
Families Citing this family (82)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US7118757B1 (en) | 1988-12-19 | 2006-10-10 | Wyeth Holdings Corporation | Meningococcal class 1 outer-membrane protein vaccine |
| NZ239643A (en) * | 1990-09-17 | 1996-05-28 | North American Vaccine Inc | Vaccine containing bacterial polysaccharide protein conjugate and adjuvant (c-nd-che-a-co-b-r) with a long chain alkyl group. |
| EP0967279B1 (fr) | 1992-03-02 | 2008-01-02 | Novartis Vaccines and Diagnostics S.r.l. | Cytotoxine d' Helicobacter pylori utile dans des vaccins et en diagnostique |
| NL9201716A (nl) * | 1992-10-02 | 1994-05-02 | Nederlanden Staat | Buitenmembraanvesikel dat voorzien is van een groep polypeptiden welke ten minste de immuunwerking van aan membraan gebonden buitenmembraaneiwitten (OMP's) hebben, werkwijze ter bereiding ervan alsmede een vaccin dat een dergelijk buitenmembraanvesikel omvat. |
| AU683030B2 (en) * | 1992-10-26 | 1997-10-30 | United States Of America, As Represented By The Secretary, Department Of Health And Human Services, The | Immunization against (neisseria gonorrhoeae) and (neisseria meningitidis) |
| DK0624376T3 (da) | 1993-05-13 | 2000-07-24 | American Cyanamid Co | Fremstilling og anvendelse af LOS-udtømte ydre membranproteiner af gram-negative cocci |
| US6153406A (en) * | 1993-07-23 | 2000-11-28 | North American Vaccine, Inc. | Method for the high level expression, purification and refolding of the outer membrane protein P2 from Haemophilus influenzae type B |
| US5439808A (en) * | 1993-07-23 | 1995-08-08 | North American Vaccine, Inc. | Method for the high level expression, purification and refolding of the outer membrane group B porin proteins from Neisseria meningitidis |
| US5747287A (en) * | 1995-04-28 | 1998-05-05 | North American Vaccine, Inc. | Method for the high level expression, purification and refolding of the outer membrane group B porin proteins from Neisseria meningitidis |
| US5811102A (en) | 1995-06-07 | 1998-09-22 | National Research Council Of Canada | Modified meningococcal polysaccharide conjugate vaccines |
| US20020028215A1 (en) | 1999-08-09 | 2002-03-07 | Jagath L. Kadurugamuwa | Novel vaccines and pharmaceutical compositions using membrane vesicles of microorganisms, and methods for preparing same |
| AU707131B2 (en) * | 1995-08-04 | 1999-07-01 | University Of Guelph | Novel vaccines and pharmaceutical compositions using membrane vesicles of microorganisms, and methods for preparing same |
| EA199800208A1 (ru) * | 1995-09-18 | 1998-10-29 | Юнайтед Стэйтс Арми Медикал Ресерч Материэл Комманд (Юсамрмк) | Усовершенствованные способы изготовления нековалентно комплексированных и поливалентных вакцин протеосомной подгруппы |
| WO1997025429A1 (fr) | 1996-01-04 | 1997-07-17 | Rican Limited | Bacterioferritine de helicobacter pilori |
| GB9611673D0 (en) * | 1996-06-05 | 1996-08-07 | Peptide Therapeutics Ltd | Meningococcal vaccine |
| WO1998008874A1 (fr) | 1996-08-27 | 1998-03-05 | Chiron Corporation | Anticorps monoclonaux definissant des epitopes meningococciques b et leurs utilisations dans la preparation de compositions vaccinales |
| US6558677B2 (en) * | 1996-10-15 | 2003-05-06 | Wendell D. Zollinger | Vaccine against gram negative bacteria |
| GB9701489D0 (en) | 1997-01-24 | 1997-03-12 | Auspharm Int Ltd | Antigen |
| EP2261346A3 (fr) | 1998-05-01 | 2012-01-04 | Novartis Vaccines and Diagnostics, Inc. | Antigènes de Neisseria meningitidis et compositions |
| JP5074644B2 (ja) * | 1998-05-29 | 2012-11-14 | ノバルティス バクシンズ アンド ダイアグノスティックス，インコーポレーテッド | 組合わせの髄膜炎菌ｂ／ｃワクチン |
| EP1741443B1 (fr) * | 1998-05-29 | 2014-05-21 | Novartis Vaccines and Diagnostics, Inc. | Vaccin B/C combiné contre la méningite |
| AU2003213540B8 (en) * | 1998-05-29 | 2006-09-28 | Novartis Vaccines And Diagnostic Inc. | Combination meningitidis B/C vaccines |
| GB9814902D0 (en) * | 1998-07-10 | 1998-09-09 | Univ Nottingham | Screening of neisserial vaccine candidates against pathogenic neisseria |
| US7252828B2 (en) | 1998-07-15 | 2007-08-07 | The Brigham And Women's Hospital, Inc. | Polysaccharide vaccine for staphylococcal infections |
| US6693186B2 (en) | 1998-09-01 | 2004-02-17 | Antex Biologics Inc | Neisseria meningitidis polypeptide, nucleic acid sequence and uses thereof |
| US6756493B1 (en) | 1998-09-01 | 2004-06-29 | Antex Biologics, Inc. | Nucleic acid sequence and uses thereof |
| GB9823978D0 (en) * | 1998-11-02 | 1998-12-30 | Microbiological Res Authority | Multicomponent meningococcal vaccine |
| US10967045B2 (en) | 1998-11-02 | 2021-04-06 | Secretary of State for Health and Social Care | Multicomponent meningococcal vaccine |
| US6797273B1 (en) | 1999-01-15 | 2004-09-28 | Glaxosmithkline Biologicals S.A. | Neisseria meningitidis antigen |
| EP2278007B1 (fr) | 1999-04-30 | 2014-04-16 | Novartis Vaccines and Diagnostics S.r.l. | Antigènes conservés de Neisseria |
| EP1069133A1 (fr) * | 1999-07-13 | 2001-01-17 | Institut National De La Sante Et De La Recherche Medicale (Inserm) | Compositions a base de Neisseria meningitidis et leur utilisation comme agents anti-infectieux |
| GB9916529D0 (en) * | 1999-07-14 | 1999-09-15 | Chiron Spa | Antigenic peptides |
| GB9918319D0 (en) * | 1999-08-03 | 1999-10-06 | Smithkline Beecham Biolog | Vaccine composition |
| CA2954411A1 (fr) * | 1999-10-29 | 2001-05-03 | Novartis Vaccines And Diagnostics S.R.L. | Peptides antigeniques de neisseria |
| DK1741784T3 (da) * | 1999-11-29 | 2010-05-25 | Novartis Vaccines & Diagnostic | 85kDa-antigen fra neisseria |
| GB9928196D0 (en) | 1999-11-29 | 2000-01-26 | Chiron Spa | Combinations of B, C and other antigens |
| DE60011560T2 (de) * | 1999-12-28 | 2005-08-18 | Akzo Nobel N.V. | Salmonella Impfstoff, der keinen Antikörper gegen Flagellin oder gegen Flagella induziert |
| DK1897555T3 (da) * | 2000-01-17 | 2014-10-13 | Novartis Vaccines & Diagnostic | Kompletteret OMV-vaccine mod meningococcus |
| BR0107857A (pt) * | 2000-01-25 | 2002-10-29 | Univ Queensland | Proteìnas compreendendo regiões conservadas de antìgeno nhha de superfìcie de neisseria meningitidis |
| DK1947187T5 (da) | 2000-02-28 | 2011-10-24 | Novartis Vaccines & Diagnostic | Hybrid ekspression af neisserial-proteiner |
| US6936261B2 (en) | 2000-07-27 | 2005-08-30 | Children's Hospital & Research Center At Oakland | Vaccines for broad spectrum protection against diseases caused by Neisseria meningitidis |
| GB0103170D0 (en) * | 2001-02-08 | 2001-03-28 | Smithkline Beecham Biolog | Vaccine composition |
| HU230490B1 (hu) * | 2001-01-23 | 2016-08-29 | Sanofi Pasteur Inc. | Multivalens, meningokokkusz-eredetű poliszaccharid és fehérje konjugátumát tartalmazó vakcina |
| AU2002252638A1 (en) | 2001-04-17 | 2002-10-28 | Children's Hospital Oakland Research Institute | Molecular mimetics of meningococcal b epitopes which elicit functionally active antibodies |
| GB0115176D0 (en) | 2001-06-20 | 2001-08-15 | Chiron Spa | Capular polysaccharide solubilisation and combination vaccines |
| GB0118249D0 (en) | 2001-07-26 | 2001-09-19 | Chiron Spa | Histidine vaccines |
| GB0121591D0 (en) | 2001-09-06 | 2001-10-24 | Chiron Spa | Hybrid and tandem expression of neisserial proteins |
| GB0130123D0 (en) * | 2001-12-17 | 2002-02-06 | Microbiological Res Agency | Outer membrane vesicle vaccine and its preparation |
| US7405039B2 (en) | 2002-02-07 | 2008-07-29 | Austin Health | Viral variants with altered susceptibility to nucleoside analogs and uses thereof |
| WO2003087351A1 (fr) | 2002-04-12 | 2003-10-23 | Melbourne Health | Variants viraux de l'hepatite b presentant une sensibilite reduite aux analogues de nucleoside et utilisations desdits variants |
| GB0220194D0 (en) | 2002-08-30 | 2002-10-09 | Chiron Spa | Improved vesicles |
| HUE031886T2 (en) | 2002-10-11 | 2017-08-28 | Glaxosmithkline Biologicals Sa | Polypeptide vaccines for extensive protection against hypervirulent meningococcal lines |
| AU2003290867A1 (en) | 2002-11-12 | 2004-06-03 | The Brigham And Women's Hospital, Inc. | Methods and products for treating staphylococcal infections |
| EP1565478B1 (fr) | 2002-11-12 | 2017-08-02 | The Brigham And Women's Hospital, Inc. | Vaccin a base de polysaccharide destine a combattre les infections aux staphylocoques |
| ATE466875T1 (de) | 2002-11-15 | 2010-05-15 | Novartis Vaccines & Diagnostic | Unerwartete oberflächenproteine in neisseria meningitidis |
| GB0227346D0 (en) | 2002-11-22 | 2002-12-31 | Chiron Spa | 741 |
| CA2514328C (fr) | 2003-01-30 | 2020-01-14 | Chiron Srl | Vaccins injectables contre les multiples serogroupes du meningocoque |
| GB0323103D0 (en) | 2003-10-02 | 2003-11-05 | Chiron Srl | De-acetylated saccharides |
| WO2005042564A1 (fr) * | 2003-10-20 | 2005-05-12 | Sidney Kimmel Cancer Center | Proteines de fusion flagelline, comme adjuvants ou vaccins, et procedes d'utilisation |
| US7786255B2 (en) | 2004-04-21 | 2010-08-31 | The Bringham and Women's Hospital, Inc. | Poly-N-acetyl glucosamine (PNAG/dPNAG)-binding peptides and methods of use thereof |
| GB0408977D0 (en) | 2004-04-22 | 2004-05-26 | Chiron Srl | Immunising against meningococcal serogroup Y using proteins |
| GB0424092D0 (en) | 2004-10-29 | 2004-12-01 | Chiron Srl | Immunogenic bacterial vesicles with outer membrane proteins |
| AU2006208208B2 (en) | 2005-01-27 | 2011-05-19 | Children's Hospital & Research Center At Oakland | GNA1870-based vesicle vaccines for broad spectrum protection against diseases caused by Neisseria meningitidis |
| AU2006230802A1 (en) | 2005-04-08 | 2006-10-12 | Austin Health | Variants of hepatitis B virus with resistance to anti-viral nucleoside agents and applications thereof |
| WO2006105597A1 (fr) | 2005-04-08 | 2006-10-12 | Melbourne Health | Variantes du virus de l’hepatite b presentant une resistance aux agents de nucleotide anti-virale et application de ces variantes |
| GB0524066D0 (en) | 2005-11-25 | 2006-01-04 | Chiron Srl | 741 ii |
| 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 |
| AU2009215364B2 (en) | 2008-02-21 | 2014-09-18 | Glaxosmithkline Biologicals S.A. | Meningococcal fHBP polypeptides |
| GB0809659D0 (en) * | 2008-05-28 | 2008-07-02 | Univ Nottingham | Polypeptides |
| NZ589812A (en) | 2008-05-30 | 2012-08-31 | U S A As Represented By The Secretary Of The Army On Behalf Of Walter Reed Army Inst Of Res | Meningococcal multivalent native outer membrane vesicle vaccine, methods of making and use thereof |
| KR101573648B1 (ko) | 2008-07-21 | 2015-12-01 | 더 브리검 앤드 우먼즈 하스피털, 인크. | 합성 베타-1,6 글루코사민 올리고당에 관한 방법 및 조성물 |
| WO2010027499A2 (fr) * | 2008-09-05 | 2010-03-11 | University Of Massachusetts Medical School | Procédés, compositions et vaccins se rapportant à des anticorps anti- neisseria meningitidis |
| US20110076300A1 (en) | 2009-08-27 | 2011-03-31 | Mariagrazia Pizza | Hybrid Polypeptides Including Meningococcal fHBP Sequences |
| CA2776004A1 (fr) | 2009-09-30 | 2011-04-07 | Novartis Ag | Expression de polypeptides fhbp meningococciques |
| US20130022633A1 (en) | 2009-10-27 | 2013-01-24 | University Of Florence | MENINGOCOCCAL fHBP POLYPEPTIDES |
| US9259462B2 (en) | 2010-09-10 | 2016-02-16 | Glaxosmithkline Biologicals Sa | Developments in meningococcal outer membrane vesicles |
| JP2012090571A (ja) * | 2010-10-27 | 2012-05-17 | Sekisui Chem Co Ltd | 動物の免疫方法、免疫用組成物、抗体の製造方法、並びに、ハイブリドーマの製造方法 |
| RU2644340C2 (ru) | 2012-06-14 | 2018-02-08 | Новартис Аг | Вакцины для менингококка серогруппы х |
| US10392424B2 (en) | 2014-02-28 | 2019-08-27 | Glaxosmithkline Biologicals Sa | Modified meningococcal fHbp polypeptides |
| EP3132020B1 (fr) * | 2014-04-17 | 2019-11-27 | Corning Inc. | Récipient pour la culture cellulaire et son utilisation |
| KR20170031251A (ko) * | 2014-07-30 | 2017-03-20 | 클리브랜드 바이오랩스, 아이엔씨. | 플라젤린 조성물 및 용도 |
| US20240325517A1 (en) * | 2020-09-15 | 2024-10-03 | The University Of Montana | Compositions and methods targeting filamentous bacteriophage |
Family Cites Families (6)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4673574A (en) * | 1981-08-31 | 1987-06-16 | Anderson Porter W | Immunogenic conjugates |
| WO1983003354A1 (fr) * | 1982-03-30 | 1983-10-13 | Us Army | Vaccin anti-neisseria gonorrhoeae |
| EP0145359B1 (fr) * | 1983-11-21 | 1991-01-16 | The Wellcome Foundation Limited | Complexes, leur procédé de préparation et formulations les contenant |
| US4601903A (en) * | 1985-05-01 | 1986-07-22 | The United States Of America As Represented By The Department Of Health And Human Services | Vaccine against Neisseria meningitidis Group B serotype 2 invasive disease |
| JPH01125328A (ja) * | 1987-07-30 | 1989-05-17 | Centro Natl De Biopreparados | 髄膜炎菌ワクチン |
| AU637049B2 (en) * | 1988-05-05 | 1993-05-20 | American Cyanamid Company | Recombinant flagellin vaccines |
-
1989
- 1989-12-19 AT AT90901397T patent/ATE120093T1/de not_active IP Right Cessation
- 1989-12-19 WO PCT/US1989/005678 patent/WO1990006696A2/fr active IP Right Grant
- 1989-12-19 AU AU48219/90A patent/AU640118B2/en not_active Expired
- 1989-12-19 ES ES90901397T patent/ES2070312T5/es not_active Expired - Lifetime
- 1989-12-19 EP EP90901397A patent/EP0449958B9/fr not_active Expired - Lifetime
- 1989-12-19 JP JP50166290A patent/JP3436756B2/ja not_active Expired - Lifetime
- 1989-12-19 DE DE68921895T patent/DE68921895T3/de not_active Expired - Lifetime
-
1991
- 1991-06-18 DK DK199101174A patent/DK175788B1/da not_active IP Right Cessation
- 1991-06-18 NO NO912369A patent/NO305463B1/no not_active IP Right Cessation
- 1991-06-18 FI FI912965A patent/FI113009B/fi active
Also Published As
| Publication number | Publication date |
|---|---|
| ES2070312T3 (es) | 1995-06-01 |
| ATE120093T1 (de) | 1995-04-15 |
| DE68921895T3 (de) | 2003-05-22 |
| DK117491D0 (da) | 1991-06-18 |
| DK117491A (da) | 1991-08-15 |
| FI113009B (fi) | 2004-02-27 |
| NO912369D0 (no) | 1991-06-18 |
| EP0449958B9 (fr) | 2003-05-28 |
| ES2070312T5 (es) | 2003-05-16 |
| AU4821990A (en) | 1990-07-10 |
| JP3436756B2 (ja) | 2003-08-18 |
| NO305463B1 (no) | 1999-06-07 |
| FI912965A0 (fi) | 1991-06-18 |
| NO912369L (no) | 1991-08-06 |
| EP0449958B2 (fr) | 2002-11-13 |
| WO1990006696A3 (fr) | 1990-07-12 |
| DE68921895D1 (de) | 1995-04-27 |
| WO1990006696A2 (fr) | 1990-06-28 |
| EP0449958B1 (fr) | 1995-03-22 |
| DE68921895T2 (de) | 1995-09-07 |
| EP0449958A1 (fr) | 1991-10-09 |
| JPH06503465A (ja) | 1994-04-21 |
| AU640118B2 (en) | 1993-08-19 |
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| PUP | Patent expired |