BE1000811A4 - Anticorps monoclonaux, peptides et compositions les contenant, destinees au diagnostic et au traitement des infections par le virus hiv. - Google Patents
Anticorps monoclonaux, peptides et compositions les contenant, destinees au diagnostic et au traitement des infections par le virus hiv. Download PDFInfo
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- BE1000811A4 BE1000811A4 BE8700922A BE8700922A BE1000811A4 BE 1000811 A4 BE1000811 A4 BE 1000811A4 BE 8700922 A BE8700922 A BE 8700922A BE 8700922 A BE8700922 A BE 8700922A BE 1000811 A4 BE1000811 A4 BE 1000811A4
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- Prior art keywords
- hiv
- peptide
- gpl10
- sep
- peptides
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Classifications
-
- F—MECHANICAL ENGINEERING; LIGHTING; HEATING; WEAPONS; BLASTING
- F04—POSITIVE - DISPLACEMENT MACHINES FOR LIQUIDS; PUMPS FOR LIQUIDS OR ELASTIC FLUIDS
- F04B—POSITIVE-DISPLACEMENT MACHINES FOR LIQUIDS; PUMPS
- F04B25/00—Multi-stage pumps
-
- 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
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/08—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from viruses
- C07K16/10—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from viruses from RNA viruses
- C07K16/1036—Retroviridae, e.g. leukemia viruses
- C07K16/1045—Lentiviridae, e.g. HIV, FIV, SIV
- C07K16/1054—Lentiviridae, e.g. HIV, FIV, SIV gag-pol, e.g. p17, p24
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Q—MEASURING OR TESTING PROCESSES INVOLVING ENZYMES, NUCLEIC ACIDS OR MICROORGANISMS; COMPOSITIONS OR TEST PAPERS THEREFOR; PROCESSES OF PREPARING SUCH COMPOSITIONS; CONDITION-RESPONSIVE CONTROL IN MICROBIOLOGICAL OR ENZYMOLOGICAL PROCESSES
- C12Q1/00—Measuring or testing processes involving enzymes, nucleic acids or microorganisms; Compositions therefor; Processes of preparing such compositions
- C12Q1/70—Measuring or testing processes involving enzymes, nucleic acids or microorganisms; Compositions therefor; Processes of preparing such compositions involving virus or bacteriophage
- C12Q1/701—Specific hybridization probes
- C12Q1/702—Specific hybridization probes for retroviruses
- C12Q1/703—Viruses associated with AIDS
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
-
- 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
-
- 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
- C12N2740/16211—Human Immunodeficiency Virus, HIV concerning HIV gagpol
- C12N2740/16222—New viral proteins or individual genes, new structural or functional aspects of known viral proteins or genes
Landscapes
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Organic Chemistry (AREA)
- Virology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Engineering & Computer Science (AREA)
- Immunology (AREA)
- Biochemistry (AREA)
- Biophysics (AREA)
- General Health & Medical Sciences (AREA)
- Genetics & Genomics (AREA)
- Molecular Biology (AREA)
- General Engineering & Computer Science (AREA)
- Medicinal Chemistry (AREA)
- Zoology (AREA)
- AIDS & HIV (AREA)
- Wood Science & Technology (AREA)
- Analytical Chemistry (AREA)
- Physics & Mathematics (AREA)
- Biotechnology (AREA)
- Microbiology (AREA)
- Gastroenterology & Hepatology (AREA)
- Hematology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Oncology (AREA)
- Mechanical Engineering (AREA)
- Peptides Or Proteins (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US89827386A | 1986-08-20 | 1986-08-20 | |
| US4502687A | 1987-05-01 | 1987-05-01 | |
| US6799687A | 1987-06-29 | 1987-06-29 |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| BE1000811A4 true BE1000811A4 (fr) | 1989-04-11 |
Family
ID=27366600
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| BE8700922A BE1000811A4 (fr) | 1986-08-20 | 1987-08-19 | Anticorps monoclonaux, peptides et compositions les contenant, destinees au diagnostic et au traitement des infections par le virus hiv. |
Country Status (28)
| Country | Link |
|---|---|
| JP (1) | JPS6485928A (da) |
| KR (1) | KR920008744B1 (da) |
| AT (1) | AT398080B (da) |
| AU (1) | AU616156B2 (da) |
| BE (1) | BE1000811A4 (da) |
| CH (1) | CH675728A5 (da) |
| CS (1) | CS275838B6 (da) |
| DE (1) | DE3727703A1 (da) |
| DK (1) | DK433087A (da) |
| ES (1) | ES2010727A6 (da) |
| FI (1) | FI873553A (da) |
| FR (1) | FR2603107B1 (da) |
| GB (1) | GB2196634B (da) |
| GR (1) | GR871298B (da) |
| HU (1) | HU214439B (da) |
| IE (1) | IE60671B1 (da) |
| IL (1) | IL83580A (da) |
| IT (1) | IT1222518B (da) |
| LU (1) | LU86972A1 (da) |
| NL (1) | NL8701950A (da) |
| NO (2) | NO300462B1 (da) |
| NZ (1) | NZ221440A (da) |
| OA (1) | OA08652A (da) |
| PL (1) | PL155084B1 (da) |
| PT (1) | PT85567B (da) |
| SE (1) | SE506025C2 (da) |
| YU (1) | YU152587A (da) |
| ZW (1) | ZW15487A1 (da) |
Families Citing this family (23)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| AP96A (en) * | 1986-06-03 | 1990-08-12 | The Usa Dept Of Commerce | Small peptides which inhibit binding to T-4 receptors and act as immunogens. |
| AU625720B2 (en) * | 1987-05-01 | 1992-07-16 | Genetic Systems Corporation | Monoclonal antibodies to specific antigenic regions of the human immunodeficiency virus and methods for use |
| US6657050B1 (en) | 1987-05-29 | 2003-12-02 | Tanox, Inc. | Chimeric viral-neutralizing immunoglobulins |
| EP0366718B1 (en) * | 1987-05-29 | 1995-05-10 | Tanox Biosystems, Inc. | Monoclonal antibodies neutralizing hiv-1 |
| US5981278A (en) * | 1987-05-29 | 1999-11-09 | Tanox, Inc. | Chimeric monoclonal antibodies which neutralize HIV-1 infection and their applications in therapy and prevention for AIDS |
| US5834599A (en) * | 1987-05-29 | 1998-11-10 | Tanox Biosystems, Inc. | Immunoconjugates which neutralize HIV-1 infection |
| ATE138077T1 (de) * | 1988-01-26 | 1996-06-15 | Us Health | Synthetisches antigen zum bewirken einer anti-hiv-reaktion |
| CA1341285C (en) * | 1988-02-12 | 2001-08-14 | Chang Yi Wang | Synthetic peptides for the detection of antibodies to hiv gp120 envelope protein for diagnosis of aids and pre-aids conditions and as vaccines |
| IL90048A0 (en) * | 1988-04-25 | 1989-12-15 | Merck & Co Inc | Recombinant gag precursor of hiv,its preparation and its use as aids vaccine |
| US5562905A (en) * | 1988-04-26 | 1996-10-08 | E. I. Du Pont De Nemours And Company | Human immunodeficiency virus (hiv) env-coded peptide capable of eliciting hiv-inhibiting antibodies in mammals |
| EP0339504A3 (en) * | 1988-04-26 | 1990-09-12 | The Du Pont Merck Pharmaceutical Company | Human immunodeficiency virus (hiv) env-coded peptide capable of eliciting hiv-inhibiting antibodies in mammals |
| FR2632310B1 (fr) * | 1988-06-06 | 1992-04-10 | Pasteur Institut | Peptides ayant des proprietes protectrices d'un virus pathogene du type hiv dans des cellules sensibles |
| AU640619B2 (en) * | 1988-10-03 | 1993-09-02 | Repligen Corporation | Hiv proteins and peptides useful in the diagnosis, prophylaxis or therapy of aids |
| EP0421626A1 (en) * | 1989-09-19 | 1991-04-10 | Merck & Co. Inc. | Vaccine for aids and hepatitis B |
| SE9000333D0 (sv) * | 1990-01-31 | 1990-01-31 | Britta Wahren | Monoklonal antikropp |
| SE468168B (sv) * | 1990-02-20 | 1992-11-16 | Replico Medical Ab | Hiv-1, p24 peptider, diagnostiska antigener och foerfarande foer saerskiljande diagnostik av preliminaert hiv-1 positiva serumprov |
| JPH03271233A (ja) * | 1990-03-19 | 1991-12-03 | Inst Pasteur | ウイルスエンベロープ糖タンパク質及びその糖タンパク質の中和エピトープに対応するペプチドの間の相乗作用による、ウイルス性感染に対する防御の誘発 |
| CA2047042A1 (en) * | 1990-07-19 | 1992-01-20 | John Hannah | Cyclic hiv principal neutralizing determinant peptides |
| CA2047078A1 (en) * | 1990-07-19 | 1992-01-20 | Steven S. Bondy | Cyclic hiv principal neutralizing determinant peptides |
| JPH05310785A (ja) * | 1991-09-30 | 1993-11-22 | Nitto Denko Corp | Ｈｉｖ関連環状ペプチドおよびこれを固定化した吸着体 |
| DK0635027T3 (da) * | 1992-03-27 | 2000-10-02 | Advanced Immunit T Inc | Peptid T og beslægtede peptider til behandling af inflammation, herunder dissemineret sclerose |
| KR20140041943A (ko) | 2005-12-09 | 2014-04-04 | 벡투스 바이오시스템즈 피티와이 리미티드 | Ｖｉｐ 단편 및 사용 방법 |
| US8253311B2 (en) | 2008-09-02 | 2012-08-28 | Ngk Spark Plug Co., Ltd | Spark plug |
Citations (8)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO1986002383A1 (en) * | 1984-10-18 | 1986-04-24 | Institut Pasteur | Envelope antigens of lymphadenopathy associated virus and their applications |
| EP0185444A2 (en) * | 1984-10-10 | 1986-06-25 | Centocor, Inc. | Cloning and expression of HTLV-III DNA |
| WO1986004336A1 (en) * | 1985-01-21 | 1986-07-31 | Institut Pasteur | Monoclonal antibodies against core proteins of lymphadenopathy-associated-viruses |
| WO1986006099A1 (en) * | 1985-04-08 | 1986-10-23 | Genetic Systems Corporation | EXPRESSION AND DIAGNOSTIC USE OF gag ENCODED PEPTIDES WHICH ARE IMMUNOLOGICALLY REACTIVE WITH ANTIBODIES TO LAV |
| EP0199301A1 (en) * | 1985-04-19 | 1986-10-29 | F. Hoffmann-La Roche Ag | Recombinant acquired immune deficiency syndrome (AIDS) viral envelope protein and method of testing for AIDS |
| WO1987002775A1 (en) * | 1985-10-24 | 1987-05-07 | Southwest Foundation For Biomedical Research | Synthetic peptides and use for diagnosis and vaccination for aids and arc |
| EP0273716A2 (en) * | 1986-12-30 | 1988-07-06 | THE UNITED STATES OF AMERICA as represented by the Secretary United States Department of Commerce | Synthetic peptides which induce cellular immunity to the aids virus and aids viral proteins |
| EP0181150B1 (en) * | 1984-10-31 | 1993-06-09 | Chiron Corporation | Recombinant proteins of viruses associated with lymphadenopathy syndrome and/or acquired immune deficiency syndrome |
Family Cites Families (9)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| IE64785B1 (en) * | 1985-04-08 | 1995-09-06 | Genetic Systems Corp | Expression of immunologically reactive viral proteins |
| WO1986006414A1 (en) * | 1985-04-29 | 1986-11-06 | Genetic Systems Corporation | Synthetic antigens for the detection of aids-related disease |
| GB8525615D0 (en) * | 1985-10-17 | 1985-11-20 | Hoffmann La Roche | Polypeptides |
| EP0245459B1 (en) * | 1985-11-07 | 1993-09-29 | The President And Fellows Of Harvard College | T-cell lymphotrophic virus protein and assay |
| US4734362A (en) * | 1986-02-03 | 1988-03-29 | Cambridge Bioscience Corporation | Process for purifying recombinant proteins, and products thereof |
| US4772547A (en) * | 1986-02-03 | 1988-09-20 | Hoffmann-La Roche Inc. | HTLV-III envelope peptides |
| US4925784A (en) * | 1986-04-04 | 1990-05-15 | Hoffmann-La Roche Inc. | Expression and purification of an HTLV-III gag/env gene protein |
| IE63109B1 (en) * | 1986-06-23 | 1995-03-22 | Genetic Systems Corp | Human monoclonal antibody to lymphadenopathy-associated virus |
| EP0255190A3 (en) * | 1986-08-01 | 1990-08-29 | Repligen Corporation | Recombinant polypeptides and their uses, inclusing assay for aids virus |
-
1987
- 1987-08-13 NZ NZ221440A patent/NZ221440A/xx unknown
- 1987-08-14 ZW ZW154/87A patent/ZW15487A1/xx unknown
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- 1987-08-18 ES ES8702431A patent/ES2010727A6/es not_active Expired
- 1987-08-19 LU LU86972A patent/LU86972A1/fr unknown
- 1987-08-19 DE DE19873727703 patent/DE3727703A1/de not_active Withdrawn
- 1987-08-19 SE SE8703225A patent/SE506025C2/sv not_active IP Right Cessation
- 1987-08-19 FR FR878711736A patent/FR2603107B1/fr not_active Expired - Fee Related
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- 1987-08-20 JP JP62207336A patent/JPS6485928A/ja active Pending
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-
1993
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Patent Citations (8)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| EP0185444A2 (en) * | 1984-10-10 | 1986-06-25 | Centocor, Inc. | Cloning and expression of HTLV-III DNA |
| WO1986002383A1 (en) * | 1984-10-18 | 1986-04-24 | Institut Pasteur | Envelope antigens of lymphadenopathy associated virus and their applications |
| EP0181150B1 (en) * | 1984-10-31 | 1993-06-09 | Chiron Corporation | Recombinant proteins of viruses associated with lymphadenopathy syndrome and/or acquired immune deficiency syndrome |
| WO1986004336A1 (en) * | 1985-01-21 | 1986-07-31 | Institut Pasteur | Monoclonal antibodies against core proteins of lymphadenopathy-associated-viruses |
| WO1986006099A1 (en) * | 1985-04-08 | 1986-10-23 | Genetic Systems Corporation | EXPRESSION AND DIAGNOSTIC USE OF gag ENCODED PEPTIDES WHICH ARE IMMUNOLOGICALLY REACTIVE WITH ANTIBODIES TO LAV |
| EP0199301A1 (en) * | 1985-04-19 | 1986-10-29 | F. Hoffmann-La Roche Ag | Recombinant acquired immune deficiency syndrome (AIDS) viral envelope protein and method of testing for AIDS |
| WO1987002775A1 (en) * | 1985-10-24 | 1987-05-07 | Southwest Foundation For Biomedical Research | Synthetic peptides and use for diagnosis and vaccination for aids and arc |
| EP0273716A2 (en) * | 1986-12-30 | 1988-07-06 | THE UNITED STATES OF AMERICA as represented by the Secretary United States Department of Commerce | Synthetic peptides which induce cellular immunity to the aids virus and aids viral proteins |
Non-Patent Citations (1)
| Title |
|---|
| PROC. NATL. ACAD. SCI. USA, vol. 83, décembre 1986, pages 9254-9258; C.B. PERT et al.: "Octapeptides deduced from the neuropeptide receptor-like pattern of antigen T4 in brain potently inhibit human immunodeficiency virus receptor binding and T-cell infectivity" * |
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Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| RE | Patent lapsed |
Owner name: GENETIC SYSTEMS CORP. Effective date: 19980831 |