CA2936092A1 - Stabilized hepatitis b core polypeptide - Google Patents
Stabilized hepatitis b core polypeptide Download PDFInfo
- Publication number
- CA2936092A1 CA2936092A1 CA2936092A CA2936092A CA2936092A1 CA 2936092 A1 CA2936092 A1 CA 2936092A1 CA 2936092 A CA2936092 A CA 2936092A CA 2936092 A CA2936092 A CA 2936092A CA 2936092 A1 CA2936092 A1 CA 2936092A1
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- CA
- Canada
- Prior art keywords
- hbc
- polypeptide
- amino acid
- seq
- protein
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Abandoned
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Classifications
-
- 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
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
- C12P21/00—Preparation of peptides or proteins
- C12P21/02—Preparation of peptides or proteins having a known sequence of two or more amino acids, e.g. glutathione
-
- 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
- C07K14/01—DNA viruses
- C07K14/02—Hepadnaviridae, e.g. hepatitis B virus
-
- 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
- A61K39/12—Viral antigens
- A61K39/29—Hepatitis virus
-
- 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
- C12N2730/00—Reverse transcribing DNA viruses
- C12N2730/00011—Details
- C12N2730/10011—Hepadnaviridae
- C12N2730/10111—Orthohepadnavirus, e.g. hepatitis B virus
- C12N2730/10122—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
- C12N2730/00—Reverse transcribing DNA viruses
- C12N2730/00011—Details
- C12N2730/10011—Hepadnaviridae
- C12N2730/10111—Orthohepadnavirus, e.g. hepatitis B virus
- C12N2730/10123—Virus like particles [VLP]
-
- 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
- C12N2770/00—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA ssRNA viruses positive-sense
- C12N2770/00011—Details
- C12N2770/32011—Picornaviridae
- C12N2770/32411—Hepatovirus, i.e. hepatitis A virus
- C12N2770/32423—Virus like particles [VLP]
-
- 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
- C12N2770/00—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA ssRNA viruses positive-sense
- C12N2770/00011—Details
- C12N2770/32011—Picornaviridae
- C12N2770/32411—Hepatovirus, i.e. hepatitis A virus
- C12N2770/32434—Use of virus or viral component as vaccine, e.g. live-attenuated or inactivated virus, VLP, viral protein
Landscapes
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Health & Medical Sciences (AREA)
- Virology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Molecular Biology (AREA)
- Genetics & Genomics (AREA)
- Biochemistry (AREA)
- General Health & Medical Sciences (AREA)
- Zoology (AREA)
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- Engineering & Computer Science (AREA)
- Gastroenterology & Hepatology (AREA)
- Biophysics (AREA)
- Medicinal Chemistry (AREA)
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- Communicable Diseases (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Microbiology (AREA)
- General Chemical & Material Sciences (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Peptides Or Proteins (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
Applications Claiming Priority (5)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US201361755850P | 2013-01-23 | 2013-01-23 | |
| US61/755,850 | 2013-01-23 | ||
| US201361901243P | 2013-11-07 | 2013-11-07 | |
| US61/901,243 | 2013-11-07 | ||
| PCT/US2014/012586 WO2014116730A2 (en) | 2013-01-23 | 2014-01-22 | Stabilized hepatitis b core polypeptide |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| CA2936092A1 true CA2936092A1 (en) | 2014-07-31 |
Family
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Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CA2936092A Abandoned CA2936092A1 (en) | 2013-01-23 | 2014-01-22 | Stabilized hepatitis b core polypeptide |
Country Status (5)
| Country | Link |
|---|---|
| US (1) | US9896483B2 (cg-RX-API-DMAC7.html) |
| EP (1) | EP2948469A4 (cg-RX-API-DMAC7.html) |
| JP (1) | JP2016507520A (cg-RX-API-DMAC7.html) |
| CA (1) | CA2936092A1 (cg-RX-API-DMAC7.html) |
| WO (1) | WO2014116730A2 (cg-RX-API-DMAC7.html) |
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| JP2016507520A (ja) | 2013-01-23 | 2016-03-10 | ザ ボード オブ トラスティーズ オブ ザ レランド スタンフォード ジュニア ユニバーシティー | 安定化されたｂ型肝炎コアポリペプチド |
| DE16703049T1 (de) | 2015-01-15 | 2018-07-12 | University Of Copenhagen | Virusähnliche partikel mit effizienter epitopanzeige |
| EP3368068B1 (en) | 2015-10-30 | 2020-11-18 | University of Copenhagen | Virus like particle with efficient epitope display |
| CN106636016B (zh) * | 2017-02-24 | 2020-03-17 | 天津大学 | 一种通过正负电荷引入辅助病毒样颗粒自组装的方法和应用 |
| EP3723796A1 (en) * | 2017-12-13 | 2020-10-21 | CureVac AG | Flavivirus vaccine |
| US11261216B2 (en) * | 2018-12-28 | 2022-03-01 | The Board Of Trustees Of The Leland Stanford Junior University | Engineered hepatitis B core polypeptide |
| CN109666067A (zh) * | 2019-01-07 | 2019-04-23 | 中国科学院过程工程研究所 | 一种重组病毒样颗粒及其制备方法和用途 |
| WO2020145901A1 (en) * | 2019-01-11 | 2020-07-16 | Agency For Science, Technology And Research | Use of hla-a*11:01-restricted hepatitis b virus (hbv) peptides for identifying hbv-specific cd8+ t cells |
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| EP1167378B1 (en) | 1994-07-15 | 2011-05-11 | University of Iowa Research Foundation | Immunomodulatory oligonucleotides |
| US6239116B1 (en) | 1994-07-15 | 2001-05-29 | University Of Iowa Research Foundation | Immunostimulatory nucleic acid molecules |
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| US6429199B1 (en) | 1994-07-15 | 2002-08-06 | University Of Iowa Research Foundation | Immunostimulatory nucleic acid molecules for activating dendritic cells |
| US5968767A (en) | 1996-06-07 | 1999-10-19 | Genentech, Inc. | Methods for in vitro protein synthesis |
| WO1998035062A1 (en) | 1997-02-07 | 1998-08-13 | Lingappa Jaisri R | Multistep, atp-dependent cell-free system for the assembly of human immunodeficiency virus capsids |
| US6406705B1 (en) | 1997-03-10 | 2002-06-18 | University Of Iowa Research Foundation | Use of nucleic acids containing unmethylated CpG dinucleotide as an adjuvant |
| CA2293489C (en) | 1997-06-06 | 2009-09-29 | The Regents Of The University Of California | Inhibitors of dna immunostimulatory sequence activity |
| CA2320488C (en) * | 1998-02-12 | 2007-03-06 | Immune Complex, Corporation | Strategically modified hepatitis b core proteins and their derivatives |
| DE69929232T2 (de) | 1998-10-21 | 2006-08-31 | The United States Government As Represented By The Department Of Health And Human Services | Virusähnliche partikel zur induktion von autoantikörpern |
| WO2000032625A1 (en) * | 1998-12-04 | 2000-06-08 | Biogen, Inc. | Hbv core antigen particles with multiple immunogenic components attached via peptide ligands |
| US6168931B1 (en) | 1999-03-17 | 2001-01-02 | The Board Of Trustees Of The Leland Stanford Junior University | Enhanced in vitro synthesis of biological macromolecules using a novel ATP regeneration system |
| US6994986B2 (en) | 1999-03-17 | 2006-02-07 | The Board Of Trustees Of The Leland Stanford University | In vitro synthesis of polypeptides by optimizing amino acid metabolism |
| US6337191B1 (en) | 1999-03-22 | 2002-01-08 | The Board Of Trustees Of The Leland Stanford Junior University | Vitro protein synthesis using glycolytic intermediates as an energy source |
| US6586207B2 (en) | 2000-05-26 | 2003-07-01 | California Institute Of Technology | Overexpression of aminoacyl-tRNA synthetases for efficient production of engineered proteins containing amino acid analogues |
| US6548276B2 (en) | 2000-09-06 | 2003-04-15 | The Board Of Trustees Of The Leland Stanford Junior University | Enhanced in vitro synthesis of active proteins containing disulfide bonds |
| US7041479B2 (en) | 2000-09-06 | 2006-05-09 | The Board Of Trustess Of The Leland Stanford Junior University | Enhanced in vitro synthesis of active proteins containing disulfide bonds |
| IL158418A0 (en) | 2001-04-19 | 2004-05-12 | Scripps Research Inst | In vivo incorporation of unnatural amino acids |
| AU2002339224B2 (en) | 2001-09-14 | 2008-10-09 | Kuros Us Llc | Packaging of immunostimulatory substances into virus-like particles: method of preparation and use |
| 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 |
| US7615227B2 (en) | 2001-12-20 | 2009-11-10 | 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 |
| ES2346646T5 (es) | 2002-05-30 | 2018-02-15 | The Scripps Research Institute | Ligación catalizada con cobre de azidas y acetilenos |
| WO2004016778A1 (en) | 2002-08-19 | 2004-02-26 | The Board Of Trustees Of The Leland Stanford Junior University | Improved methods of in vitro protein synthesis |
| CA2497972C (en) * | 2002-09-06 | 2016-04-26 | Advanced Life Science Institute, Inc. | Hbv precore protein having a particle-forming ability |
| EP1897548B2 (en) | 2003-02-28 | 2024-05-22 | The Johns Hopkins University | T cell regulation |
| MXPA05009289A (es) | 2003-03-26 | 2005-10-18 | Cytos Biotechnology Ag | Conjugados de particulas tipo virus del analogo del peptido melan-a. |
| EP1636340A4 (en) | 2003-06-18 | 2009-02-11 | Scripps Research Inst | COMPLEMENTS TO THE GENETIC CODE OF UNNATURATIVE REACTIVE AMINO ACIDS |
| WO2005005614A2 (en) * | 2003-07-03 | 2005-01-20 | Pecos Labs, Inc. | Combined b-cell and t-cell epitopes on vlp for improved vaccines |
| US20050054044A1 (en) | 2003-07-18 | 2005-03-10 | The Board Of Trustees Of The Leland Stanford Junior University | Method of alleviating nucleotide limitations for in vitro protein synthesis |
| US7341852B2 (en) | 2003-07-18 | 2008-03-11 | The Board Of Trustees Of The Leland Stanford Junior University | Methods of decoupling reaction scale and protein synthesis yield in batch mode |
| CA2541360A1 (en) | 2003-10-08 | 2005-04-21 | Bradley T. Messmer | Methods and compositions for diagnosis and treatment of b cell chronic lymphocytic leukemia |
| JP5074768B2 (ja) | 2003-11-20 | 2012-11-14 | ボード オブ トラスティーズ オブ ザ レランド スタンフォード ジュニア ユニバーシティ | インビトロにおけるタンパク質合成の改良された方法 |
| US20050170551A1 (en) | 2004-02-04 | 2005-08-04 | Strip David R. | Manufacture of flat panel light emitting devices |
| WO2006033679A2 (en) * | 2004-05-25 | 2006-03-30 | Chimeracore, Inc. | Self-assembling nanoparticle drug delivery system |
| ES2519444T3 (es) | 2004-09-21 | 2014-11-07 | The Scripps Research Institute | Incorporación in vivo de alquinil aminoácidos a proteínas en eubacterias |
| US9809824B2 (en) | 2004-12-13 | 2017-11-07 | The United States Of America, Represented By The Secretary, Department Of Health And Human Services | CpG oligonucleotide prodrugs, compositions thereof and associated therapeutic methods |
| AU2007348315A1 (en) * | 2006-04-07 | 2008-09-12 | Chimeros, Inc. | Compositions and methods for treating B- cell malignancies |
| US20080096819A1 (en) | 2006-05-02 | 2008-04-24 | Allozyne, Inc. | Amino acid substituted molecules |
| US20110129438A1 (en) | 2006-06-28 | 2011-06-02 | James Robert Swartz | Immunogenic protein constructs |
| WO2008066583A2 (en) | 2006-06-29 | 2008-06-05 | The Board Of Trustees Of The Leland Stanford Junior University | Cell-free synthesis of proteins containing unnatural amino acids |
| US20090317861A1 (en) | 2006-06-29 | 2009-12-24 | Bundy Bradley C | Cell-free synthesis of virus like particles |
| CN101511856B (zh) | 2006-09-08 | 2016-01-20 | Ambrx公司 | 脊椎动物细胞中抑制因子trna的转录 |
| AU2008205479A1 (en) | 2007-01-18 | 2008-07-24 | The Board Of Trustees Of The Leland Stanford Junior University | Enhanced cell-free synthesis of active proteins containing disulfide bonds |
| CA2707840A1 (en) | 2007-08-20 | 2009-02-26 | Allozyne, Inc. | Amino acid substituted molecules |
| US8445706B2 (en) | 2008-09-05 | 2013-05-21 | Board Of Trustees Of Northern Illinois University | Unnatural amino acids capable of covalently modifying protein phosphatases and their use as general and specific inhibitors and probes |
| WO2010042755A2 (en) * | 2008-10-08 | 2010-04-15 | Chimeros Inc. | Chimeric therapeutics, compositions, and methods for using same |
| US20100168402A1 (en) | 2008-11-14 | 2010-07-01 | Bundy Bradley C | Direct Attachment of Polypeptides to Virus Like Particles |
| US8324149B2 (en) | 2008-11-18 | 2012-12-04 | The Board Of Trustees Of The Leland Stanford Junior University | Encapsidation of heterologous entities into virus-like particles |
| CA2816401C (en) | 2009-11-05 | 2017-07-18 | Novici Biotech Llc | Generation of antigenic virus-like particles through protein-protein linkages |
| WO2011109422A2 (en) | 2010-03-02 | 2011-09-09 | The United States Of America, Represented By The Secretary, Department Of Health And Human Services | Compositions and methods for the treatment of cancer |
| AU2012305714A1 (en) * | 2011-09-09 | 2014-03-27 | Biomed Realty, L.P. | Methods and compositions for controlling assembly of viral proteins |
| EP3520809B1 (en) | 2012-02-03 | 2025-08-06 | Emory University | Immunostimulatory compositions. |
| JP2016507520A (ja) | 2013-01-23 | 2016-03-10 | ザ ボード オブ トラスティーズ オブ ザ レランド スタンフォード ジュニア ユニバーシティー | 安定化されたｂ型肝炎コアポリペプチド |
| JP2016515538A (ja) | 2013-03-15 | 2016-05-30 | ブレット バイオテクノロジー、 インク．Ｂｕｌｌｅｔ Ｂｉｏｔｅｃｈｎｏｌｏｇｙ， Ｉｎｃ． | 特異的な多価ウイルス様粒子ワクチンおよびその使用 |
| JP2017500313A (ja) | 2013-12-09 | 2017-01-05 | ブレット バイオテクノロジー， インコーポレーテッドＢｕｌｌｅｔ Ｂｉｏｔｅｃｈｎｏｌｏｇｙ， Ｉｎｃ． | 特異的ウイルス様粒子−ＣｐＧオリゴヌクレオチドワクチンおよびその使用 |
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Also Published As
| Publication number | Publication date |
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| WO2014116730A3 (en) | 2014-10-23 |
| JP2016507520A (ja) | 2016-03-10 |
| US20150329598A1 (en) | 2015-11-19 |
| US9896483B2 (en) | 2018-02-20 |
| EP2948469A4 (en) | 2016-11-02 |
| EP2948469A2 (en) | 2015-12-02 |
| WO2014116730A2 (en) | 2014-07-31 |
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| FZDE | Discontinued |
Effective date: 20190122 |