AU2010249046A1 - Neutralizing molecules to influenza viruses - Google Patents
Neutralizing molecules to influenza viruses Download PDFInfo
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- AU2010249046A1 AU2010249046A1 AU2010249046A AU2010249046A AU2010249046A1 AU 2010249046 A1 AU2010249046 A1 AU 2010249046A1 AU 2010249046 A AU2010249046 A AU 2010249046A AU 2010249046 A AU2010249046 A AU 2010249046A AU 2010249046 A1 AU2010249046 A1 AU 2010249046A1
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- C07K2317/90—Immunoglobulins specific features characterized by (pharmaco)kinetic aspects or by stability of the immunoglobulin
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- 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
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Landscapes
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| PCT/US2010/034604 WO2010132604A2 (en) | 2009-05-13 | 2010-05-12 | Neutralizing molecules to influenza viruses |
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| US20120128671A1 (en) | 2009-05-13 | 2012-05-24 | Lawrence Horowitz | Neutralizing molecules to influenza viruses |
| WO2012099566A1 (en) | 2010-11-17 | 2012-07-26 | Sea Lane Biotechnologies, Llc | Influenza virus neutralizing agents that mimic the binding site of an influenza neutralizing antibody |
| CN103635584B (zh) | 2011-04-12 | 2017-10-27 | 冈戈根股份有限公司 | 嵌合抗菌多肽 |
| WO2013016714A1 (en) | 2011-07-28 | 2013-01-31 | Sea Lane Biotechnologies | Sur-binding proteins against erbb3 |
| GB201115214D0 (en) * | 2011-09-02 | 2011-10-19 | Health Prot Agency | Influenza virus antibody compositions |
| KR101514682B1 (ko) | 2011-09-30 | 2015-04-23 | (주)셀트리온 | 인간 ｂ 세포에서 생산된 인플루엔자 ａ 바이러스 중화 활성을 가지는 결합 분자 |
| WO2013086052A2 (en) | 2011-12-05 | 2013-06-13 | Trellis Bioscience, Llc | Antibodies useful in passive influenza immunization |
| US9975956B2 (en) | 2011-12-22 | 2018-05-22 | I2 Pharmaceuticals, Inc. | Surrogate binding proteins which bind DR4 and/or DR5 |
| US9969794B2 (en) | 2012-05-10 | 2018-05-15 | Visterra, Inc. | HA binding agents |
| WO2014152841A1 (en) | 2013-03-14 | 2014-09-25 | Contrafect Corporation | Composition and methods based on neutralizing antibodies delivered intranasally for enhanced therapeutic efficacy |
| WO2014161483A1 (zh) * | 2013-04-02 | 2014-10-09 | 厦门大学 | 识别流感病毒血凝素蛋白ha1结构域的广谱单克隆抗体 |
| US10639370B2 (en) | 2014-02-04 | 2020-05-05 | Contrafect Corporation | Antibodies useful in passive influenza immunization, and compositions, combinations and methods for use thereof |
| RU2720282C1 (ru) | 2014-02-04 | 2020-04-28 | Контрафект Корпорейшн | Антитела, подходящие для пассивной иммунизации против гриппа, и их композиции, комбинации и способы применения |
| EP3126384B1 (en) | 2014-04-01 | 2020-12-02 | Adimab, LLC | Multispecific antibody analogs comprising a common light chain, and methods of their preparation and use |
| US10732180B2 (en) | 2014-06-04 | 2020-08-04 | Indevr, Inc. | Universal capture array for multiplexed subtype-specific quantification and stability determination of influenza proteins |
| TWI702229B (zh) | 2014-12-19 | 2020-08-21 | 美商再生元醫藥公司 | 流行性感冒病毒血球凝集素之人類抗體 |
| US10513553B2 (en) | 2015-11-13 | 2019-12-24 | Visterra, Inc. | Compositions and methods for treating and preventing influenza |
| CA3015347A1 (en) | 2016-02-24 | 2017-08-31 | Visterra, Inc. | Formulations of antibody molecules to influenza virus |
| RU2748233C2 (ru) * | 2017-01-31 | 2021-05-21 | Мсм Протеин Текнолоджиз Инк. | Антитела против cxcr4 |
| CA3088194A1 (en) | 2018-01-26 | 2019-08-01 | Regeneron Pharmaceuticals, Inc. | Human antibodies to influenza hemagglutinin |
| JP2022521819A (ja) | 2019-03-25 | 2022-04-12 | ビステラ， インコーポレイテッド | インフルエンザを処置および予防するための組成物および方法 |
| WO2022192634A1 (en) * | 2021-03-12 | 2022-09-15 | Massachusetts Institute Of Technology | Compositions and methods for dominant antiviral therapy |
Family Cites Families (102)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4307016A (en) | 1978-03-24 | 1981-12-22 | Takeda Chemical Industries, Ltd. | Demethyl maytansinoids |
| US4256746A (en) | 1978-11-14 | 1981-03-17 | Takeda Chemical Industries | Dechloromaytansinoids, their pharmaceutical compositions and method of use |
| JPS55162791A (en) | 1979-06-05 | 1980-12-18 | Takeda Chem Ind Ltd | Antibiotic c-15003pnd and its preparation |
| JPS5645483A (en) | 1979-09-19 | 1981-04-25 | Takeda Chem Ind Ltd | C-15003phm and its preparation |
| EP0028683A1 (en) | 1979-09-21 | 1981-05-20 | Takeda Chemical Industries, Ltd. | Antibiotic C-15003 PHO and production thereof |
| JPS5645485A (en) | 1979-09-21 | 1981-04-25 | Takeda Chem Ind Ltd | Production of c-15003pnd |
| WO1982001188A1 (en) | 1980-10-08 | 1982-04-15 | Takeda Chemical Industries Ltd | 4,5-deoxymaytansinoide compounds and process for preparing same |
| US4450254A (en) | 1980-11-03 | 1984-05-22 | Standard Oil Company | Impact improvement of high nitrile resins |
| US4313946A (en) | 1981-01-27 | 1982-02-02 | The United States Of America As Represented By The Secretary Of Agriculture | Chemotherapeutically active maytansinoids from Trewia nudiflora |
| US4315929A (en) | 1981-01-27 | 1982-02-16 | The United States Of America As Represented By The Secretary Of Agriculture | Method of controlling the European corn borer with trewiasine |
| US4563304A (en) | 1981-02-27 | 1986-01-07 | Pharmacia Fine Chemicals Ab | Pyridine compounds modifying proteins, polypeptides or polysaccharides |
| US4475196A (en) | 1981-03-06 | 1984-10-02 | Zor Clair G | Instrument for locating faults in aircraft passenger reading light and attendant call control system |
| US4447233A (en) | 1981-04-10 | 1984-05-08 | Parker-Hannifin Corporation | Medication infusion pump |
| JPS57192389A (en) | 1981-05-20 | 1982-11-26 | Takeda Chem Ind Ltd | Novel maytansinoid |
| US4439196A (en) | 1982-03-18 | 1984-03-27 | Merck & Co., Inc. | Osmotic drug delivery system |
| US4522811A (en) | 1982-07-08 | 1985-06-11 | Syntex (U.S.A.) Inc. | Serial injection of muramyldipeptides and liposomes enhances the anti-infective activity of muramyldipeptides |
| ZA836080B (en) * | 1982-08-23 | 1984-04-25 | Scripps Clinic Res | Broad spectrum influenza antisera |
| US4447224A (en) | 1982-09-20 | 1984-05-08 | Infusaid Corporation | Variable flow implantable infusion apparatus |
| US4487603A (en) | 1982-11-26 | 1984-12-11 | Cordis Corporation | Implantable microinfusion pump system |
| US4816567A (en) | 1983-04-08 | 1989-03-28 | Genentech, Inc. | Recombinant immunoglobin preparations |
| US4486194A (en) | 1983-06-08 | 1984-12-04 | James Ferrara | Therapeutic device for administering medicaments through the skin |
| JPS60222842A (ja) | 1984-04-19 | 1985-11-07 | Fuji Photo Film Co Ltd | ハロゲン化銀写真乳剤およびその製造方法 |
| US4596556A (en) | 1985-03-25 | 1986-06-24 | Bioject, Inc. | Hypodermic injection apparatus |
| US4965188A (en) | 1986-08-22 | 1990-10-23 | Cetus Corporation | Process for amplifying, detecting, and/or cloning nucleic acid sequences using a thermostable enzyme |
| US4683202A (en) | 1985-03-28 | 1987-07-28 | Cetus Corporation | Process for amplifying nucleic acid sequences |
| US5374548A (en) | 1986-05-02 | 1994-12-20 | Genentech, Inc. | Methods and compositions for the attachment of proteins to liposomes using a glycophospholipid anchor |
| MX9203291A (es) | 1985-06-26 | 1992-08-01 | Liposome Co Inc | Metodo para acoplamiento de liposomas. |
| US4800159A (en) | 1986-02-07 | 1989-01-24 | Cetus Corporation | Process for amplifying, detecting, and/or cloning nucleic acid sequences |
| DE3789138T2 (de) | 1986-11-27 | 1994-05-26 | Hoffmann La Roche | Nukleotid-Sequenzen, die selektiv exprimiert sind in pre-B-Zellen und Sonden zu diesem Zweck. |
| US5182205A (en) | 1986-11-27 | 1993-01-26 | Hoffmann-La Roche Inc. | Nucleotide sequences which are selectively expressed in pre-B cells and probes therefor |
| US4790824A (en) | 1987-06-19 | 1988-12-13 | Bioject, Inc. | Non-invasive hypodermic injection device |
| US4941880A (en) | 1987-06-19 | 1990-07-17 | Bioject, Inc. | Pre-filled ampule and non-invasive hypodermic injection device assembly |
| US5108921A (en) | 1989-04-03 | 1992-04-28 | Purdue Research Foundation | Method for enhanced transmembrane transport of exogenous molecules |
| US5208020A (en) | 1989-10-25 | 1993-05-04 | Immunogen Inc. | Cytotoxic agents comprising maytansinoids and their therapeutic use |
| US5064413A (en) | 1989-11-09 | 1991-11-12 | Bioject, Inc. | Needleless hypodermic injection device |
| US5312335A (en) | 1989-11-09 | 1994-05-17 | Bioject Inc. | Needleless hypodermic injection device |
| US5183884A (en) | 1989-12-01 | 1993-02-02 | United States Of America | Dna segment encoding a gene for a receptor related to the epidermal growth factor receptor |
| US5427908A (en) | 1990-05-01 | 1995-06-27 | Affymax Technologies N.V. | Recombinant library screening methods |
| IL101943A0 (en) | 1991-05-24 | 1992-12-30 | Genentech Inc | Structure,production and use of heregulin |
| US5622929A (en) | 1992-01-23 | 1997-04-22 | Bristol-Myers Squibb Company | Thioether conjugates |
| US5474765A (en) | 1992-03-23 | 1995-12-12 | Ut Sw Medical Ctr At Dallas | Preparation and use of steroid-polyanionic polymer-based conjugates targeted to vascular endothelial cells |
| ES2149768T3 (es) | 1992-03-25 | 2000-11-16 | Immunogen Inc | Conjugados de agentes enlazantes de celulas derivados de cc-1065. |
| US5383851A (en) | 1992-07-24 | 1995-01-24 | Bioject Inc. | Needleless hypodermic injection device |
| US6337070B1 (en) | 1993-04-29 | 2002-01-08 | Takara Shuzo Co., Ltd. | Polypeptides for use in generating anti-human influenza virus antibodies |
| FR2706982B1 (enExample) | 1993-06-21 | 1995-08-04 | Thermique Generale Vinicole | |
| GB9522351D0 (en) | 1995-11-01 | 1996-01-03 | Medeva Holdings Bv | Vaccine compositions |
| JP2000503639A (ja) | 1995-12-22 | 2000-03-28 | ブリストル―マイヤーズ スクイブ カンパニー | 分枝ヒドラゾンのリンカー類 |
| WO2000073349A1 (en) | 1999-05-28 | 2000-12-07 | Genentech, Inc. | Dr4 antibodies and uses thereof |
| ES2462532T3 (es) | 1999-10-18 | 2014-05-23 | Novartis Vaccines And Diagnostics, Inc. | Composiciones y métodos para estimular una respuesta inmune contra agentes infecciosos |
| US20030215453A1 (en) | 2002-05-14 | 2003-11-20 | Dedera Douglas A. | Methods of therapy and diagnosis using immunotargeting of cells expressing VpreB1 protein |
| WO2001060402A2 (en) | 2000-02-15 | 2001-08-23 | Intellivax International Inc. | Proteosome influenza vaccine |
| US7476383B2 (en) | 2000-05-02 | 2009-01-13 | The Uab Research Foundation | Antibody selective for DR4 and uses thereof |
| US6333410B1 (en) | 2000-08-18 | 2001-12-25 | Immunogen, Inc. | Process for the preparation and purification of thiol-containing maytansinoids |
| IL155002A0 (en) | 2000-10-12 | 2003-10-31 | Genentech Inc | Reduced-viscosity concentrated protein formulations |
| US7115717B2 (en) | 2001-05-18 | 2006-10-03 | Kirin Beer Kabushiki Kaisha | Anti-TRAIL-R antibodies |
| US6441163B1 (en) | 2001-05-31 | 2002-08-27 | Immunogen, Inc. | Methods for preparation of cytotoxic conjugates of maytansinoids and cell binding agents |
| GB0113179D0 (en) | 2001-05-31 | 2001-07-25 | Novartis Ag | Organic compounds |
| US6716821B2 (en) | 2001-12-21 | 2004-04-06 | Immunogen Inc. | Cytotoxic agents bearing a reactive polyethylene glycol moiety, cytotoxic conjugates comprising polyethylene glycol linking groups, and methods of making and using the same |
| AU2003244817B2 (en) | 2002-06-28 | 2010-08-26 | Domantis Limited | Antigen-binding immunoglobulin single variable domains and dual-specific constructs |
| SI2357006T1 (sl) | 2002-07-31 | 2016-01-29 | Seattle Genetics, Inc. | Konjugati zdravil in njihova uporaba za zdravljenje raka, avtoimunske bolezni ali infekcijske bolezni |
| US8088387B2 (en) | 2003-10-10 | 2012-01-03 | Immunogen Inc. | Method of targeting specific cell populations using cell-binding agent maytansinoid conjugates linked via a non-cleavable linker, said conjugates, and methods of making said conjugates |
| US7276497B2 (en) | 2003-05-20 | 2007-10-02 | Immunogen Inc. | Cytotoxic agents comprising new maytansinoids |
| BR122018071808B8 (pt) | 2003-11-06 | 2020-06-30 | Seattle Genetics Inc | conjugado |
| RU2402548C2 (ru) | 2004-05-19 | 2010-10-27 | Медарекс, Инк. | Химические линкеры и их конъюгаты |
| EP1817341A2 (en) | 2004-11-29 | 2007-08-15 | Seattle Genetics, Inc. | Engineered antibodies and immunoconjugates |
| US20060147997A1 (en) | 2004-11-30 | 2006-07-06 | Virosys Pharmaceuticals, Inc. | PenetraBodies: receptor-mediated targeted delivery of functionally-active human antibody fragments into cytosol for the treatment of chronic infections and diseases |
| CA2605024C (en) | 2005-04-15 | 2018-05-22 | Macrogenics, Inc. | Covalent diabodies and uses thereof |
| US7612181B2 (en) | 2005-08-19 | 2009-11-03 | Abbott Laboratories | Dual variable domain immunoglobulin and uses thereof |
| AR056857A1 (es) | 2005-12-30 | 2007-10-24 | U3 Pharma Ag | Anticuerpos dirigidos hacia her-3 (receptor del factor de crecimiento epidérmico humano-3) y sus usos |
| FR2896162B1 (fr) | 2006-01-13 | 2008-02-15 | Sanofi Pasteur Sa | Emulsion huile dans eau thermoreversible |
| US8148085B2 (en) * | 2006-05-15 | 2012-04-03 | Sea Lane Biotechnologies, Llc | Donor specific antibody libraries |
| JP2009537147A (ja) | 2006-05-15 | 2009-10-29 | シー レーン バイオテクノロジーズ， エルエルシー | インフルエンザウイルスに対する中和抗体 |
| EP2059532B1 (en) * | 2006-09-07 | 2012-12-26 | Crucell Holland B.V. | Human binding molecules capable of neutralizing influenza virus h5n1 and uses thereof |
| AU2007303572A1 (en) | 2006-10-02 | 2008-04-10 | Sea Lane Biotechnologies, Llc | Design and construction of diverse synthetic peptide and polypeptide libraries |
| CN101622347A (zh) * | 2007-01-12 | 2010-01-06 | 航道生物技术有限责任公司 | 构象约束多肽序列的组合文库 |
| HRP20131113T1 (hr) | 2007-02-16 | 2014-01-17 | Merrimack Pharmaceuticals, Inc. | Protutijela protiv erbb3 i njihova uporaba |
| JP5779350B2 (ja) | 2007-03-27 | 2015-09-16 | シー レーン バイオテクノロジーズ， エルエルシー | 抗体代替軽鎖配列を含む構築物およびライブラリー |
| KR101466326B1 (ko) * | 2007-06-15 | 2014-12-02 | 주식회사 바이오트라이온 | 약독화된 인플루엔자 바이러스 및 이를 포함하는 생백신 |
| EP2187973A2 (en) | 2007-08-13 | 2010-05-26 | Sea Lane Biotechnologies,llc. | Spore displaying antigens |
| ES2628395T3 (es) | 2007-08-15 | 2017-08-02 | Bayer Pharma Aktiengesellschaft | Anticuerpo regulado por proteasa |
| SI2211904T1 (sl) | 2007-10-19 | 2016-12-30 | Seattle Genetics, Inc. | CD19 vezavna sredstva in njihove uporabe |
| US20110038935A1 (en) * | 2007-12-06 | 2011-02-17 | Marasco Wayne A | Antibodies against influenza virus and methods of use thereof |
| AU2009221729A1 (en) | 2008-03-06 | 2009-09-11 | Genentech, Inc. | Combination therapy with c-met and HER antagonists |
| US20100040635A1 (en) | 2008-03-28 | 2010-02-18 | Sea Lane Biotechnologies | Neutralizing antibodies to influenza viruses |
| MX2010011808A (es) | 2008-04-30 | 2011-03-04 | Immunogen Inc | Conjugados potentes y enlazadores hidrofilicos. |
| CN104524590B (zh) | 2008-04-30 | 2019-06-21 | 伊缪诺金公司 | 交联剂和它们的用途 |
| CN102149727A (zh) | 2008-07-11 | 2011-08-10 | 航道生物技术有限责任公司 | 包含抗体替代卡帕轻链序列的构建体和文库 |
| JP5746051B2 (ja) | 2009-01-15 | 2015-07-08 | ラボラトリー コーポレイション オブ アメリカ ホールディングス | Ｈｅｒ−３の測定による患者の反応を判定する方法 |
| MA33198B1 (fr) | 2009-03-20 | 2012-04-02 | Genentech Inc | Anticorps anti-her di-spécifiques |
| JP2012521786A (ja) | 2009-03-30 | 2012-09-20 | モウント シナイ スクール オフ メディシネ | インフルエンザウイルスワクチン及びその使用 |
| US20120128671A1 (en) | 2009-05-13 | 2012-05-24 | Lawrence Horowitz | Neutralizing molecules to influenza viruses |
| EP3205723A1 (en) | 2009-06-26 | 2017-08-16 | i2 Pharmaceuticals, Inc. | Expression of surrogate light chains |
| US20120269830A1 (en) | 2009-12-07 | 2012-10-25 | Lawrence Horowitz | Conjugates with improved pharmacokinetic properties |
| NZ702145A (en) | 2010-03-12 | 2016-03-31 | Merial Inc | Bluetongue virus recombinant vaccines and uses thereof |
| ES2566602T3 (es) | 2010-04-09 | 2016-04-14 | Aveo Pharmaceuticals, Inc. | Anticuerpos anti-ErbB3 |
| SMT202000095T1 (it) | 2010-05-14 | 2020-03-13 | Amgen Inc | Formulazioni di anticorpi anti-sclerostina ad alta concentrazione |
| CN103221062A (zh) | 2010-06-03 | 2013-07-24 | 阿布拉西斯生物科学有限责任公司 | 外周血sparc 结合抗体及其用途 |
| CA2815277A1 (en) | 2010-10-29 | 2012-05-03 | Immunogen, Inc. | Novel egfr-binding molecules and immunoconjugates thereof |
| WO2013003647A2 (en) | 2011-06-28 | 2013-01-03 | Sea Lane Biotechnologies, Llc | Multispecific stacked variable domain binding proteins |
| WO2013016714A1 (en) | 2011-07-28 | 2013-01-31 | Sea Lane Biotechnologies | Sur-binding proteins against erbb3 |
| US9975956B2 (en) | 2011-12-22 | 2018-05-22 | I2 Pharmaceuticals, Inc. | Surrogate binding proteins which bind DR4 and/or DR5 |
| US20150011736A1 (en) | 2012-01-20 | 2015-01-08 | Sea Lane Biotechnologies, Llc | Binding molecule conjugates |
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- 2010-05-12 EP EP10719210.6A patent/EP2430047B1/en active Active
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| WO2010132604A3 (en) | 2011-03-24 |
| EP2430047B1 (en) | 2018-03-28 |
| AU2016247163B2 (en) | 2018-06-21 |
| US10017561B2 (en) | 2018-07-10 |
| JP2017141231A (ja) | 2017-08-17 |
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