ES2709065T7 - Anticuerpos que se unen específicamente a la toxina alfa de Staphylococcus aureus y métodos de uso - Google Patents
Anticuerpos que se unen específicamente a la toxina alfa de Staphylococcus aureus y métodos de uso Download PDFInfo
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- ES2709065T7 ES2709065T7 ES12745207T ES12745207T ES2709065T7 ES 2709065 T7 ES2709065 T7 ES 2709065T7 ES 12745207 T ES12745207 T ES 12745207T ES 12745207 T ES12745207 T ES 12745207T ES 2709065 T7 ES2709065 T7 ES 2709065T7
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- C07K2317/30—Immunoglobulins specific features characterized by aspects of specificity or valency
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- C07K2317/50—Immunoglobulins specific features characterized by immunoglobulin fragments
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Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
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| US201161440581P | 2011-02-08 | 2011-02-08 | |
| PCT/US2012/024201 WO2012109285A2 (en) | 2011-02-08 | 2012-02-07 | Antibodies that specifically bind staphylococcus aureus alpha toxin and methods of use |
Publications (2)
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| ES2709065T3 ES2709065T3 (es) | 2019-04-15 |
| ES2709065T7 true ES2709065T7 (es) | 2021-12-09 |
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| ES12745207T Active ES2709065T7 (es) | 2011-02-08 | 2012-02-07 | Anticuerpos que se unen específicamente a la toxina alfa de Staphylococcus aureus y métodos de uso |
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| PL2718320T3 (pl) | 2011-06-10 | 2018-06-29 | Medimmune Limited | Cząsteczki wiążące przeciwko PSL Pseudomonas i ich zastosowanie |
| KR102184343B1 (ko) * | 2011-11-07 | 2020-11-30 | 메디뮨 엘엘씨 | 항슈도모나스 ｐｓｌ 및 ｐｃｒｖ 결합 분자를 이용한 병용 요법 |
| WO2013096948A1 (en) | 2011-12-23 | 2013-06-27 | Lydon Nicholas B | Immunoglobulins and variants directed against pathogenic microbes |
| US9988439B2 (en) | 2011-12-23 | 2018-06-05 | Nicholas B. Lydon | Immunoglobulins and variants directed against pathogenic microbes |
| JOP20200236A1 (ar) * | 2012-09-21 | 2017-06-16 | Regeneron Pharma | الأجسام المضادة لمضاد cd3 وجزيئات ربط الأنتيجين ثنائية التحديد التي تربط cd3 وcd20 واستخداماتها |
| SG11201502937PA (en) * | 2012-11-06 | 2015-06-29 | Medimmune Llc | COMBINATION THERAPIES USING ANTI-<i>PSEUDOMONAS</i> PSL AND PCRV BINDING MOLECULES |
| CA2890385C (en) * | 2012-11-06 | 2022-07-12 | Medimmune, Llc | Methods of treating s. aureus-associated diseases |
| SG11201503232TA (en) * | 2012-11-06 | 2015-05-28 | Medimmune Llc | Antibodies to s. aureus surface determinants |
| WO2015055814A1 (en) * | 2013-10-17 | 2015-04-23 | Arsanis Biosciences Gmbh | Cross-reactive staphylococcus aureus antibody sequences |
| WO2015109012A1 (en) | 2014-01-14 | 2015-07-23 | Integrated Biotherapeutics, Inc. | Targeting immunological functions to the site of bacterial infections using cell wall targeting domains of bacteriolysins |
| TWI701042B (zh) | 2014-03-19 | 2020-08-11 | 美商再生元醫藥公司 | 用於腫瘤治療之方法及抗體組成物 |
| TWI719938B (zh) * | 2014-06-19 | 2021-03-01 | 美商麥迪紐有限責任公司 | 多重細菌感染之治療 |
| US20180017559A1 (en) * | 2014-08-12 | 2018-01-18 | Arsanis Biosciences Gmbh | Predicting s. aureus disease |
| LT3699198T (lt) | 2014-11-17 | 2025-05-12 | Regeneron Pharmaceuticals, Inc. | Būdai navikams gydyti naudojant cd3×cd20 bispecifinį antikūną |
| JP6889701B2 (ja) | 2015-09-24 | 2021-06-18 | エフ．ホフマン−ラ ロシュ アーゲーＦ． Ｈｏｆｆｍａｎｎ−Ｌａ Ｒｏｃｈｅ Ａｋｔｉｅｎｇｅｓｅｌｌｓｃｈａｆｔ | アルファ溶血素バリアント |
| US20190077851A1 (en) * | 2015-10-30 | 2019-03-14 | Bruno Francois | Methods of using anti-alpha toxin antibody |
| TW202311284A (zh) | 2017-01-03 | 2023-03-16 | 美商再生元醫藥公司 | 抗金黃色葡萄球菌溶血素ａ毒素之人類抗體 |
| CA3053164A1 (en) | 2017-02-09 | 2018-08-16 | Bluefin Biomedicine, Inc. | Anti-ilt3 antibodies and antibody drug conjugates |
| CN108456250B (zh) * | 2017-02-17 | 2025-11-28 | 恺兴生命科技(上海)有限公司 | 靶向il-13ra2的抗体及其应用 |
| CN109384844B (zh) * | 2017-08-04 | 2020-12-18 | 中国人民解放军军事医学科学院基础医学研究所 | 一种抗金黄色葡萄球菌α溶血素单克隆抗体及应用 |
| EP3840838A2 (en) | 2018-07-24 | 2021-06-30 | MedImmune, LLC | Antibody directed against s.aureus clumping factor a (clfa) |
| WO2020041532A1 (en) * | 2018-08-21 | 2020-02-27 | Sf17 Therapeutics, Inc. | Compositions and methods for treating progressive neurodegenerative diseases |
| FI3844189T3 (fi) | 2018-08-31 | 2025-03-05 | Regeneron Pharma | Annostusstrategia, joka lieventää bispesifisten CD3/CD20-vasta-aineiden sytokiinien vapautumisoireyhtymää |
| CN113015745B (zh) | 2018-10-09 | 2025-02-11 | 免疫医疗有限责任公司 | 针对金黄色葡萄球菌白细胞毒素的抗体 |
| JP2022512647A (ja) | 2018-10-09 | 2022-02-07 | メディミューン，エルエルシー | 抗黄色ブドウ球菌（Ｓｔａｐｈｙｌｏｃｏｃｃｕｓ ａｕｒｅｕｓ）抗体の組み合わせ |
| US12264194B2 (en) | 2019-03-13 | 2025-04-01 | Medimmune, Llc | Decreasing Staphylococcus aureus infections in colonized patients |
| WO2020210650A1 (en) | 2019-04-12 | 2020-10-15 | Medimmune, Llc | Neutralization of tgf-beta or alpha-v-beta-8 integrin for s. aureus infections |
| CN112538112B (zh) * | 2019-09-20 | 2023-10-27 | 迈威(上海)生物科技股份有限公司 | 抗α-溶血素的抗体及其应用 |
| CN113444173A (zh) | 2020-03-25 | 2021-09-28 | 兴盟生物医药(苏州)有限公司 | 金黄色葡萄球菌α-毒素特异性抗体及其应用 |
| EP4286409A4 (en) * | 2021-01-11 | 2025-01-01 | Starmab Biologics (Suzhou) Co., Ltd | ANTIGEN-BINDING PROTEIN TARGETING STAPHYLOCOCCUS AUREUS ?-HEMOLYTIC AND RELATED APPLICATION |
| CN112941136B (zh) * | 2021-03-24 | 2023-04-28 | 成都欧林生物科技股份有限公司 | 一种重组金黄色葡萄球菌疫苗hi抗原蛋白的纯化方法 |
| CN114455048B (zh) * | 2022-03-02 | 2023-03-14 | 江苏微导纳米科技股份有限公司 | 一种桨杆 |
| WO2023208123A1 (zh) * | 2022-04-28 | 2023-11-02 | 珠海泰诺麦博制药股份有限公司 | 特异性结合金黄色葡萄球菌Hla毒素的全人源单克隆抗体 |
| CN116589566A (zh) * | 2022-11-18 | 2023-08-15 | 昆明医科大学第一附属医院 | 一种HIV-1中和抗体的改造重组单克隆IgM抗体及其应用 |
| CN116023486B (zh) * | 2023-01-10 | 2024-10-08 | 西北农林科技大学 | 金黄色葡萄球菌α-溶血素纳米抗体、制备方法及其应用 |
Family Cites Families (23)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| IL85035A0 (en) | 1987-01-08 | 1988-06-30 | Int Genetic Eng | Polynucleotide molecule,a chimeric antibody with specificity for human b cell surface antigen,a process for the preparation and methods utilizing the same |
| CA2103059C (en) | 1991-06-14 | 2005-03-22 | Paul J. Carter | Method for making humanized antibodies |
| RU2251572C2 (ru) | 1996-04-25 | 2005-05-10 | Дженикон Сайенсиз Корпорейшн, Дзе Риджентс Оф Дзе Юниверсити Оф Калифорния | Анализ аналитов с использованием частиц в качестве метки |
| EP1522590B1 (en) | 2000-06-28 | 2009-08-26 | Glycofi, Inc. | Methods for producing modified glycoproteins |
| US6596541B2 (en) | 2000-10-31 | 2003-07-22 | Regeneron Pharmaceuticals, Inc. | Methods of modifying eukaryotic cells |
| EP1355919B1 (en) | 2000-12-12 | 2010-11-24 | MedImmune, LLC | Molecules with extended half-lives, compositions and uses thereof |
| US20030226155A1 (en) | 2001-08-30 | 2003-12-04 | Biorexis Pharmaceutical Corporation | Modified transferrin-antibody fusion proteins |
| ES2338105T3 (es) | 2003-05-14 | 2010-05-04 | Kenta Biotech Ag | Anticuerpo monoclonal humano especifico para lipopolisacaridos (lps) de serotipo iats 06 pseudomonas aeruginosa. |
| CN1324049C (zh) | 2003-08-04 | 2007-07-04 | 中国疾病预防控制中心病毒病预防控制所 | 人源抗sars冠状病毒基因工程抗体 |
| JP4633788B2 (ja) * | 2004-04-13 | 2011-02-16 | エフ．ホフマン−ラ ロシュ アーゲー | 抗ｐ−セレクチン抗体 |
| KR101505496B1 (ko) * | 2004-09-22 | 2015-03-25 | 글락소스미스클라인 바이오로지칼즈 에스.에이. | 스태필로코쿠스에 대한 예방접종에 사용하기 위한 면역원성 조성물 |
| WO2007084926A2 (en) | 2006-01-17 | 2007-07-26 | Biolex Therapeutics, Inc. | Compositions and methods for humanization and optimization of n-glycans in plants |
| TW200813091A (en) | 2006-04-10 | 2008-03-16 | Amgen Fremont Inc | Targeted binding agents directed to uPAR and uses thereof |
| AU2007259415B2 (en) * | 2006-06-12 | 2013-09-26 | Glaxosmithkline Biologicals Sa | Use of alpha-toxin for treating and preventing Staphylococcus infections |
| MX2009012891A (es) * | 2007-05-31 | 2009-12-10 | Merck & Co Inc | Proteinas de union a antigeno dirigidas a staphylococcus aureus orf0657n. |
| WO2009026303A1 (en) * | 2007-08-21 | 2009-02-26 | Amgen Inc. | Human c-fms antigen binding proteins |
| AU2008292897B2 (en) * | 2007-08-31 | 2015-01-22 | University Of Chicago | Methods and compositions related to immunizing against staphylococcal lung diseases and conditions |
| US8172115B1 (en) | 2008-04-10 | 2012-05-08 | Spencer Forrest, Inc. | Hair building solids dispenser for one handed operation |
| EA201170028A1 (ru) * | 2008-07-02 | 2011-12-30 | Эмерджент Продакт Дивелопмент Сиэтл, Ллс | СВЯЗЫВАЮЩИЕ НЕСКОЛЬКО МИШЕНЕЙ БЕЛКИ, ОБЛАДАЮЩИЕ АНТАГОНИСТИЧЕСКИМ ДЕЙСТВИЕМ TNF-α |
| EP2208787A1 (en) * | 2009-01-19 | 2010-07-21 | Université de Liège | A recombinant alpha-hemolysin polypeptide of Staphylococcus aureus, having a deletion in the stem domain and heterologous sequences inserted |
| GB2467939A (en) * | 2009-02-20 | 2010-08-25 | Univ Sheffield | Removal of bacteria from media |
| PL2445522T3 (pl) * | 2009-06-22 | 2018-01-31 | Wyeth Llc | Kompozycje immunogenne antygenów Staphylococcus aureus |
| SG11201503232TA (en) * | 2012-11-06 | 2015-05-28 | Medimmune Llc | Antibodies to s. aureus surface determinants |
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