Screening for target toxins of the antiophidic protein DM64 through a gel-based interactomics approach

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• 作者：Surza L.G. Rocha^a ; ^d ; Ana G.C. Neves-Ferreira^a ; ^d ; ^{anag@ioc.fiocruz.br} ; ^{anagextra@gmail.com} ; Monique R.O. Trugilho^a ; ^d ; ¹ ; Yamileth Angulo^b ; Bruno Lomonte^b ; Richard H. Valente^a ; ^d ; Gilberto B. Domont^c ; ^d ; Jonas Perales^a ; ^d ; ^{jperales@ioc.fiocruz.br} ; ^{jonasperales@gmail.com}
• 关键词：Snake venoms ; Myotoxin ; Myotoxin inhibitor ; Didelphis aurita ; Proteomics ; Interactomics
• 刊名：Journal of Proteomics
• 出版年：2017
• 出版时间：16 January 2017
• 年：2017
• 卷：151
• 期：Complete
• 页码：204-213
• 全文大小：1406 K
• 卷排序：151

文摘

Immobilized DM64 interacted with a wide variety of basic snake venom myotoxic PLA2. However, snake venom acidic PLA2 does not seem a preferential target for this inhibitor Soluble DM64 inhibited the cytotoxicity of several isolated basic myotoxins C-type lectins and CRISP may represent putative new targets for DM64 The results shed light on the structure-function relationship of DM64 This affinity-based approach can be useful in the search for novel toxin components