High-resolution proteomic profiling of spider venom: expanding the toxin diversity of Phoneutria nigriventer venom

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• 作者：Tarcísio Liberato ; Lanfranco Ranieri Paolo Troncone ; Edson T. Yamashiro…
• 关键词：Phoneutria nigriventer ; Proteome ; Spider venom ; Chitinase
• 刊名：Amino Acids
• 出版年：2016
• 出版时间：March 2016
• 年：2016
• 卷：48
• 期：3
• 页码：901-906
• 全文大小：861 KB
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• 作者单位：Tarcísio Liberato (1) (2)
  Lanfranco Ranieri Paolo Troncone (1)
  Edson T. Yamashiro (3)
  Solange M. T. Serrano (3)
  André Zelanis (2) (3)
  
  1. Laboratório de Farmacologia, Instituto Butantan, São Paulo, Brazil
  2. Laboratório de Proteômica Funcional, Departamento de Ciência e Tecnologia, Universidade Federal de São Paulo, ICT-UNIFESP, Campus de São José dos Campos, Rua Talim, 330, São Paulo, SP, 12231-280, Brazil
  3. Laboratório Especial de Toxinologia Aplicada, Center of Toxins, Immune-Response and Cell Signaling (CeTICS), Instituto Butantan, São Paulo, Brazil
  
• 刊物类别：Biomedical and Life Sciences
• 刊物主题：Life Sciences
  Biochemistry
  Analytical Chemistry
  Biochemical Engineering
  Life Sciences
  Proteomics
  Neurobiology
  
• 出版者：Springer Wien
• ISSN：1438-2199

文摘

Here we present a proteomic characterization of Phoneutria nigriventer venom. A shotgun proteomic approach allowed the identification, for the first time, of O-glycosyl hydrolases (chitinases) in P. nigriventer venom. The electrophoretic profiles under nonreducing and reducing conditions, and protein identification by mass spectrometry, indicated the presence of oligomeric toxin structures in the venom. Complementary proteomic approaches allowed for a qualitative and semi-quantitative profiling of P. nigriventer venom complexity, expanding its known venom proteome diversity. Keywords Phoneutria nigriventer Proteome Spider venom Chitinase