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Identification and characterization of a new member of snake venom thrombin inhibitors from Bothrops insularis using a proteomic approach

Authors
  • OLIVEIRA-CARVALHO, Ana Lucia
  • GUIMARAES, Patricia Ramos
  • ABREU, Paula Alvarez
  • DUTRA, Denis L. S.
  • JUNQUEIRA-DE-AZEVEDO, Inacio L. M.
  • RODRIGUES, Carlos Rangel
  • HO, Paulo Lee
  • CASTRO, Helena C.
  • ZINGALI, Russolina B.
Publication Date
Jan 01, 2008
Source
Biblioteca Digital da Produção Intelectual da Universidade de São Paulo (BDPI/USP)
Keywords
Language
English
License
Unknown
External links

Abstract

Snake venom C-type lectin-like proteins (CLPs) are ubiquitously found in Viperidae snake venoms and differ from the C-type lectins as they display different biological activities but no carbohydrate-binding activity. Previous analysis of the transcriptome obtained from the Bothrops insularis venom gland showed the presence of two clusters homologous to bothrojaracin (BJC) chains a and P. In an effort to identify a new BJC-like molecule, we used an approach associated with proteomic technologies to identify the presence of the expressed protein and then to purify and characterize a new thrombin inhibitor from B. insularis venom. We also constructed homology models of this protein and BJC, which were compared with other C-type lectin-like family members and revealed several conserved features of this intriguing snake venom toxin family. (C)0 2007 Elsevier Ltd. All rights reserved.

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