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

• Published in: Toxicon (Oxford) 2008-03, Vol.51 (4), p.659-671
• Main Authors: Oliveira-Carvalho, Ana Lúcia, Guimarães, Patrícia Ramos, Abreu, Paula Alvarez, Dutra, Denis L.S., Junqueira-de-Azevedo, Inácio L.M., Rodrigues, Carlos Rangel, Ho, Paulo Lee, Castro, Helena C., Zingali, Russolina B.
• Format: Article
• Language: English
• Subjects: Amino Acid Sequence; Animal poisons toxicology. Antivenoms; Animals; Anticoagulants - chemistry; Biological and medical sciences; Bothrops; Bothrops insularis; Crotalid Venoms - chemistry; Electrophoresis 2D; Lectin C-type; Medical sciences; Models, Molecular; Molecular Sequence Data; Phylogenetic; Proteomics; Snake venom; Structure; Thrombin - antagonists & inhibitors; Thrombin inhibitor; Toxicology; Viperidae
• ISSN: 0041-0101; 1879-3150
• DOI: 10.1016/j.toxicon.2007.11.026

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 α and β. 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.