Citation

Oliveira-Carvalho AL, Guimarães PR, Abreu PA, Dutra DL, Junqueira-de-Azevedo IL, Rodrigues CR, Ho PL, Castro HC, Zingali RB. Toxicon 2008; 51(4): 659-671.

Affiliation

Rede Proteômica do Rio de Janeiro and Laboratório de Hemostase e Venenos, Unidade de Espectrometria de Massas e Proteômica, Instituto de Bioquímica Médica-ICB, Universidade Federal do Rio de Janeiro, Rio de Janeiro/RJ, Brazil.

Copyright

(Copyright © 2008, Elsevier Publishing)

DOI

10.1016/j.toxicon.2007.11.026

PMID

18221976

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 alpha and beta. 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.

Language: en