Identification and characterization of a new member of snake venom thrombin inhibitors from Bothrops insularis using a proteomic approach.
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.
Oliveira-Carvalho
Ana Lúcia
AL
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.
Guimarães
Patrícia Ramos
PR
Abreu
Paula Alvarez
PA
Dutra
Denis L S
DL
Junqueira-de-Azevedo
Inácio L M
IL
Rodrigues
Carlos Rangel
CR
Ho
Paulo Lee
PL
Castro
Helena C
HC
Zingali
Russolina B
RB
D000595:Amino Acid Sequence; D000818:Animals; D000925:Anticoagulants / Q000737:chemistry*; D017837:Bothrops; D003435:Crotalid Venoms / Q000737:chemistry*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D040901:Proteomics; D013917:Thrombin / Q000037:antagonists & inhibitors*
D000925:Anticoagulants; D003435:Crotalid Venoms; D013917:Thrombin