Expression of mRNAs coding for VAP1/crotastatin-like metalloproteases in the venom glands of three South American pit vipers assessed by quantitative real-time PCR

• Autor(a) principal: Tavares, N.A.C.
• Data de Publicação: 2008
• Outros Autores: Correia, J.M., Guarnieri, M.C., Lima-Filho, J.L., Prieto-da-Silva, A.R.B., Rádis-Baptista, Gandhi
• Tipo de documento: Artigo
• Idioma: eng
• Título da fonte: Repositório Institucional da Universidade Federal do Ceará (UFC)
• Texto Completo: http://www.repositorio.ufc.br/handle/riufc/59748
• topic: Toxina; Veneno

Snake venom metalloproteases encompass a large family of toxins, with approximately 200 members already catalogued, which exhibit a diversity of structures and biological functions. From this relatively large number, only a dozen examples of apoptosis-inducing metalloproteases, like VAP1 and 2 from the venom of Crotalus atrox, are known. Since most VAP1-like toxins ever characterized were purified from the venom of Viperidae species inhabiting diverse places on earth, we investigate the expression of VAP-like metalloproteases in the venom gland of three representative pit vipers of the Brazilian territory. By molecular cloning and quantitative real-time polymerase chain reaction, using as calibrator gene the Crotalus durissus terrificus homolog of VAP1, named crotastatin, it is reported here that VAP1/crotastatin-like homologues in the venom gland of Bothrops atrox, C. d. cascavella and Lachesis m. rhombeata are expressed at different levels. Hence, batroxstatins, the crotastatin-like precursors from B. atrox, are expressed 87 times more than crotastatin-1, from C. d. cascavella, and 7.5-fold that lachestatins, from L. m. rhombeata. Moreover, in silico structural analysis of amino acid sequences indicates that batroxstatin2, crotastatins and lachestatin-1 and -2 which share the archetypal motifs and metalbinding sites of VAP1, are subgrouped in a branch that comprises some apoptosis-inducing toxins.