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Molecular characterization of BjussuSP-I, a new thrombin-like enzyme with procoagulant and kallikrein-like activity isolated from Bothrops jararacussu snake venom

2007; Elsevier BV; Volume: 90; Issue: 3 Linguagem: Inglês

10.1016/j.biochi.2007.10.005

1638-6183

Carolina Oliveira de Santana, Carolina P. Bernardes, Luíz Fernando Moreira Izidoro, Maurício V. Mazzi, Sandro G. Soares, André Lopes Fuly, Russolina B. Zingali, Ângelo J. Magro, Antônio Sérgio Kimus Braz, Marcos R.M. Fontes, Rodrigo G. Stábeli, Suely Vilela Sampaio, Andreimar M. Soares,

Biochemical and Structural Characterization

A thrombin-like enzyme, named BjussuSP-I, isolated from Bothrops jararacussu snake venom, is an acidic single-chain glycoprotein with Mr = 61,000, pI ∼ 3.8 and 6% sugar. BjussuSP-I shows high proteolytic activity upon synthetic substrates, such as S-2238 and S-2288. It also shows procoagulant and kallikrein-like activity, but is unable to act on platelets and plasmin. These activities are inhibited by specific inhibitors of this class of enzymes. The complete cDNA sequence of BjussuSP-I with 696 bp encodes open reading frames of 232 amino acid residues, which conserve the common domains of thrombin-like serine proteases. BjussuSP-I shows a high structural homology with other thrombin-like enzymes from snake venoms where common amino acid residues are identified as those corresponding to the catalytic site and subsites S1, S2 and S3 already reported. In this study, we also demonstrated the importance of N-linked glycans to improve thrombin-like activity of BjussuSP-I toxin.