Snake venomics of the Brazilian pitvipers Bothrops cotiara and Bothrops fonsecai. Identification of taxonomy markers

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• 作者：Alex ; re K. Tashima ; Libia Sanz ; Antonio C.M. Camargo ; Solange M.T. Serrano ; Juan J. Calvete
• 关键词：Snake venomics ; Bothrops cotiara ; Bothrops fonsecai ; Snake venom protein families ; Proteomics ; Viperid toxins ; N-terminal sequencing ; Mass spectrometry ; Snake phylogeny ; Taxonomy marker
• 刊名：Journal of Proteomics
• 出版年：2008
• 出版时间：7 October 2008
• 年：2008
• 卷：71
• 期：4
• 页码：473-485
• 全文大小：1172 K

文摘

We report the proteomic characterization of venom of the pitvipers Bothrops cotiara and Bothrops fonsecai. Crude venoms were fractionated by reverse-phase HPLC, followed by SDS-PAGE, N-terminal sequencing, MALDI-TOF mass fingerprinting, and CID-MS/MS. Each venom contained around 30 proteins in the range of 7–110 kDa belonging to only 8 (B. cotiara) and 9 (B. fonsecai) families which may target the hemostatic system, albeit distinctly distributed among the two species. B. cotiara and B. fonsecai share medium-sized disintegrins, disintegrin-like/cysteine-rich (DC) fragments, snake venom vascular endothelial growth factor, cysteine-rich secretory proteins, serine proteinases, C-type lectins, l-amino acid oxidase, and Zn²⁺-dependent metalloproteinases. In addition, B. fonsecai expresses a high abundance PLA₂ molecule (13,890 Da), whereas PLA₂ molecules were not detected in B. cotiara's venom. This stricking finding is in line with previous biochemical analyses showing the absence of phospholipasic activity in the venom of B. cotiara. The potential adaptive significance of the lack of PLA₂ molecules is enigmatic, and alternative explanations are discussed. B. fonsecai is morphologically extremely similar to B. cotiara. Our comparative proteomic analysis shows that compositional differences between their venoms can be employed as a taxonomy signature for unambiguous species identification independently of geographic origin and morphological characteristics.