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(Referência obtida automaticamente do Web of Science, por meio da informação sobre o financiamento pela FAPESP e o número do processo correspondente, incluída na publicação pelos autores.)

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

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Autor(es):
Tashima, Alexandre K. [1] ; Sanz, Libia [2] ; Camargo, Antonio C. M. [1] ; Serrano, Solange M. T. [1] ; Calvete, Juan J. [2]
Número total de Autores: 5
Afiliação do(s) autor(es):
[1] Inst Butantan, Lab Especial Toxinol Aplicada, CAT Cepid, BR-05503900 Sao Paulo - Brazil
[2] CSIC, Inst Biomed Valencia, Valencia 46010 - Spain
Número total de Afiliações: 2
Tipo de documento: Artigo Científico
Fonte: JOURNAL OF PROTEOMICS; v. 71, n. 4, p. 473-485, OCT 7 2008.
Citações Web of Science: 51
Resumo

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 PLA(2) 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 PLA(2) 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. (C) 2008 Elsevier B.V. All rights reserved. (AU)

Processo FAPESP: 98/14307-9 - Center for Applied Toxinology
Beneficiário:Hugo Aguirre Armelin
Modalidade de apoio: Auxílio à Pesquisa - Centros de Pesquisa, Inovação e Difusão - CEPIDs