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Protein & Peptide Letters

Editor-in-Chief

ISSN (Print): 0929-8665
ISSN (Online): 1875-5305

The Phospholipase A2 Homologues of Snake Venoms: Biological Activities and Their Possible Adaptive Roles

Author(s): Bruno Lomonte, Yamileth Angulo, Mahmood Sasa and Jose Maria Gutierrez

Volume 16, Issue 8, 2009

Page: [860 - 876] Pages: 17

DOI: 10.2174/092986609788923356

Price: $65

Abstract

A particular subgroup of toxins with phospholipase A2 (PLA2) structure, but devoid of this enzymatic activity, is commonly found in the venoms of snakes of the family Viperidae, and known as the PLA2 homologues. Among these, the most frequent type presents a lysine residue at position 49 (Lys49), in substitution of the otherwise conserved aspartate (Asp49) of catalytically-active PLA2s. A brief and updated overview of these toxic PLA2 homologues is presented, emphasizing their various biological activities, both in vivo and in vitro. The relevance of these bioactivities in relation to their possible adaptive roles for the snakes is discussed. Finally, experiments designed to assess the validity of such hypothetical roles are suggested, to stimulate future studies in this field.

Keywords: Snake, venom, myotoxin, phospholipase A2, Lys49 homologues


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