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

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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: Lys49 homologues; Snake; myotoxin; phospholipase A2; venom

Document Type: Research Article


Publication date: 2009-08-01

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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