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MBE Advance Access originally published online on March 10, 2004
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Mol. Biol. Evol. 21(5):870-883. 2004
DOI: 10.1093/molbev/msh091
© 2004 by the Society for Molecular Biology and Evolution. ISSN: 0737-4038

Assembling an Arsenal: Origin and Evolution of the Snake Venom Proteome Inferred from Phylogenetic Analysis of Toxin Sequences

B. G. Fry* and W. Wüster{dagger}

* Australian Venom Research Unit, Department of Pharmacology, University of Melbourne, Parkville, Australia
{dagger} School of Biological Sciences, University of Wales, Bangor, Wales, UK

E-mail: bgf{at}unimelb.edu.au.

We analyzed the origin and evolution of snake venom toxin families represented in both viperid and elapid snakes by means of phylogenetic analysis of the amino acid sequences of the toxins and related nonvenom proteins. Out of eight toxin families analyzed, five provided clear evidence of recruitment into the snake venom proteome before the diversification of the advanced snakes (Kunitz-type protease inhibitors, CRISP toxins, galactose-binding lectins, M12B peptidases, nerve growth factor toxins), and one was equivocal (cystatin toxins). In two others (phospholipase A2 and natriuretic toxins), the nonmonophyly of venom toxins demonstrates that presence of these proteins in elapids and viperids results from independent recruitment events. The ANP/BNP natriuretic toxins are likely to be basal, whereas the CNP/BPP toxins are Viperidae only. Similarly, the lectins were recruited twice. In contrast to the basal recruitment of the galactose-binding lectins, the C-type lectins were shown to be Viperidae only, with the {alpha}-chains and ß-chains resulting from an early duplication event. These results provide strong additional evidence that venom evolved once, at the base of the advanced snake radiation, rather than multiple times in different lineages, with these toxins also present in the venoms of the "colubrid" snake families. Moreover, they provide a first insight into the composition of the earliest ophidian venoms and point the way toward a research program that could elucidate the functional context of the evolution of the snake venom proteome.

Key Words: venom • evolution • multigene family • Elapidae • Viperidae • colubrid • snake


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