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MBE Advance Access published online on March 10, 2004

Molecular Biology and Evolution, doi:10.1093/molbev/msh091
Molecular Biology and Evolution © Society for Molecular Biology and Evolution 2004; all rights reserved
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Accepted December 30, 2003
© 2004 Molecular Biology and Evolution © Society for Molecular Biology and Evolution 2004; all rights reserved.

Original Articles

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

B. G. Fry 1* and W. Wüster 2

1 Australian Venom Research Unit, Department of Pharmacology, University of Melbourne, Parkville, Vic 3010 Australia
2 School of Biological Sciences, University of Wales, Bangor LL57 2UW, Wales, UK

* To whom correspondence should be addressed. E-mail: bgf{at}unimelb.edu.au.


   Abstract

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 non-venom proteins. Out of eight toxin families analyzed, four provided clear evidence of recruitment into the snake venom proteome prior to the diversification of the advanced snakes (Kunitz-type protease inhibitors, CRISP toxins, M12B peptidases, nerve growth factor toxins), and two were equivocal (cystatin toxins and galactose-binding lectins). In two others (phospholipase A2 and CNP/BPP-type natriuretic toxins), the non-monophyly of venom toxins demonstrates that presence of these proteins in elapids and viperids results from independent recruitment events. ANP/BNP-type natriuretic toxins may also be an ancestral toxin family. These results provide strong additional evidence that venom evolved once, at the base of the advanced snake radiation, rather than evolving multiple times in different lineages. Moreover, they provide a first insight into the composition of the earliest ophidian venoms, and point the way towards 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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