Functional and structural diversification of the Anguimorpha lizard venom system.

Molecular & Cellular Proteomics : MCP
B G FryWayne C Hodgson

Abstract

Venom has only been recently discovered to be a basal trait of the Anguimorpha lizards. Consequently, very little is known about the timings of toxin recruitment events, venom protein molecular evolution, or even the relative physical diversifications of the venom system itself. A multidisciplinary approach was used to examine the evolution across the full taxonomical range of this ∼130 million-year-old clade. Analysis of cDNA libraries revealed complex venom transcriptomes. Most notably, three new cardioactive peptide toxin types were discovered (celestoxin, cholecystokinin, and YY peptides). The latter two represent additional examples of convergent use of genes in toxic arsenals, both having previously been documented as components of frog skin defensive chemical secretions. Two other novel venom gland-overexpressed modified versions of other protein frameworks were also recovered from the libraries (epididymal secretory protein and ribonuclease). Lectin, hyaluronidase, and veficolin toxin types were sequenced for the first time from lizard venoms and shown to be homologous to the snake venom forms. In contrast, phylogenetic analyses demonstrated that the lizard natriuretic peptide toxins were recruited independently of the ...Continue Reading

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Citations

Jun 29, 2013·Journal of Zoo and Wildlife Medicine : Official Publication of the American Association of Zoo Veterinarians·Ellie J C GoldsteinBryan G Fry
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Aug 11, 2021·Proceedings. Biological Sciences·Alessandro PalciMichael S Y Lee

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