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Molecular diversity in venom from the Australian brown snake, pseudonaja textilis.

Birrell GW, Earl S, Masci PP, de Jersey J, Wallis TP, Gorman JJ, Lavin MF

Cancer and Cell Biology, Queensland Institute of Medical Research, Brisbane, Queensland 4036.

Venom from the Australian elapid Pseudonaja textilis (Common or Eastern Brown snake), is the second most toxic snake venom known and is the most common cause of death from snake bite in Australia. This venom is known to contain a prothrombin activator complex, serine proteinase inhibitors, various phospholipase A2s, and pre- and postsynaptic neurotoxins. In this study, we have performed a proteomic identification of the venom using two dimensional gel electrophoresis, mass spectrometry and de novo peptide sequencing. We have identified most of the venom proteins including proteins previously not known to be present in the venom. In addition, we used immunoblotting and post-translational modification-specific enzyme stains and antibodies that reveal the complexity and regional diversity of the venom. Modifications observed include phosphorylation, -carboxylation and glycosylation. Glycoproteins were further characterised by enzymatic deglycosylation and by lectin binding specificity. The venom contains an abundance of glycoproteins with N-linked sugars that include glucose/mannose, N-acetyl galactosamine, N-acetyl glucosamine and sialic acids. Additionally, there are multiple isoforms of mammalian coagulation factors that comprise a significant proportion of the venom. Indeed two of the identified proteins, a procoagulant and a plasmin inhibitor, are currently in development as human therapeutics.

Published 14 November 2005 in Mol Cell Proteomics.
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