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Originally published In Press as doi:10.1074/mcp.M500270-MCP200 on November 10, 2005.
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Molecular & Cellular Proteomics 5:379-389, 2006.
© 2006 by The American Society for Biochemistry and Molecular Biology, Inc.

Research

Molecular Diversity in Venom from the Australian Brown Snake, Pseudonaja textilis*,S

Geoff W. Birrell{ddagger}, Stephen Earl{ddagger},§, Paul P. Masci, John de Jersey||, Tristan P. Wallis**, Jeffrey J. Gorman** and Martin F. Lavin{ddagger},¶,{ddagger}{ddagger}

From {ddagger} The Queensland Institute of Medical Research, P. O. Royal Brisbane Hospital, Brisbane 4029, § Central Clinical Division and Southern Clinical Division, Faculty of Health Sciences, University of Queensland, Brisbane 4029, and || School of Molecular and Microbial Sciences and ** Institute for Molecular Biosciences, University of Queensland, Brisbane 4072, Australia

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 performed a proteomic identification of the venom using two-dimensional gel electrophoresis, mass spectrometry, and de novo peptide sequencing. We 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, {gamma}-carboxylation, and glycosylation. Glycoproteins were further characterized by enzymatic deglycosylation and by lectin binding specificity. The venom contains an abundance of glycoproteins with N-linked sugars that include glucose/mannose, N-acetylgalactosamine, N-acetylglucosamine, 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 therapeutic agents.

{ddagger}{ddagger} To whom correspondence should be addressed: The Queensland Cancer Fund Research Unit, The Queensland Inst. of Medical Research, P. O. Box Royal Brisbane Hospital, Herston, Brisbane 4029, Australia. Tel.: 617-3362-0341; Fax: 617-3362-0106; E-mail: martin.lavin{at}qimr.edu.au


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