Molecular diversity in venom from the Australian Brown Snake, Pseudonaja textilis

Birrell, GW, Earl, S, Masci, PP, de Jersey, J, Wallis, TP, Gorman, JJ and Lavin, MF (2006) Molecular diversity in venom from the Australian Brown Snake, Pseudonaja textilis. Molecular and Cellular Proteomics, 5 2: 379-389. doi:10.1074/mcp.M500270-MCP200

Author Birrell, GW
Earl, S
Masci, PP
de Jersey, J
Wallis, TP
Gorman, JJ
Lavin, MF
Title Molecular diversity in venom from the Australian Brown Snake, Pseudonaja textilis
Journal name Molecular and Cellular Proteomics   Check publisher's open access policy
ISSN 1535-9476
Publication date 2006-02-01
Sub-type Article (original research)
DOI 10.1074/mcp.M500270-MCP200
Volume 5
Issue 2
Start page 379
End page 389
Total pages 11
Place of publication Bethesda, USA
Publisher American Society for Biochemistry & Molecular Biology
Language eng
Subject 0608 Zoology
1101 Medical Biochemistry and Metabolomics
Abstract 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 A(2)s, 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.
Keyword Biochemical Research Methods
2-dimensional Gel-electrophoresis
Prothrombin Activator
Q-Index Code C1

Document type: Journal Article
Sub-type: Article (original research)
Collections: Excellence in Research Australia (ERA) - Collection
School of Medicine Publications
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Created: Wed, 15 Aug 2007, 18:59:36 EST