The diversity of bioactive proteins in Australian snake venoms

Birrell, G. W., Earl, S. T. H., Wallis, T. P., Masci, P. P., de Jersey, J., Gorman, J. J. and Lavin, M. F. (2007) The diversity of bioactive proteins in Australian snake venoms. Molecular & Cellular Proteomics, 6 6: 973-986. doi:10.1074/mcp.M600419-MCP200


Author Birrell, G. W.
Earl, S. T. H.
Wallis, T. P.
Masci, P. P.
de Jersey, J.
Gorman, J. J.
Lavin, M. F.
Title The diversity of bioactive proteins in Australian snake venoms
Journal name Molecular & Cellular Proteomics   Check publisher's open access policy
ISSN 1535-9476
Publication date 2007-02-01
Sub-type Article (original research)
DOI 10.1074/mcp.M600419-MCP200
Volume 6
Issue 6
Start page 973
End page 986
Total pages 14
Editor Burlingame, A. L.
Bradshaw, R. A.
Place of publication Bethesda, USA
Publisher American Society for Biochemistry and Molecular Biology Inc
Language eng
Subject 320305 Medical Biochemistry - Proteins and Peptides
C1
730106 Cardiovascular system and diseases
Abstract Australian elapid snakes are among the most venomous in the world. Their venoms contain multiple components that target blood hemostasis, neuromuscular signaling, and the cardiovascular system. We describe here a comprehensive approach to separation and identification of the venom proteins from 18 of these snake species, representing nine genera. The venom protein components were separated by two-dimensional PAGE and identified using mass spectrometry and de novo peptide sequencing. The venoms are complex mixtures showing up to 200 protein spots varying in size from < 7 to over 150 kDa and in pl from 3 to > 10. These include many proteins identified previously in Australian snake venoms, homologs identified in other snake species, and some novel proteins. In many cases multiple trains of spots were typically observed in the higher molecular mass range (> 20 kDa) (indicative of post-translational modification). Venom proteins and their post-translational modifications were characterized using specific kantibodies, phosphoprotein- and glycoprotein-specific stains, enzymatic digestion, lectin binding, and antivenom reactivity. In the lower molecular weight range, several proteins were identified, but the predominant species were phospholipase A(2) and alpha-neurotoxins, both represented by different sequence variants. The higher molecular weight range contained proteases, nucleotidases, oxidases, and homologs of mammalian coagulation factors. This information together with the identification of several novel proteins (metalloproteinases, vespryns, phospholipase A(2) inhibitors, protein-disulfide isomerase, 5'-nucleotidases, cysteinerich secreted proteins, C-type lectins, and acetylcholinesterases) aids in understanding the lethal mechanisms of elapid snake venoms and represents a valuable resource for future development of novel human therapeutics.
Keyword Biochemical Research Methods
Coagulation-factor-xa
Amino-acid-sequence
Pseudonaja-textilis-textilis
Nerve Growth-factor
Gated Ion Channels
King Cobra Venom
Prothrombin Activators
Phospholipase A(2)
Brown Snake
Disulfide Isomerization
Q-Index Code C1
Q-Index Status Confirmed Code

Document type: Journal Article
Sub-type: Article (original research)
Collections: Excellence in Research Australia (ERA) - Collection
2008 Higher Education Research Data Collection
School of Medicine Publications
 
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Created: Tue, 19 Feb 2008, 03:28:33 EST