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Snake venomics of the Siamese Russell's viper (Daboia russelli siamensis) — Relation to pharmacological activities

Risch, Michaela, Georgieva, Dessislava, von Bergen, Martin, Jehmlich, Nico, Genov, Nicolay, Arni, Raghuvir K., Betzel, Christian·2009·Journal of Proteomics
DOI 10.1016/j.jprot.2009.01.006
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Abstract

The venom proteome of Daboia russelli siamensis, a snake of medical importance in several Asian countries, was analysed by 2-D electrophoresis, subsequent MS/MS and enzymatic assays. The proteome comprises toxins from six protein families: serine proteinases, metalloproteinases, phospholipases A(2), L-amino acid oxidases, vascular endothelial growth factors and C-type lectin-like proteins. The venom toxin composition correlates with the clinical manifestation of the Russell's viper bite and explains pathological effects of the venom such as coagulopathy, oedema, hypotensive, necrotic and tissue damaging effects. The vast majority of toxins are potentially involved in coagulopathy and neurotoxic effects. The predominant venom components are proteinases capable of activating blood coagulation factors and promoting a rapid clotting of the blood, and neurotoxic phospholipase A(2)s. The analysis of the venom protein composition provides a catalogue of secreted toxins. The proteome of D. r. siamensis exhibits a lower level of toxin diversity than the proteomes of other viperid snakes. In comparison to the venoms of Vipera ammodytes ammodytes and Vipera ammodytes meridionalis, the venom from D. r. siamensis showed quantitative differences in the proteolytic, phospholipase A(2), L-amino acid oxidase and alkaline phosphatase activities.

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Metadata

Authors
Risch, M., Georgieva, D., von Bergen, M., Jehmlich, N., Genov, N., Arni, R. K., & Betzel, C.
Venue
Journal of Proteomics
Publisher
Elsevier BV
Published
2009-03
Volume
72
Issue
2
Pages
256-269
ISSN
1874-3919
DOI
10.1016/j.jprot.2009.01.006
Cited by
65
References
1
Language
en
Licence
www.elsevier.com/tdm/userlicense/1.0/ (tdm)

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