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

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dc.contributor.authorRisch, Michaela
dc.contributor.authorGeorgieva, Dessislava
dc.contributor.authorvon Bergen, Martin
dc.contributor.authorJehmlich, Nico
dc.contributor.authorGenov, Nicolay
dc.contributor.authorArni, Raghuvir K. [UNESP]
dc.contributor.authorBetzel, Christian
dc.contributor.institutionUniv Hamburg
dc.contributor.institutionUFZ Helmholtz Ctr Environm Res
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.contributor.institutionBulgarian Acad Sci
dc.date.accessioned2014-05-20T14:02:37Z
dc.date.available2014-05-20T14:02:37Z
dc.date.issued2009-03-06
dc.description.abstractThe 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 A2, L-amino acid oxidase and alkaline phosphatase activities. (c) 2009 Published by Elsevier B.V.en
dc.description.affiliationUniv Hamburg, Inst Biochem & Mol Biol, Lab Struct Biol Infect & Inflammat, DESY, D-22603 Hamburg, Germany
dc.description.affiliationUFZ Helmholtz Ctr Environm Res, Dept Prote, D-04318 Leipzig, Germany
dc.description.affiliationUNESP, IBILCE, Dept Phys, BR-15054000 Sao Jose do Rio Preto, Brazil
dc.description.affiliationBulgarian Acad Sci, Inst Organ Chem, Sofia 1000, Bulgaria
dc.description.affiliationUnespUNESP, IBILCE, Dept Phys, BR-15054000 Sao Jose do Rio Preto, Brazil
dc.description.sponsorshipDeutsche Forschungsgemeinschaft (DFG)
dc.description.sponsorshipBulgarian National Foundation for Scientific Research
dc.description.sponsorshipIdDFG: 1443-18-1
dc.description.sponsorshipIdBulgarian National Foundation for Scientific Research: TK-B 1610/06
dc.format.extent256-269
dc.identifierhttp://dx.doi.org/10.1016/j.jprot.2009.01.006
dc.identifier.citationJournal of Proteomics. Amsterdam: Elsevier B.V., v. 72, n. 2, p. 256-269, 2009.
dc.identifier.doi10.1016/j.jprot.2009.01.006
dc.identifier.issn1874-3919
dc.identifier.lattes9162508978945887
dc.identifier.orcid0000-0003-2460-1145
dc.identifier.urihttp://hdl.handle.net/11449/22074
dc.identifier.wosWOS:000264574500013
dc.language.isoeng
dc.publisherElsevier B.V.
dc.relation.ispartofJournal of Proteomics
dc.relation.ispartofjcr3.722
dc.relation.ispartofsjr1,430
dc.rights.accessRightsAcesso restrito
dc.sourceWeb of Science
dc.subjectProteomeen
dc.subjectSnake venomen
dc.subjectProtein familyen
dc.subjectDaboia russelli siamensisen
dc.subject2-D electrophoresisen
dc.titleSnake venomics of the Siamese Russell's viper (Daboia russelli siamensis) - Relation to pharmacological activitiesen
dc.typeArtigo
dcterms.licensehttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dcterms.rightsHolderElsevier B.V.
unesp.author.lattes9162508978945887[6]
unesp.author.orcid0000-0003-2732-2977[3]
unesp.author.orcid0000-0002-5638-6868[4]
unesp.author.orcid0000-0003-2460-1145[6]
unesp.campusUniversidade Estadual Paulista (Unesp), Instituto de Biociências Letras e Ciências Exatas, São José do Rio Pretopt

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Artigos - Física - IBILCE