The Venomics of Bothrops alternatus is a Pool of Acidic Proteins with Predominant Hemorrhagic and Coagulopathic Activities

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dc.contributor.authorOehler, Michaela
dc.contributor.authorGeorgieva, Dessislava
dc.contributor.authorSeifert, Jana
dc.contributor.authorvon Bergen, Martin
dc.contributor.authorArni, Raghuvir K. [UNESP]
dc.contributor.authorGenov, Nicolay
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.accessioned2014-05-20T14:02:33Z
dc.date.available2014-05-20T14:02:33Z
dc.date.issued2010-05-01
dc.description.abstractThe venom proteome of Bothrops alternatus, a venomous snake widespread in South America, was analyzed by 2-D electrophoresis followed by mass spectrometric analysis and determination of enzymatic activities. The venomic composition revealed that metallo- and serine proteinases play primary roles in the pathogenesis of the envenomation by this pitviper. The identified 100 venom components with molecular masses from 10 to 100 kDa belong to six protein families: metalloproteinases, serine/thrombin-like proteinases, phospholipases A(2), L-amino acid oxidases, disintegrins and thrombin inhibitors. Metalloproteinases predominate and belong exclusively to the P-III class including the most potent hemorrhagic toxins. They represent 50% of all identified proteins. Two isoforms were identified: homologous to jararhagin, a hemorrhagic toxin, and to beritractivase, a nonhemorrhagic and pro-coagulant metalloproteinase. The B. alternatus venom is a rich source of proteins influencing the blood coagulation system with a potential for medical application. The isoelectric points of the components are distributed in the acidic pH range (the p/values are between 4 and 7) and no basic proteins were detected.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, Helmholtz Ctr Environm Res, Dept Prote, D-04318 Leipzig, Germany
dc.description.affiliationUNESP, Dept Phys, IBILCE, BR-15054000 Sao Jose do Rio Preto, SP, Brazil
dc.description.affiliationBulgarian Acad Sci, Inst Organ Chem, BU-1113 Sofia, Bulgaria
dc.description.affiliationUnespUNESP, Dept Phys, IBILCE, BR-15054000 Sao Jose do Rio Preto, SP, Brazil
dc.description.sponsorshipDeutsche Forschungsgemeinschaft (DFG)
dc.description.sponsorshipBulgarian National Foundation for Scientific Research
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.description.sponsorshipConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.description.sponsorshipIdDFG: BE 1443-18-1
dc.description.sponsorshipIdBulgarian National Foundation for Scientific Research: TK-B-1610/06
dc.description.sponsorshipIdFAPESP: 07/54865-1
dc.description.sponsorshipIdCNPq: 303593/2009-1
dc.description.sponsorshipIdCNPq: 474989/2009-7
dc.format.extent2422-2437
dc.identifierhttp://dx.doi.org/10.1021/pr901128x
dc.identifier.citationJournal of Proteome Research. Washington: Amer Chemical Soc, v. 9, n. 5, p. 2422-2437, 2010.
dc.identifier.doi10.1021/pr901128x
dc.identifier.issn1535-3893
dc.identifier.lattes9162508978945887
dc.identifier.orcid0000-0003-2460-1145
dc.identifier.urihttp://hdl.handle.net/11449/22051
dc.identifier.wosWOS:000277353200032
dc.language.isoeng
dc.publisherAmer Chemical Soc
dc.relation.ispartofJournal of Proteome Research
dc.relation.ispartofjcr3.950
dc.relation.ispartofsjr1,818
dc.rights.accessRightsAcesso restrito
dc.sourceWeb of Science
dc.subjectSnake venomicen
dc.subjectBothrops alternatusen
dc.subject2-D electrophoresisen
dc.titleThe Venomics of Bothrops alternatus is a Pool of Acidic Proteins with Predominant Hemorrhagic and Coagulopathic Activitiesen
dc.typeArtigo
dcterms.licensehttp://pubs.acs.org/page/copyright/journals/faqs.html
dcterms.rightsHolderAmer Chemical Soc
unesp.author.lattes9162508978945887[5]
unesp.author.orcid0000-0003-2460-1145[5]
unesp.campusUniversidade Estadual Paulista (Unesp), Instituto de Biociências Letras e Ciências Exatas, São José do Rio Pretopt

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Artigos - Física - IBILCE