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Molecular characterization and phylogenetic analysis of JussuMP-I: A RGD-P-III class hemorrhagic metalloprotease from Bothrops jararacussu snake venom

dc.contributor.authorMazzi, Mauricio V.
dc.contributor.authorMagro, Angelo J.
dc.contributor.authorAmui, Saulo F.
dc.contributor.authorOliveira, Clayton Z.
dc.contributor.authorTicli, Fabio K.
dc.contributor.authorStabeli, Rodrigo G.
dc.contributor.authorFuly, Andre L.
dc.contributor.authorRosa, Jose C.
dc.contributor.authorBraz, Antnio S. K.
dc.contributor.authorFontes, Marcos R. M.
dc.contributor.authorSampaio, Suely V.
dc.contributor.authorSoares, Andreimar M.
dc.contributor.institutionUniversidade de São Paulo (USP)
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.contributor.institutionUniv Rondonia
dc.contributor.institutionUniversidade Federal Fluminense (UFF)
dc.date.accessioned2014-05-20T13:49:19Z
dc.date.available2014-05-20T13:49:19Z
dc.date.issued2007-07-01
dc.description.abstractSnake venom metalloproteases (SVMPs) embody zinc-dependent multidomain enzymes responsible for a relevant pathophysiology in envenomation. including local and systemic hemorrhage. The molecular features responsible for hemorrhagic potency of SVMPs have been associated with their multidomains structures which can target these proteins them to several receptors of different tissues and cellular types. BjussuMP-I. a SVMP isolated from the Bothrops jararacussu venom, has been characterized as a P-III hemorrhagic metalloprotease. The complete cDNA sequence of BjussuMP-I with 1641bp encodes open reading frames of 547 amino acid residues, which conserve the common domains of P-III high molecular weight hemorrhagic metalloproteases: (i) pre-pro-peptide, (ii) metalloprotease, (iii) disintegrin-like and (iv) rich cysteine domain. BjussuMP-I induced lyses in fibrin clots and inhibited collagen- and ADP-induced platelet aggregation. We are reporting, for the first time, the primary structure of an RGD-P-III class snake venom metalloprotease. A phylogenetic analysis of the BjussuMP-1 metalloprotease/catalytic domain was performed to get new insights into the molecular evolution of the metalloproteases. A theoretical molecular model of this domain was built through folding recognition (threading) techniques and refined by molecular dynamics simulation. Then, the final BjussuMP-I catalytic domain model was compared to other SVMPs and Reprolysin family proteins in order to identify eventual structural differences, which could help to understand the biochemical activities of these enzymes. The presence of large hydrophobic areas and some conserved surface charge-positive residues were identified as important features of the SVMPs and other metalloproteases. (C) 2006 Elsevier B.V. All rights reserved.en
dc.description.affiliationUniv São Paulo, Dept Anal Clin Toxicol & Bromatol, Fac Ciências Farmaceut Ribeirao Preto, BR-14049 Ribeirao Preto, Brazil
dc.description.affiliationUNESP, Dept Fis & Biofis, Inst Biociencias, Botucatu, SP, Brazil
dc.description.affiliationUniv Rondonia, UNIR, Inst Pesquisa Patol Trop, Porto Velho, RO, Brazil
dc.description.affiliationUniv Fed Fluminense, Inst Biol, Dept Biol Celular & Mol, Niteroi, RJ, Brazil
dc.description.affiliationUSP, FMRP, Dept Biol Celular & Mol & Bioagentes Patogenicos, Ribeirao Preto, Brazil
dc.description.affiliationUSP, FMRP, Ctr Quim Prot, Ribeirao Preto, Brazil
dc.description.affiliationUNESP, Inst Biociencias, Dept Genet, Botucatu, SP, Brazil
dc.description.affiliationUnespUNESP, Dept Fis & Biofis, Inst Biociencias, Botucatu, SP, Brazil
dc.description.affiliationUnespUNESP, Inst Biociencias, Dept Genet, Botucatu, SP, Brazil
dc.format.extent69-85
dc.identifierhttp://dx.doi.org/10.1016/j.jmgm.2006.09.010
dc.identifier.citationJournal of Molecular Graphics & Modelling. New York: Elsevier B.V., v. 26, n. 1, p. 69-85, 2007.
dc.identifier.doi10.1016/j.jmgm.2006.09.010
dc.identifier.issn1093-3263
dc.identifier.urihttp://hdl.handle.net/11449/17570
dc.identifier.wosWOS:000248646500007
dc.language.isoeng
dc.publisherElsevier B.V.
dc.relation.ispartofJournal of Molecular Graphics & Modelling
dc.relation.ispartofjcr1.885
dc.relation.ispartofsjr0,510
dc.rights.accessRightsAcesso restrito
dc.sourceWeb of Science
dc.subjectBothrops jararacussupt
dc.subjectsnake venom hemorrhagic metalloproteasept
dc.subjectcDNApt
dc.subjectphylogenetic analysispt
dc.subjectmolecular evolutionpt
dc.subjectstructural analysispt
dc.titleMolecular characterization and phylogenetic analysis of JussuMP-I: A RGD-P-III class hemorrhagic metalloprotease from Bothrops jararacussu snake venomen
dc.typeArtigo
dcterms.licensehttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dcterms.rightsHolderElsevier B.V.
dspace.entity.typePublication
unesp.author.lattes0059017255172730[2]
unesp.author.orcid0000-0003-2900-8703[9]
unesp.author.orcid0000-0002-4634-6221[10]
unesp.author.orcid0000-0002-0476-920X[6]
unesp.author.orcid0000-0003-3274-180X[11]
unesp.author.orcid0000-0002-4253-6992[2]
unesp.campusUniversidade Estadual Paulista (UNESP), Instituto de Biociências, Botucatupt
unesp.departmentFísica e Biofísica - IBBpt
unesp.departmentGenética - IBBpt

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