SMase II, a new sphingomyelinase D from Loxosceles laeta venom gland: Molecular cloning, expression, function and structural analysis

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dc.contributor.authorde Santi Ferrara, Guilherme I.
dc.contributor.authorFernandes-Pedrosa, Matheus de F.
dc.contributor.authorJunqueira-de-Azevedo, Inacio de L. M.
dc.contributor.authorGoncalves-de-Andrade, Rute M.
dc.contributor.authorPortaro, Fernanda C. V.
dc.contributor.authorManzoni-de-Almeida, Daniel
dc.contributor.authorMurakami, Mario T.
dc.contributor.authorArni, Raghuvir K. [UNESP]
dc.contributor.authorvan den Berg, Carmen W.
dc.contributor.authorHo, Paulo L.
dc.contributor.authorTambourgi, Denise V.
dc.contributor.institutionInstituto Butantan
dc.contributor.institutionCtr Biol Mol Estrutural
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.contributor.institutionCardiff Univ
dc.date.accessioned2014-05-20T14:02:31Z
dc.date.available2014-05-20T14:02:31Z
dc.date.issued2009-06-01
dc.description.abstractSphingomyelinase D (SMase D) present in the venoms of Loxosceles spiders is the principal component responsible for local and systemic effects observed in the loxoscelism. By using "expressed sequencing tag", it was possible to identify, in a L. laeta venom gland library, clones containing inserts coding for proteins with similarity to SMase D. One of these clones was expressed and the recombinant protein compared with the previously characterized SMase I from L laeta, in terms of their biological, biochemical and structural properties. The new recombinant protein, SMase II, possesses all the biological properties ascribed to the whole venom and SMase I. SMase II shares 40% and 77% sequence similarity with SMase I and Lb3, respectively; the latter, a SMase D isoform from L boned, catalytically inactive. Molecular modeling and molecular dynamics simulations were employed to understand the structural basis, especially the presence of an additional disulfide bridge, in an attempt to account for the observed differences in SMases D activity. (C) 2009 Elsevier Ltd. All rights reserved.en
dc.description.affiliationInst Butantan, Lab Imunoquim, BR-05503900 São Paulo, Brazil
dc.description.affiliationInst Butantan, Ctr Biotecnol, BR-05503900 São Paulo, Brazil
dc.description.affiliationCtr Biol Mol Estrutural, Lab Brasileiro Luz Synchrotron, São Paulo, Brazil
dc.description.affiliationUNESP, IBILCE, Dept Fis, Sao Jose do Rio Preto, Brazil
dc.description.affiliationCardiff Univ, Dept Pharmacol Therapeut & Toxicol, Cardiff, S Glam, Wales
dc.description.affiliationUnespUNESP, IBILCE, Dept Fis, Sao Jose do Rio Preto, Brazil
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.sponsorshipFundação Butantan
dc.format.extent743-753
dc.identifierhttp://dx.doi.org/10.1016/j.toxicon.2009.02.013
dc.identifier.citationToxicon. Oxford: Pergamon-Elsevier B.V. Ltd, v. 53, n. 7-8, p. 743-753, 2009.
dc.identifier.doi10.1016/j.toxicon.2009.02.013
dc.identifier.issn0041-0101
dc.identifier.lattes9162508978945887
dc.identifier.orcid0000-0003-2460-1145
dc.identifier.urihttp://hdl.handle.net/11449/22040
dc.identifier.wosWOS:000266752900007
dc.language.isoeng
dc.publisherPergamon-Elsevier B.V. Ltd
dc.relation.ispartofToxicon
dc.relation.ispartofjcr2.352
dc.relation.ispartofsjr0,692
dc.rights.accessRightsAcesso restrito
dc.sourceWeb of Science
dc.subjectLoxosceles laetaen
dc.subjectVenomen
dc.subjectSphingomyelinase geneen
dc.subjectActivityen
dc.subjectProtein structureen
dc.titleSMase II, a new sphingomyelinase D from Loxosceles laeta venom gland: Molecular cloning, expression, function and structural analysisen
dc.typeArtigo
dcterms.licensehttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dcterms.rightsHolderPergamon-Elsevier B.V. Ltd
unesp.author.lattes9162508978945887[8]
unesp.author.orcid0000-0003-2460-1145[8]
unesp.campusUniversidade Estadual Paulista (Unesp), Instituto de Biociências Letras e Ciências Exatas, São José do Rio Pretopt

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