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dc.contributor.authorSantos, Lucilene D.
dc.contributor.authorSantos, Keity S.
dc.contributor.authorde Souza, Bibiana M.
dc.contributor.authorArcuri, Helen A.
dc.contributor.authorCunha-Neto, Edecio
dc.contributor.authorCastro, Fabio Morato
dc.contributor.authorKalil, Jorge Elias
dc.contributor.authorPalma, Mario Sergio [UNESP]
dc.date.accessioned2014-05-20T15:19:28Z
dc.date.available2014-05-20T15:19:28Z
dc.date.issued2007-12-01
dc.identifierhttp://dx.doi.org/10.1016/j.toxicon.2007.06.027
dc.identifier.citationToxicon. Oxford: Pergamon-Elsevier B.V., v. 50, n. 7, p. 923-937, 2007.
dc.identifier.issn0041-0101
dc.identifier.urihttp://hdl.handle.net/11449/30936
dc.description.abstractThe biochemical and functional characterization of wasp venom toxins is an important prerequisite for the development of new tools both for the therapy of the toxic reactions due to envenomation caused by multiple stinging accidents and also for the diagnosis and therapy of allergic reactions caused by this type of venom. PLA(1) was purified from the venom of the neotropical social wasp Polybia paulista by using molecular exclusion and cation exchange chromatographies; its amino acid sequence was determined by using automated Edman degradation and compared to the sequences of other vespid venom PLA(1)'s. The enzyme exists as a 33,961.40 da protein, which was identified as a lipase of the GX class, liprotein lipase superfamily, pancreatic lipases (ab20.3) homologous family and RP2 sub-group of phospholipase. P. paulista PLA(1) is 53-82% identical to the phospholipases from wasp species from Northern Hemisphere. The use restrained-based modeling permitted to describe the 3-D structure of the enzyme, revealing that its molecule presents 23% alpha-helix, 28% beta-sheet and 49% coil. The protein structure has the alpha/beta fold common to many lipases; the core consists of a tightly packed beta-sheet constituted of six-stranded parallel and one anti-parallel beta-strand, surrounded by four alpha-helices. P. paulista PLA(1) exhibits direct hemolytic action against washed red blood cells with activity similar to the Cobra cardiotoxin from Naja naja atra. In addition to this, PLA(1) was immunoreactive to specific IgE from the sera of P. paulista-sensitive patients. (c) 2007 Elsevier Ltd. All rights reserved.en
dc.format.extent923-937
dc.language.isoeng
dc.publisherElsevier B.V.
dc.relation.ispartofToxicon
dc.sourceWeb of Science
dc.subjectwasp venompt
dc.subjectphospholipasept
dc.subjectimmunoreactivitypt
dc.subjectIgEpt
dc.subjectmolecular modelingpt
dc.subjectHymenopterapt
dc.subjecthemolysinpt
dc.subjectallergenpt
dc.titlePurification, sequencing and structural characterization of the phospholipase A(1) from the venom of the social wasp Polybia paulista (Hymenoptera, Vespidae)en
dc.typeArtigo
dcterms.licensehttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dcterms.rightsHolderElsevier B.V.
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.contributor.institutionUniversidade de São Paulo (USP)
dc.description.affiliationUniv Nacl Estadual São Paulo, Ctr Study Social Insects, Inst Biosci Rio Claro, Dept Biol, BR-13506 Rio Claro, SP, Brazil
dc.description.affiliationUniv São Paulo, Fac Med, Discipline Allergy & Immunol InCor, São Paulo, SP, Brazil
dc.description.affiliationUniv São Paulo, SJRP, IBILCE, Dept Phys, São Paulo, Brazil
dc.description.affiliationUnespUniv São Paulo, SJRP, IBILCE, Dept Phys, São Paulo, Brazil
dc.identifier.doi10.1016/j.toxicon.2007.06.027
dc.identifier.wosWOS:000251476400005
dc.rights.accessRightsAcesso restrito
unesp.campusUniversidade Estadual Paulista (Unesp), Instituto de Biociências Letras e Ciências Exatas, São José do Rio Pretopt
dc.identifier.lattes2901888624506535
unesp.advisor.lattes2901888624506535
unesp.author.orcid0000-0001-5832-1825[1]
unesp.author.orcid0000-0002-6211-5773[6]
unesp.author.orcid0000-0002-7363-8211[8]
unesp.author.orcid0000-0002-3699-3345[5]
dc.relation.ispartofjcr2.352
dc.relation.ispartofsjr0,692
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