Proteomic Characterization of the Hyaluronidase (EC 3.2.1.35) from the Venom of the Social Wasp Polybia paulista

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dc.contributor.authorAparecido dos Santos Pinto, Jose Roberto [UNESP]
dc.contributor.authordos Santos, Lucilene Delazari [UNESP]
dc.contributor.authorArcuri, Helen Andrade
dc.contributor.authorDias, Nathalia Baptista [UNESP]
dc.contributor.authorPalma, Mario Sergio [UNESP]
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.contributor.institutionUniversidade de São Paulo (USP)
dc.contributor.institutionInstituto de Investigação em Imunologia - Instituto Nacional de Ciência e Tecnologia (III-INCT)
dc.date.accessioned2014-05-20T13:55:08Z
dc.date.available2014-05-20T13:55:08Z
dc.date.issued2012-06-01
dc.description.abstractPolybia paulista wasp venom possesses three major allergens: phospholipase A(1), hyaluronidase and antigen-5. To the best of our knowledge, no hyaluronidase from the venom of Neotropical social wasps was structurally characterized up to this moment, mainly due to its reduced amount in the venom of the tropical wasp species (about 0.5% of crude venom). Four different glycoproteic forms of this enzyme were detected in the venom of the wasp Polybia paulista. In the present investigation, an innovative experimental approach was developed combining 2-D SDS-PAGE with in-gel protein digestion by different proteolytic enzymes, followed by mass spectrometry analysis under collision-induced dissociation CID) conditions for the complete assignment of the protein sequencing. Thus, the most abundant form of this enzyme in P. paulista venom, the hyaluronidase-III, was sequenced, revealing that the first 47 amino acid residues from the N-terminal region, common to other Hymenoptera venom hyaluronidases, are missing. The molecular modeling revealed that hyaluronidase-III has a single polypeptide chain, folded into a tertiary structure, presenting a central (beta/alpha)(5) core with alternation of beta-strands and alpha-helices; the tertiary structure stabilized by a single disulfide bridge between the residues Cys(189) and Cys(201). The structural pattern reported for P. paulista venom hyaluronidase-III is compatible with the classification of the enzyme as member of the family 56 of glycosidase hydrolases. Moreover, its structural characterization will encourage the use of this protein as a model for future development of component-resolved diagnosis.en
dc.description.affiliationUNESP Univ Estadual Paulista, São Paulo State Univ, Inst Biosci Rio Claro, Ctr Study Social Insects,Dept Biol, Rio Claro, SP, Brazil
dc.description.affiliationINCOR HC FMUSP, Discipline Allergy & Immunol, São Paulo, Brazil
dc.description.affiliationInst Res Immunol INCT Iii, São Paulo, Brazil
dc.description.affiliationUnespUNESP Univ Estadual Paulista, São Paulo State Univ, Inst Biosci Rio Claro, Ctr Study Social Insects,Dept Biol, Rio Claro, SP, 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.sponsorshipCoordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)
dc.description.sponsorshipIdFAPESP: 11/51684-1
dc.format.extent625-635
dc.identifierhttp://eurekaselect.com/97510/article
dc.identifier.citationProtein and Peptide Letters. Sharjah: Bentham Science Publ Ltd, v. 19, n. 6, p. 625-635, 2012.
dc.identifier.issn0929-8665
dc.identifier.lattes2901888624506535
dc.identifier.urihttp://hdl.handle.net/11449/19720
dc.identifier.wosWOS:000304442400008
dc.language.isoeng
dc.publisherBentham Science Publ Ltd
dc.relation.ispartofProtein and Peptide Letters
dc.relation.ispartofjcr1.039
dc.relation.ispartofsjr0,429
dc.rights.accessRightsAcesso restrito
dc.sourceWeb of Science
dc.subjectAllergenen
dc.subjecthyaluronidaseen
dc.subjectmass spectrometryen
dc.subjectmolecular modelingen
dc.subjectpeptide sequencingen
dc.subjectwasp venomen
dc.titleProteomic Characterization of the Hyaluronidase (EC 3.2.1.35) from the Venom of the Social Wasp Polybia paulistaen
dc.typeArtigo
dcterms.licensehttp://www.benthamscience.com/permission.php
dcterms.rightsHolderBentham Science Publ Ltd
unesp.author.lattes2901888624506535
unesp.author.orcid0000-0001-5832-1825[2]
unesp.author.orcid0000-0002-7363-8211[5]
unesp.campusUniversidade Estadual Paulista (Unesp), Instituto de Biociências, Rio Claropt

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Artigos - Biologia - IBRC