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dc.contributor.authorSciani, Juliana Mozer-
dc.contributor.authorMarques-Porto, Rafael-
dc.contributor.authorLourenco Junior, Airton-
dc.contributor.authorOrsi, Ricardo de Oliveira-
dc.contributor.authorFerreira Junior, Rui Seabra-
dc.contributor.authorBarraviera, Benedito-
dc.contributor.authorPimenta, Daniel Carvalho-
dc.date.accessioned2014-05-20T13:12:54Z-
dc.date.accessioned2016-10-25T16:33:31Z-
dc.date.available2014-05-20T13:12:54Z-
dc.date.available2016-10-25T16:33:31Z-
dc.date.issued2010-08-01-
dc.identifierhttp://dx.doi.org/10.1016/j.peptides.2010.05.001-
dc.identifier.citationPeptides. New York: Elsevier B.V., v. 31, n. 8, p. 1473-1479, 2010.-
dc.identifier.issn0196-9781-
dc.identifier.urihttp://hdl.handle.net/11449/801-
dc.identifier.urihttp://acervodigital.unesp.br/handle/11449/801-
dc.description.abstractApis mellifera, the European honey bee, is perhaps the most studied insect in the Apidae family. Its venom is comprised basically of melittin, phospholipase A(2), histamine, hyaluronidase, cathecolamines and serotonin. Some of these components have been associated to allergic reactions, among several other symptoms. on the other hand, bee mass-stinging is increasingly becoming a serious public health issue; therefore, the development of efficient serum-therapies has become necessary, with a consequent better characterization of the venom. In this work, we report the isolation and biochemical characterization of melittin-S, an isoform of melittin comprising a Ser residue at the 10th position, from the venom of Africanized A. mellifera. This peptide demonstrated to be less hemolytic than melittin and to adopt a less organized secondary structure, as assessed by circular dichroism spectroscopy. Melittin-S venom contents varied seasonally, and the maximum secretion occurred during the (southern) winter months. Data on the variation of the honey bee venom composition are necessary to guide future immunological studies, aiming for the development of an efficient anti-serum against Africanized A. mellifera venom and, consequently, an effective treatment for the victims of mass-stinging. (C) 2010 Elsevier B.V. All rights reserved.en
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)-
dc.description.sponsorshipConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)-
dc.format.extent1473-1479-
dc.language.isoeng-
dc.publisherElsevier B.V.-
dc.sourceWeb of Science-
dc.subjectApis melliferaen
dc.subjectMelittinen
dc.subjectVenomen
dc.subjectSeasonal variationen
dc.subjectPeptidesen
dc.subjectNatural peptidesen
dc.titleIdentification of a novel melittin isoform from Africanized Apis mellifera venomen
dc.typeoutro-
dc.contributor.institutionInstituto Butantan-
dc.contributor.institutionUniversidade Estadual Paulista (UNESP)-
dc.contributor.institutionUniversidade de São Paulo (USP)-
dc.description.affiliationInst Butantan, Lab Bioquim & Biofis, BR-05503900 São Paulo, Brazil-
dc.description.affiliationUNESP, Fac Med, BR-18603970 Botucatu, SP, Brazil-
dc.description.affiliationFac Med Vet & Zootecnia, BR-18618000 Botucatu, SP, Brazil-
dc.description.affiliationUNESP, Ctr Estudos Venenos & Anim Peconhentos, BR-18610307 Botucatu, SP, Brazil-
dc.description.affiliationUnespUNESP, Fac Med, BR-18603970 Botucatu, SP, Brazil-
dc.description.affiliationUnespUNESP, Ctr Estudos Venenos & Anim Peconhentos, BR-18610307 Botucatu, SP, Brazil-
dc.description.sponsorshipIdFAPESP: 07/02476-1-
dc.description.sponsorshipIdFAPESP: 07/08478-6-
dc.description.sponsorshipIdFAPESP: 06/55545-8-
dc.description.sponsorshipIdFAPESP: 07/05159-7-
dc.description.sponsorshipIdCNPq: 470873/2007-8-
dc.identifier.doi10.1016/j.peptides.2010.05.001-
dc.identifier.wosWOS:000280663600008-
dc.rights.accessRightsAcesso restrito-
dc.relation.ispartofPeptides-
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