The defensive functions of plant inhibitors are not restricted to insect enzyme inhibition

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dc.contributor.authorSumikawa, Joana Tomomi
dc.contributor.authorBrito, Marlon Vilela de
dc.contributor.authorRodrigues Macedo, Maria Ligia
dc.contributor.authorUchoa, Adriana F.
dc.contributor.authorMiranda, Antonio [UNIFESP]
dc.contributor.authorAraujo, Ana Paula U.
dc.contributor.authorSilva-Lucca, Rosemeire A.
dc.contributor.authorSampaio, Misako Uemura
dc.contributor.authorOliva, Maria Luiza Vilela [UNIFESP]
dc.contributor.institutionUniversidade Federal de São Paulo (UNIFESP)
dc.contributor.institutionUniv Fed Mato Grosso
dc.contributor.institutionUniv Estadual Fluminense Darcy Ribeiro
dc.contributor.institutionUniversidade de São Paulo (USP)
dc.contributor.institutionUniv Estadual Oeste Parana
dc.date.accessioned2016-01-24T13:59:16Z
dc.date.available2016-01-24T13:59:16Z
dc.date.issued2010-02-01
dc.description.abstractThree plant proteinase inhibitors BbKI (kallikrein inhibitor) and BbCI (cruzipain inhibitor) from Bauhinia bouhinioides, and a BrTI (trypsin inhibitor) from B. rufa, were examined for other effects in Callosobruchus maculatus development; of these only BrTI affected bruchid emergence. BrTI and BbKI share 81% identities in their primary sequences and the major differences between them are the regions comprising the RGD and RGE motifs in BrTI. These sequences were shown to be essential for BrTI insecticidal activity, since a modified BbKI [that is a recombinant form (BbKIm) with some amino acid residues replaced by those found in BrTI sequence] also strongly inhibited insect development. By using synthetic peptides related to the BrTI sequence, YLEAPVARGDGGLA-NH(2) (RGE) and IVYYPDRGETGL-NH(2) (RGE), it was found that the peptide with an RGE sequence was able to block normal development of C. maculatus larvae (ED(50) 0.16% and LD(50) 0.09%), this being even more effective than the native protein. (C) 2009 Elsevier B.V. All rights reserved.en
dc.description.affiliationUniversidade Federal de São Paulo, Escola Paulista Med, Dept Bioquim, BR-04044020 São Paulo, Brazil
dc.description.affiliationUniv Fed Mato Grosso, Dept Nat Sci, BR-79603011 Tres Lagoas, MS, Brazil
dc.description.affiliationUniv Estadual Fluminense Darcy Ribeiro, Lab Prot & Peptide Biochem, CBB, BR-28015620 Campos Dos Goytacazes, RJ, Brazil
dc.description.affiliationUniversidade Federal de São Paulo, Dept Biophys, BR-04044020 São Paulo, Brazil
dc.description.affiliationUniv São Paulo, Inst Fis Sao Carlos, Sao Carlos, SP, Brazil
dc.description.affiliationUniv Estadual Oeste Parana, Ctr Engn & Ciencias Exatas, BR-85903000 Toledo, PR, Brazil
dc.description.affiliationUnifespUniversidade Federal de São Paulo, Escola Paulista Med, Dept Bioquim, BR-04044020 São Paulo, Brazil
dc.description.affiliationUnifespUniversidade Federal de São Paulo, Dept Biophys, BR-04044020 São Paulo, Brazil
dc.description.sourceWeb of Science
dc.description.sponsorshipCoordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)
dc.description.sponsorshipConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.description.sponsorshipFAP/FADA (UNIFESP)
dc.format.extent214-220
dc.identifierhttp://dx.doi.org/10.1016/j.phytochem.2009.10.009
dc.identifier.citationPhytochemistry. Oxford: Pergamon-Elsevier B.V., v. 71, n. 2-3, p. 214-220, 2010.
dc.identifier.doi10.1016/j.phytochem.2009.10.009
dc.identifier.issn0031-9422
dc.identifier.urihttp://repositorio.unifesp.br/handle/11600/32229
dc.identifier.wosWOS:000274827100010
dc.language.isoeng
dc.publisherElsevier B.V.
dc.relation.ispartofPhytochemistry
dc.rightsinfo:eu-repo/semantics/restrictedAccess
dc.rights.licensehttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dc.subjectBauhinia sp.en
dc.subjectFabaceaeen
dc.subjectCaesalpinodaeen
dc.subjectCallosobruchus maculatusen
dc.subjectVigna unguiculataen
dc.subjectLeguminosaeen
dc.subjectCowpeaen
dc.subjectDefense proteinen
dc.subjectInsect attacken
dc.subjectKunitz inhibitorsen
dc.subjectPesticideen
dc.subjectPlant peptidase inhibitorsen
dc.subjectRGDen
dc.subjectTrypsin inhibitoren
dc.titleThe defensive functions of plant inhibitors are not restricted to insect enzyme inhibitionen
dc.typeinfo:eu-repo/semantics/article
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