dc.creatorFerreira, Lígia Maria
dc.creatorRomão, Tatiany Patrícia
dc.creatorMelo Neto, Osvaldo Pompílio de
dc.creatorSilva Filha, Maria Helena Neves Lobo
dc.date2018-04-26T13:59:55Z
dc.date2018-04-26T13:59:55Z
dc.date2010
dc.date.accessioned2023-09-26T23:22:52Z
dc.date.available2023-09-26T23:22:52Z
dc.identifierFERREIRA, L. M. et al. The orthologue to the Cpm1/Cqm1 receptor in Aedes aegypti is expressed as a midgut GPI-anchored α-glucosidase, which does not bind to the insecticidal binary toxin. Insect Biochemistry and Molecular Biology, v. 40, n. 8, p. 604–610, ago. 2010.
dc.identifier1879-0240
dc.identifierhttps://www.arca.fiocruz.br/handle/icict/26130
dc.identifier10.1016/j.ibmb.2010.05.007
dc.identifier.urihttps://repositorioslatinoamericanos.uchile.cl/handle/2250/8889947
dc.descriptionEste estudo foi apoiado pelas agências de fomento brasileiras Conselho Nacional de Pesquisa (CNPq Brasil, bolsa 471911 / 2006-2) e Fundação de Amparo à Ciência e Tecnologia do Estado de Pernambuco (FACEPE Brasil, outorga APQ 0427-2.13 / 08).
dc.descriptionAedes aegypti larvae are refractory to the insecticidal binary (Bin) toxin from Bacillus sphaericus, which is not able to bind to its target tissue in the larval midgut. In contrast, Culex pipiens larvae are highly susceptible to that toxin, which targets its midgut brush border membranes (BBMF) through the binding of the BinB subunit to specific receptors, the Cpm1/Cqm1 membrane-bound α-glucosidases. The identification of an Ae. aegypti gene encoding a Cpm1/Cqm1 orthologue, here named Aam1, led to the major goal of this study which was to investigate its expression. The aam1 transcript was found in larvae and adults from Ae. aegypti and a ≈73-kDa protein was recognized by an anti-Cqm1 antibody in midgut BBMF. The Aam1 protein displayed α-glucosidase activity and localized to the midgut epithelium, bound through a GPI anchor, similarly to Cpm1/Cqm1. However, no binding of native Aam1 was observed to the recombinant BinB subunit. Treatment of both proteins with endoglycosidase led to changes in the molecular weight of Aam1, but not Cqm1, implying that the former was glycosylated. The findings from this work rule out lack of receptors in larval stages, or its expression as soluble proteins, as a reason for Ae. aegypti refractoriness to Bin toxin.
dc.description2050-01-01
dc.formatapplication/pdf
dc.languageeng
dc.publisherElsevier
dc.rightsrestricted access
dc.subjectToxina bin
dc.subjectBacillus sphaericus
dc.subjectBiolarvicidas
dc.subjectReceptor
dc.subjectLigação de toxinas
dc.subjectGlicosilação
dc.subjectBin toxin
dc.subjectBacillus sphaericus
dc.subjectBiolarvicides
dc.subjectReceptor
dc.subjectToxin binding
dc.subjectGlycosylation
dc.subjectAedes / enzimologia
dc.subjectAedes / genética
dc.subjectAedes / crescimento e desenvolvimento
dc.subjectAedes / metabolismo
dc.subjectAnimais
dc.subjectToxinas bacterianas / metabolismo
dc.subjectSistema Digestivo / enzimologia
dc.subjectSistema Digestivo / metabolismo
dc.subjectExpressão genetica
dc.subjectGlicosilfosfatidilinositóis / metabolismo
dc.subjectProteínas de Insetos / genética
dc.subjectProteínas de Insetos / metabolismo
dc.subjectInseticidas / metabolismo
dc.subjectLarva / enzimologia
dc.subjectLarva / genética
dc.subjectLarva / metabolismo
dc.subjectDados de Sequencia Molecular
dc.subjectLigação proteica
dc.subjectalfa-glucosidases / genética
dc.subjectalfa-glucosidases / metabolismo
dc.titleThe orthologue to the Cpm1/Cqm1 receptor in Aedes aegypti is expressed as a midgut GPI-anchored α-glucosidase, which does not bind to the insecticidal binary toxin
dc.typeArticle


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