Article
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
Registro en:
FERREIRA, 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.
1879-0240
10.1016/j.ibmb.2010.05.007
Autor
Ferreira, Lígia Maria
Romão, Tatiany Patrícia
Melo Neto, Osvaldo Pompílio de
Silva Filha, Maria Helena Neves Lobo
Resumen
Este 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). Aedes 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. 2050-01-01
Materias
Ítems relacionados
Mostrando ítems relacionados por Título, autor o materia.
-
RAB-5- and RAB-11-dependent vesicle-trafficking pathways are required for plasma membrane repair after attack by bacterial pore-forming toxin
Los, Ferdinand C. O.; Kao, Cheng-Yuan; Smitham, Jane; McDonald, Kent L.; Ha, Christine; Peixoto, Christina A.; Aroian, Raffi V. -
Mycobacterium tuberculosis Rv1419 encodes a secreted 13 kDa lectin with immunological reactivity during human tuberculosis
Nogueira, Lucas L; Cardoso, Fernanda C; Mattos, Ana M; Bordignon, Juliano; Figueiredo, Cláudia P; Dahlstrom, Pedro; Frota, Cristiane C; Santos, Cláudia N. Duarte dos; Chalhoub, Marcelo; Cavada, Benildo Sousa; Teixeira, Henrique C; Oliveira, Sérgio Costa; Barral Netto, Manoel; Bafica, Andre Luiz Barbosa -
Vaccination with the Leishmania major ribosomal proteins plus CpG oligodeoxynucleotides induces protection against experimental cutaneous leishmaniasis in mice
Iborra, Salvador; Parody, Nuria; Abánades, Daniel Ruiz; Bonay, Pedro; Prates, Deboraci Brito; Novais, Fernanda Oliveira; Barral Netto, Manoel; Alonso, Carlos; Soto, Manuel