Please use this identifier to cite or link to this item: https://www.arca.fiocruz.br/handle/icict/20074
Title: N-glycosylation influences the catalytic activity of mosquito α-glucosidases associated with susceptibility or refractoriness to Lysinibacillus sphaericus
Authors: Nascimento, Nathaly Alexandre do
Ferreira, Lígia Maria
Romão, Tatiany Patrícia
Correia, Darleide Maria da Conceição
Vasconcelos, Crhisllane Rafaele dos Santos
Rezende, Antônio Mauro
Costa, Samara Graciane
Genta, Fernando Ariel
Melo Neto, Osvaldo Pompílio
Silva Filha, Maria Helena Neves Lobo
Affilliation: Fundação Oswaldo Cruz. Centro de Pesquisas Aggeu Magalhães. Departamento de Entomologia. Recife, PE, Brasil.
Fundação Oswaldo Cruz. Centro de Pesquisas Aggeu Magalhães. Departamento de Entomologia. Recife, PE, Brasil.
Fundação Oswaldo Cruz. Centro de Pesquisas Aggeu Magalhães. Departamento de Entomologia. Recife, PE, Brasil.
Fundação Oswaldo Cruz. Centro de Pesquisas Aggeu Magalhães. Departamento de Entomologia. Recife, PE, Brasil.
Fundação Oswaldo Cruz. Centro de Pesquisas Aggeu Magalhães. Departamento de Microbiologia. Recife, PE, Brasil.
Fundação Oswaldo Cruz. Centro de Pesquisas Aggeu Magalhães. Departamento de Microbiologia. Recife, PE, Brasil.
Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Rio de Janeiro, RJ, Brasil.
Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Rio de Janeiro, RJ. Brasil / Instituto Nacional de Ciência e Tecnologia em Entomologia Molecular. Rio de Janeiro, RJ, Brasil
Abstract: Cqm1 and Aam1 are α-glucosidases (EC 3.2.1.20) expressed in Culex quinquefasciatus and Aedes aegypti larvae midgut, respectively. These orthologs share high sequence similarity but while Cqm1 acts as a receptor for the Binary (Bin) insecticidal toxin from Lysinibacillus sphaericus, Aam1 does not bind the toxin, rendering Ae. aegypti refractory to this bacterium. Aam1 is heavily glycosylated, contrasting to Cqm1, but little is known regarding how glycosylation impacts on its function. This study aimed to compare the N-glycosylation patterns and the catalytic activities of Aam1 and Cqm1. Mutant proteins were generated where predicted Aam1 N-glycosylation sites (N-PGS) were either inserted into Cqm1 or abrogated in Aam1. The mutants validated four N-PGS which were found to localize externally on the Aam1 structure. These Aam1 and Cqm1 mutants maintained their Bin binding properties, confirming that glycosylation has no role in this interaction. The α-glucosidase activity of both proteins was next investigated, with Aam1 having a remarkably higher catalytic efficiency, influenced by changes in glycosylation. Molecular dynamics showed that glycosylated and nonglycosylated Aam1 models displayed distinct patterns that could influence their catalytic activity. Differential N-glycosylation may then be associated with higher catalytic efficiency in Aam1, enhancing the functional diversity of related orthologs.
Keywords: Cqm1
Aam1
Culex quinquefasciatus
Aedes aegypti
N-glycosylation
Glucosidases
keywords: Aedes aegypti
Glucosidases
N-Glicosilação
Issue Date: 2017
Publisher: Elsevier
Citation: NASCIMENTO, Nathaly Alexandre do; et al. N-glycosylation influences the catalytic activity of mosquito a-glucosidases associated with susceptibility or refractoriness to Lysinibacillus sphaericus. Insect Biochemistry and Molecular Biology, v.81, p.62-71, 2017.
DOI: 10.1016/j.ibmb.2016.12.009
ISSN: 0965-1748
Copyright: restricted access
Appears in Collections:IOC - Artigos de Periódicos

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