Please use this identifier to cite or link to this item: https://www.arca.fiocruz.br/handle/icict/13372
Title: Expression of active trypsin-like serine peptidases in the midgut of sugar-feeding female Anopheles aquasalis
Authors: Lopes, Geovane Dias
Veloso, Andre Borges
Vahia, Leonardo Saboia
Domont, Gilberto B.
Britto, Constança
Cuervo, Patricia
Jesus, José Batista de
Affilliation: Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório de Biologia Molecular e Doenças Endêmicas. Rio de Janeiro, RJ, Brasil.
Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório de Biologia Molecular e Doenças Endêmicas. Rio de Janeiro, RJ, Brasil.
Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório de Pesquisa em Leishmaniose. Rio de Janeiro, RJ, Brasil.
Universidade Federal do Rio de Janeiro. Departamento de Química. Laboratório de Química de Proteínas. Rio de Janeiro, RJ, Brasil.
Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório de Biologia Molecular e Doenças Endêmicas. Rio de Janeiro, RJ, Brasil.
Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório de Pesquisa em Leishmaniose. Rio de Janeiro, RJ, Brasil.
Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório de Biologia Molecular e Doenças Endêmicas. Rio de Janeiro, RJ, Brasil / Universidade Federal de São João Del Rey. Faculdade de Medicina. Departamento de Medicina. São João del Rey, MG, Brasil.
Abstract: Background: Anopheles aquasalis is a dipteran of the family Culicidae that is widely distributed in the coastal regions of South and Central America. This species acts as a vector of Plasmodium vivax, an important etiological agent of malaria, which represents a serious public health problem. In mosquitoes, trypsin-like serine proteases are important in blood meal digestion, immune responses and reproductive functions. The study of peptidases expressed in the mosquito midgut is essential to understanding the mechanisms of parasite-host interaction and the physiological process of nutrient digestion. Methods: Our study aimed to identify and characterize the proteolytic activities in the midgut of sugar-fed An. aquasalis females using zymographic analyses (substrate-SDS-PAGE), in-solution assays and mass spectrometry. Results: Here, we used a zymographic analysis to further biochemically characterize the proteolytic profile of the midgut of sugar-feeding An. aquasalis females. The trypsin peptidases migrated between ~17 and ~76 kDa and displayed higher proteolytic activities between pH 7.5 and 10 and at temperatures between 37 °C and 50 °C. Four putative trypsin-like serine peptidases were identified using mass spectrometry and data mining. The molecular masses of these peptidases were similar to those observed using zymography, which suggested that these peptidases could be responsible for some of the observed proteolytic bands. Conclusions: Taken together, our results contribute to the gene annotation of the unknown genome of this species, to the tissue location of these peptidases, and to the functional prediction of these crucial enzymes, which all impact further studies of this species.
Keywords: Anopheles aquasalis
Midgut
Zymography
Trypsin-like serine peptidases
Proteomics
Mass spectrometry
DeCS: Espectrometria de Massas
Proteômica
Dípteros
Serine proteases
Peptídeo Hidrolases
Issue Date: 2015
Publisher: BioMed Central
Citation: LOPES, Geovane Dias; et al. Expression of active trypsin-like serine peptidases in the midgut of sugar-feeding female Anopheles aquasalis. Parasites & Vectors, v.8:296, 10p, 2015.
DOI: 10.1186/s13071-015-0908-0
ISSN: 1756-3305
Copyright: open access
Appears in Collections:IOC - Artigos de Periódicos

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