Expression of active trypsin-like serine peptidases in the midgut of sugar-feeding female Anopheles aquasalis

dc.creatorLopes, Geovane Dias
dc.creatorVeloso, Andre Borges
dc.creatorVahia, Leonardo Saboia
dc.creatorDomont, Gilberto B.
dc.creatorBritto, Constança
dc.creatorCuervo, Patricia
dc.creatorJesus, José Batista de
dc.date2016-03-29T11:04:46Z
dc.date2016-03-29T11:04:46Z
dc.date2015
dc.date.accessioned2023-09-26T22:23:01Z
dc.date.available2023-09-26T22:23:01Z
dc.identifierLOPES, 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.
dc.identifier1756-3305
dc.identifierhttps://www.arca.fiocruz.br/handle/icict/13372
dc.identifier10.1186/s13071-015-0908-0
dc.identifier.urihttps://repositorioslatinoamericanos.uchile.cl/handle/2250/8878541
dc.descriptionBackground: 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.
dc.formatapplication/pdf
dc.languageeng
dc.publisherBioMed Central
dc.rightsopen access
dc.subjectAnopheles aquasalis
dc.subjectMidgut
dc.subjectZymography
dc.subjectTrypsin-like serine peptidases
dc.subjectProteomics
dc.subjectMass spectrometry
dc.subjectEspectrometria de Massas
dc.subjectProteômica
dc.subjectDípteros
dc.subjectSerine proteases
dc.subjectPeptídeo Hidrolases
dc.titleExpression of active trypsin-like serine peptidases in the midgut of sugar-feeding female Anopheles aquasalis
dc.typeArticle


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