Effects of a marine serine protease inhibitor on viability and morphology of Trypanosoma cruzi, the agent of Chagas disease

dc.creatorNogueira, Natália Pereira de Almeida
dc.creatorMorgado-Díaz, José Andrés
dc.creatorMenna-Barreto, Rubem Figueiredo Sadok
dc.creatorPaes, Marcia Cristina
dc.creatorLópez, Raquel Elisa da Silva
dc.date2016-09-06T17:20:38Z
dc.date2016-09-06T17:20:38Z
dc.date2013
dc.date.accessioned2023-09-26T23:32:53Z
dc.date.available2023-09-26T23:32:53Z
dc.identifierNOGUEIRA, Natália Pereira de Almeida; et al. Effects of a marine serine protease inhibitor on viability and morphology of Trypanosoma cruzi, the agent of Chagas disease. Acta Tropica, v.128, n.1, p.27-35, Oct. 2013.
dc.identifier0001-706X
dc.identifierhttps://www.arca.fiocruz.br/handle/icict/15709
dc.identifier10.1016/j.actatropica.2013.05.013
dc.identifier.urihttps://repositorioslatinoamericanos.uchile.cl/handle/2250/8891750
dc.descriptionIt has been reported that serine peptidase activities of Trypanosoma cruzi play crucial roles in parasite dissemination and host cell invasion and therefore their inhibition could affect the progress of Chagas disease. The present study investigates the interference of the Stichodactyla helianthus Kunitz-type serine protease inhibitor (ShPI-I), a 55-amino acid peptide, in T. cruzi serine peptidase activities, parasite viability, and parasite morphology. The effect of this peptide was also studied in Leishmania amazonensis promastigotes and it was proved to be a powerful inhibitor of serine proteases activities and the parasite viability. The ultrastructural alterations caused by ShPI-I included vesiculation of the flagellar pocket membrane and the appearance of a cytoplasmic vesicle that resembles an autophagic vacuole. ShPI-I, which showed itself to be an important T. cruzi serine peptidase inhibitor, reduced the parasite viability, in a dose and time dependent manner. The maximum effect of peptide on T. cruzi viability was observed when ShPI-I at 1×10(-5)M was incubated for 24 and 48h which killed completely both metacyclic trypomastigote and epimastigote forms. At 1×10(-6)M ShPI-I, in the same periods of time, reduced parasite viability about 91-95% respectively. Ultrastructural analysis demonstrated the formation of concentric membranar structures especially in the cytosol, involving organelles and small vesicles. Profiles of endoplasmic reticulum were also detected, surrounding cytosolic vesicles that resembled autophagic vacuoles. These results suggest that serine peptidases are important in T. cruzi physiology since the inhibition of their activity killed parasites in vitro as well as inducing important morphological alterations. Protease inhibitors thus appear to have a potential role as anti-trypanosomatidal agents.
dc.description2030-01-01
dc.formatapplication/pdf
dc.languageeng
dc.publisherElsevier
dc.rightsrestricted access
dc.subjectTrypanosoma cruzi
dc.subjectDoença de Chagas
dc.subjectViabilidade celular
dc.subjectMicroscopia eletrônica
dc.subjectinibidor da peptidase
dc.subjectTrypanosoma cruzi
dc.subjectShPI-I
dc.subjectPeptidase inhibition
dc.subjectCell viability
dc.subjectElectron microscopy
dc.subjectChagas Disease
dc.titleEffects of a marine serine protease inhibitor on viability and morphology of Trypanosoma cruzi, the agent of Chagas disease
dc.typeArticle


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