Artículo
On the functionality of a methionine sulfoxide reductase B from Trypanosoma cruzi
Arias, Diego Gustavo
; Cabeza, Matías Sebastián
; Echarren, María Laura
; Faral-Tello, Paula; Iglesias, Alberto A.; Robello, Carlos; Guerrero, Sergio Adrian
Fecha de publicación:
07/2020
Editorial:
Elsevier Science Inc
Revista:
Free Radical Biology and Medicine
ISSN:
0891-5849
Idioma:
Inglés
Tipo de recurso:
Artículo publicado
Clasificación temática:
Resumen
BackgroundMethionine is an amino acid susceptible to be oxidized to give a racemic mixture of R and S forms of methionine sulfoxide (MetSO). This posttranslational modification has been reported to occur in vivo under either normal or stress conditions. The reduction of MetSO to methionine is catalyzed by methionine sulfoxide reductases (MSRs), thiol-dependent enzymes present in almost all organisms. These enzymes can reduce specifically one or another of the isomers of MetSO (free and protein-bound). This redox modification could change the structure and function of many proteins, either concerned in redox or other metabolic pathways. The study of antioxidant systems in Trypanosoma cruzi has been mainly focused on the involvement of trypanothione, a specific redox component for these organisms. Though, little information is available concerning mechanisms for repairing oxidized methionine residues in proteins, which would be relevant for the survival of these pathogens in the different stages of their life cycle.MethodsWe report an in vitro functional and in vivo cellular characterization of methionine sulfoxide reductase B (MSRB, specific for protein-bound MetSO R-enantiomer) from T. cruzi strain Dm28c.ResultsMSRB exhibited both cytosolic and mitochondrial localization in epimastigote cells. From assays involving parasites overexpressing MSRB, we observed the contribution of this protein to increase the general resistance against oxidative damage, the infectivity of trypomastigote cells, and intracellular replication of the amastigote stage. Also, we report that epimastigotes overexpressing MSRB exhibit inhibition of the metacyclogenesis process; this suggesting the involvement of the proteins as negative modulators in this cellular differentiation.Conclusions and General SignificanceThis report contributes to novel insights concerning redox metabolism in T. cruzi. Results herein presented support the importance of enzymatic steps involved in the metabolism of L-Met and in repairing oxidized macromolecules in this parasite.
Palabras clave:
TRYPANOSOMA CRUZI
,
REDOX
,
METHIONINE SULFOXIDE
,
STRESS
Archivos asociados
Licencia
Identificadores
Colecciones
Articulos(CCT - SANTA FE)
Articulos de CTRO.CIENTIFICO TECNOL.CONICET - SANTA FE
Articulos de CTRO.CIENTIFICO TECNOL.CONICET - SANTA FE
Citación
Arias, Diego Gustavo; Cabeza, Matías Sebastián; Echarren, María Laura; Faral-Tello, Paula; Iglesias, Alberto A.; et al.; On the functionality of a methionine sulfoxide reductase B from Trypanosoma cruzi; Elsevier Science Inc; Free Radical Biology and Medicine; 158; 7-2020; 96-114
Compartir
Altmétricas