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dc.contributor.author
Arias, Diego Gustavo  
dc.contributor.author
Cabeza, Matías Sebastián  
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Echarren, María Laura  
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Faral-Tello, Paula  
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Iglesias, Alberto A.  
dc.contributor.author
Robello, Carlos  
dc.contributor.author
Guerrero, Sergio Adrian  
dc.date.available
2020-08-09T13:50:35Z  
dc.date.issued
2020-07  
dc.identifier.citation
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  
dc.identifier.issn
0891-5849  
dc.identifier.uri
http://hdl.handle.net/11336/111230  
dc.description.abstract
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.  
dc.format
application/pdf  
dc.language.iso
eng  
dc.publisher
Elsevier Science Inc  
dc.rights
info:eu-repo/semantics/restrictedAccess  
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/  
dc.subject
TRYPANOSOMA CRUZI  
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REDOX  
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METHIONINE SULFOXIDE  
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STRESS  
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Bioquímica y Biología Molecular  
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Ciencias Biológicas  
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CIENCIAS NATURALES Y EXACTAS  
dc.title
On the functionality of a methionine sulfoxide reductase B from Trypanosoma cruzi  
dc.type
info:eu-repo/semantics/article  
dc.type
info:ar-repo/semantics/artículo  
dc.type
info:eu-repo/semantics/publishedVersion  
dc.date.updated
2020-08-05T16:38:13Z  
dc.journal.volume
158  
dc.journal.pagination
96-114  
dc.journal.pais
Estados Unidos  
dc.description.fil
Fil: Arias, Diego Gustavo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe. Instituto de Agrobiotecnología del Litoral. Universidad Nacional del Litoral. Instituto de Agrobiotecnología del Litoral; Argentina  
dc.description.fil
Fil: Cabeza, Matías Sebastián. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe. Instituto de Agrobiotecnología del Litoral. Universidad Nacional del Litoral. Instituto de Agrobiotecnología del Litoral; Argentina  
dc.description.fil
Fil: Echarren, María Laura. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe. Instituto de Agrobiotecnología del Litoral. Universidad Nacional del Litoral. Instituto de Agrobiotecnología del Litoral; Argentina  
dc.description.fil
Fil: Faral-Tello, Paula. Instituto Pasteur de Montevideo; Uruguay  
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Fil: Iglesias, Alberto A.. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe. Instituto de Agrobiotecnología del Litoral. Universidad Nacional del Litoral. Instituto de Agrobiotecnología del Litoral; Argentina  
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Fil: Robello, Carlos. Instituto Pasteur de Montevideo; Uruguay  
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Fil: Guerrero, Sergio Adrian. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe. Instituto de Agrobiotecnología del Litoral. Universidad Nacional del Litoral. Instituto de Agrobiotecnología del Litoral; Argentina  
dc.journal.title
Free Radical Biology and Medicine  
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://linkinghub.elsevier.com/retrieve/pii/S0891584920311321  
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1016/j.freeradbiomed.2020.06.035