Por favor, use este identificador para citar o enlazar este ítem: https://hdl.handle.net/20.500.12008/43281
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dc.contributor.author Autor Piñeyro, María Dolores-
dc.contributor.author Autor Chiribao, María Laura-
dc.contributor.author Autor Arias, Diego G-
dc.contributor.author Autor Robello Porto, Carlos-
dc.contributor.author Autor Parodi-Tálice, Adriana Magdalena-
dc.contributor.filiacion Filiación Piñeyro María Dolores, Instituto Pasteur (Montevideo).-
dc.contributor.filiacion Filiación Chiribao María Laura, Instituto Pasteur (Montevideo).-
dc.contributor.filiacion Filiación Arias Diego G-
dc.contributor.filiacion Filiación Robello Porto Carlos, Instituto Pasteur (Montevideo).-
dc.contributor.filiacion Filiación Parodi-Tálice Adriana Magdalena, Universidad de la República (Uruguay). Facultad de Ciencias. Instituto de Biología.-
dc.date.accessioned Fecha ingreso 2024-04-01T14:07:09Z-
dc.date.available Fecha disponible 2024-04-01T14:07:09Z-
dc.date.issued Año de publicación 2023-
dc.description.abstract Resumen Peroxiredoxins (Prxs) have been shown to be important enzymes for trypanosomatids, counteracting oxidative stress and promoting cell infection and intracellular survival. In this work, we investigate the in vitro sensitivity to overoxidation and the overoxidation dynamics of Trypanosoma cruzi Prxs in parasites in culture and in the infection context. We showed that recombinant m-TXNPx, in contrast to what was observed for c-TXNPx, exists as low molecular mass forms in the overoxidized state. We observed that T. cruzi Prxs were overoxidized in epimastigotes treated with oxidants, and a significant proportion of the overoxidized forms were still present at least 24 h after treatment suggesting that these forms are not actively reversed. In in vitro infection experiments, we observed that Prxs are overoxidized in amastigotes residing in infected macrophages, demonstrating that inactivation of at least part of the Prxs by overoxidation occurs in a physiological context. We have shown that m-TXNPx has a redox-state-dependent chaperone activity. This function may be related to the increased thermotolerance observed in m-TXNPx-overexpressing parasites. This study suggests that despite the similarity between protozoan and mammalian Prxs, T. cruzi Prxs have different oligomerization dynamics and sensitivities to overoxidation, which may have implications for their function in the parasite life cycle and infection process.es
dc.format.extent Extensión 20 h.es
dc.format.mimetype Formato application/pdfes
dc.identifier.citation Citación Piñeyro, M, Chiribao, M, Arias, D [y otros autores]. "Overoxidation and oligomerization of Trypanosoma cruzi cytosolic and mitochondrial peroxiredoxins". Pathogens. [en línea] 2023, 12(10): 1273. 20 h. DOI: 10.3390/pathogens12101273.es
dc.identifier.doi DOI 10.3390/pathogens12101273-
dc.identifier.issn ISSN 2076-0817-
dc.identifier.uri URI https://hdl.handle.net/20.500.12008/43281-
dc.language.iso Idioma enes
dc.publisher Editorial MDPIes
dc.relation.ispartof EN Pathogens, 2023, 12(10): 1273.es
dc.rights Derechos Las obras depositadas en el Repositorio se rigen por la Ordenanza de los Derechos de la Propiedad Intelectual de la Universidad de la República.(Res. Nº 91 de C.D.C. de 8/III/1994 – D.O. 7/IV/1994) y por la Ordenanza del Repositorio Abierto de la Universidad de la República (Res. Nº 16 de C.D.C. de 07/10/2014)es
dc.rights.licence Licencia Licencia Creative Commons Atribución (CC - By 4.0)es
dc.subject Palabras clave Trypanosoma cruzies
dc.subject Palabras clave Peroxiredoxines
dc.subject Palabras clave Overoxidationes
dc.subject Palabras clave Chaperone activityes
dc.subject Palabras clave Oligomerizationes
dc.title Título Overoxidation and oligomerization of Trypanosoma cruzi cytosolic and mitochondrial peroxiredoxinses
dc.type Tipo de documento Artículoes

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