Thioredoxin-linked metabolism in Entamoeba histolytica

Autores
Arias, Diego Gustavo; Gutierrez, Pablo Cesar; Iglesias, Alberto Alvaro; Guerrero, Sergio Adrian
Año de publicación
2007
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Entamoeba histolytica, an intestinal protozoan that is the causative agent of amoebiasis, is exposed to elevated amounts of highly toxic reactive oxygen species during tissue invasion. In this work, we report the molecular cloning, from E. histolytica genomic DNA, of the genes ehtrxr and ehtrx41, respectively coding for thioredoxin reductase (EhTRXR) and thioredoxin (EhTRX41). The genes were expressed in Escherichia coli cells, and the corresponding recombinant proteins were purified and characterized. EhTRXR catalyzed the NADPH (Km = 4.5 μM)-dependent reduction of 5,5′-dithiobis-(2-nitrobenzoic) acid (Km = 1.7 mM), EhTRX41 (Km = 3.6 μM), and E. coli TRX (Km = 4.6 μM). EhTRXR and EhTRX41 could be assayed as a functional redox pair that, together with peroxiredoxin, mediate the NADPH-dependent reduction of hydrogen peroxide and tert-butyl hydroperoxide. It is proposed that this detoxifying system could be operative in vivo. Results add value to the genome project information and advise reconsideration of key metabolic pathways operating in E. histolytica.
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
Fil: Gutierrez, Pablo Cesar. Universidad Nacional del Litoral; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Iglesias, Alberto Alvaro. 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
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
Materia
ENTAMOEBA HISTOLYTICA
FREE RADICALS
REDOX METABOLISM
STRUCTURAL AND FUNCTIONAL CHARACTERIZATION
THIOREDOXIN SYSTEM
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/84788

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network_name_str CONICET Digital (CONICET)
spelling Thioredoxin-linked metabolism in Entamoeba histolyticaArias, Diego GustavoGutierrez, Pablo CesarIglesias, Alberto AlvaroGuerrero, Sergio AdrianENTAMOEBA HISTOLYTICAFREE RADICALSREDOX METABOLISMSTRUCTURAL AND FUNCTIONAL CHARACTERIZATIONTHIOREDOXIN SYSTEMhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Entamoeba histolytica, an intestinal protozoan that is the causative agent of amoebiasis, is exposed to elevated amounts of highly toxic reactive oxygen species during tissue invasion. In this work, we report the molecular cloning, from E. histolytica genomic DNA, of the genes ehtrxr and ehtrx41, respectively coding for thioredoxin reductase (EhTRXR) and thioredoxin (EhTRX41). The genes were expressed in Escherichia coli cells, and the corresponding recombinant proteins were purified and characterized. EhTRXR catalyzed the NADPH (Km = 4.5 μM)-dependent reduction of 5,5′-dithiobis-(2-nitrobenzoic) acid (Km = 1.7 mM), EhTRX41 (Km = 3.6 μM), and E. coli TRX (Km = 4.6 μM). EhTRXR and EhTRX41 could be assayed as a functional redox pair that, together with peroxiredoxin, mediate the NADPH-dependent reduction of hydrogen peroxide and tert-butyl hydroperoxide. It is proposed that this detoxifying system could be operative in vivo. Results add value to the genome project information and advise reconsideration of key metabolic pathways operating in E. histolytica.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; ArgentinaFil: Gutierrez, Pablo Cesar. Universidad Nacional del Litoral; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Iglesias, Alberto Alvaro. 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; ArgentinaFil: 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; ArgentinaElsevier Science Inc2007-05info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/84788Arias, Diego Gustavo; Gutierrez, Pablo Cesar; Iglesias, Alberto Alvaro; Guerrero, Sergio Adrian; Thioredoxin-linked metabolism in Entamoeba histolytica; Elsevier Science Inc; Free Radical Biology and Medicine; 42; 10; 5-2007; 1496-15050891-5849CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1016/j.freeradbiomed.2007.02.012info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/abs/pii/S0891584907001177info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-15T15:37:11Zoai:ri.conicet.gov.ar:11336/84788instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-10-15 15:37:11.905CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Thioredoxin-linked metabolism in Entamoeba histolytica
title Thioredoxin-linked metabolism in Entamoeba histolytica
spellingShingle Thioredoxin-linked metabolism in Entamoeba histolytica
Arias, Diego Gustavo
ENTAMOEBA HISTOLYTICA
FREE RADICALS
REDOX METABOLISM
STRUCTURAL AND FUNCTIONAL CHARACTERIZATION
THIOREDOXIN SYSTEM
title_short Thioredoxin-linked metabolism in Entamoeba histolytica
title_full Thioredoxin-linked metabolism in Entamoeba histolytica
title_fullStr Thioredoxin-linked metabolism in Entamoeba histolytica
title_full_unstemmed Thioredoxin-linked metabolism in Entamoeba histolytica
title_sort Thioredoxin-linked metabolism in Entamoeba histolytica
dc.creator.none.fl_str_mv Arias, Diego Gustavo
Gutierrez, Pablo Cesar
Iglesias, Alberto Alvaro
Guerrero, Sergio Adrian
author Arias, Diego Gustavo
author_facet Arias, Diego Gustavo
Gutierrez, Pablo Cesar
Iglesias, Alberto Alvaro
Guerrero, Sergio Adrian
author_role author
author2 Gutierrez, Pablo Cesar
Iglesias, Alberto Alvaro
Guerrero, Sergio Adrian
author2_role author
author
author
dc.subject.none.fl_str_mv ENTAMOEBA HISTOLYTICA
FREE RADICALS
REDOX METABOLISM
STRUCTURAL AND FUNCTIONAL CHARACTERIZATION
THIOREDOXIN SYSTEM
topic ENTAMOEBA HISTOLYTICA
FREE RADICALS
REDOX METABOLISM
STRUCTURAL AND FUNCTIONAL CHARACTERIZATION
THIOREDOXIN SYSTEM
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Entamoeba histolytica, an intestinal protozoan that is the causative agent of amoebiasis, is exposed to elevated amounts of highly toxic reactive oxygen species during tissue invasion. In this work, we report the molecular cloning, from E. histolytica genomic DNA, of the genes ehtrxr and ehtrx41, respectively coding for thioredoxin reductase (EhTRXR) and thioredoxin (EhTRX41). The genes were expressed in Escherichia coli cells, and the corresponding recombinant proteins were purified and characterized. EhTRXR catalyzed the NADPH (Km = 4.5 μM)-dependent reduction of 5,5′-dithiobis-(2-nitrobenzoic) acid (Km = 1.7 mM), EhTRX41 (Km = 3.6 μM), and E. coli TRX (Km = 4.6 μM). EhTRXR and EhTRX41 could be assayed as a functional redox pair that, together with peroxiredoxin, mediate the NADPH-dependent reduction of hydrogen peroxide and tert-butyl hydroperoxide. It is proposed that this detoxifying system could be operative in vivo. Results add value to the genome project information and advise reconsideration of key metabolic pathways operating in E. histolytica.
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
Fil: Gutierrez, Pablo Cesar. Universidad Nacional del Litoral; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Iglesias, Alberto Alvaro. 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
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
description Entamoeba histolytica, an intestinal protozoan that is the causative agent of amoebiasis, is exposed to elevated amounts of highly toxic reactive oxygen species during tissue invasion. In this work, we report the molecular cloning, from E. histolytica genomic DNA, of the genes ehtrxr and ehtrx41, respectively coding for thioredoxin reductase (EhTRXR) and thioredoxin (EhTRX41). The genes were expressed in Escherichia coli cells, and the corresponding recombinant proteins were purified and characterized. EhTRXR catalyzed the NADPH (Km = 4.5 μM)-dependent reduction of 5,5′-dithiobis-(2-nitrobenzoic) acid (Km = 1.7 mM), EhTRX41 (Km = 3.6 μM), and E. coli TRX (Km = 4.6 μM). EhTRXR and EhTRX41 could be assayed as a functional redox pair that, together with peroxiredoxin, mediate the NADPH-dependent reduction of hydrogen peroxide and tert-butyl hydroperoxide. It is proposed that this detoxifying system could be operative in vivo. Results add value to the genome project information and advise reconsideration of key metabolic pathways operating in E. histolytica.
publishDate 2007
dc.date.none.fl_str_mv 2007-05
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/84788
Arias, Diego Gustavo; Gutierrez, Pablo Cesar; Iglesias, Alberto Alvaro; Guerrero, Sergio Adrian; Thioredoxin-linked metabolism in Entamoeba histolytica; Elsevier Science Inc; Free Radical Biology and Medicine; 42; 10; 5-2007; 1496-1505
0891-5849
CONICET Digital
CONICET
url http://hdl.handle.net/11336/84788
identifier_str_mv Arias, Diego Gustavo; Gutierrez, Pablo Cesar; Iglesias, Alberto Alvaro; Guerrero, Sergio Adrian; Thioredoxin-linked metabolism in Entamoeba histolytica; Elsevier Science Inc; Free Radical Biology and Medicine; 42; 10; 5-2007; 1496-1505
0891-5849
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1016/j.freeradbiomed.2007.02.012
info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/abs/pii/S0891584907001177
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Elsevier Science Inc
publisher.none.fl_str_mv Elsevier Science Inc
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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