Biochemical characterization of thioredoxin reductase from Babesia bovis

Autores
Regner, Erika Lucía; Thompson, Carolina Soledad; Iglesias, Alberto Alvaro; Guerrero, Sergio Adrian; Arias, Diego Gustavo
Año de publicación
2014
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
This paper addresses the identification, cloning, expression, purification and functional characterization of thioredoxin reductase from Babesia bovis, the etiological agent of babesiosis. The work deals with in vitro steady state kinetic studies and other complementary analyses of the thioredoxin reductase found in the pathogenic protist. Thioredoxin reductase from B. bovis was characterized as a homodimeric flavoprotein that catalyzes the NADPH-dependent reduction of Trx with a high catalytic efficiency. Moreover, the enzyme exhibited a disulfide reductase activity using DTNB as substrate, being this activity highly sensitive to inhibition by Eosin B. The thioredoxin reductase/thioredoxin system can reduce oxidized glutathione and S-nitrosoglutathione. Our in vitro data suggest that antioxidant defense in B. bovis could be supported by this enzyme. We have performed an enzymatic characterization, searching for targets for rational design of inhibitors. This work contributes to the better understanding of the redox biochemistry occurring in the parasite.
EEA Rafaela
Fil: Regner, Erika Lucía. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Santa Fe. Instituto de Agrobiotecnologia del Litoral. Universidad Nacional del Litoral. Facultad de Bioquímica y Ciencias Biológicas. Instituto de Agrobiotecnología del Litoral; Argentina
Fil: Thompson, Carolina Soledad. Instituto Nacional de Tecnología Agropecuaria (INTA). Estación Experimental Agropecuaria Rafaela; Argentina
Fil: Iglesias, Alberto Alvaro. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Santa Fe. Instituto de Agrobiotecnologia del Litoral. Universidad Nacional del Litoral. Facultad de Bioquímica y Ciencias Biológicas. Instituto de Agrobiotecnología del Litoral; Argentina
Fil: Guerrero, Sergio Adrian. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Santa Fe. Instituto de Agrobiotecnologia del Litoral. Universidad Nacional del Litoral. Facultad de Bioquímica y Ciencias Biológicas. Instituto de Agrobiotecnología del Litoral; Argentina
Fil: Arias, Diego Gustavo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Santa Fe. Instituto de Agrobiotecnologia del Litoral. Universidad Nacional del Litoral. Facultad de Bioquímica y Ciencias Biológicas. Instituto de Agrobiotecnología del Litoral; Argentina
Fuente
Biochimie 99 : 44-53 (April 2014)
Materia
Babesia bovis
Babesiosis
Enfermedades de los Animales
Etiología
Glutation
Animal Diseases
Aetiology
Glutathione
Thioredoxin
Nivel de accesibilidad
acceso restringido
Condiciones de uso
Repositorio
INTA Digital (INTA)
Institución
Instituto Nacional de Tecnología Agropecuaria
OAI Identificador
oai:localhost:20.500.12123/3029
Acceder
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spelling Biochemical characterization of thioredoxin reductase from Babesia bovisRegner, Erika LucíaThompson, Carolina SoledadIglesias, Alberto AlvaroGuerrero, Sergio AdrianArias, Diego GustavoBabesia bovisBabesiosisEnfermedades de los AnimalesEtiologíaGlutationAnimal DiseasesAetiologyGlutathioneThioredoxinThis paper addresses the identification, cloning, expression, purification and functional characterization of thioredoxin reductase from Babesia bovis, the etiological agent of babesiosis. The work deals with in vitro steady state kinetic studies and other complementary analyses of the thioredoxin reductase found in the pathogenic protist. Thioredoxin reductase from B. bovis was characterized as a homodimeric flavoprotein that catalyzes the NADPH-dependent reduction of Trx with a high catalytic efficiency. Moreover, the enzyme exhibited a disulfide reductase activity using DTNB as substrate, being this activity highly sensitive to inhibition by Eosin B. The thioredoxin reductase/thioredoxin system can reduce oxidized glutathione and S-nitrosoglutathione. Our in vitro data suggest that antioxidant defense in B. bovis could be supported by this enzyme. We have performed an enzymatic characterization, searching for targets for rational design of inhibitors. This work contributes to the better understanding of the redox biochemistry occurring in the parasite.EEA RafaelaFil: Regner, Erika Lucía. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Santa Fe. Instituto de Agrobiotecnologia del Litoral. Universidad Nacional del Litoral. Facultad de Bioquímica y Ciencias Biológicas. Instituto de Agrobiotecnología del Litoral; ArgentinaFil: Thompson, Carolina Soledad. Instituto Nacional de Tecnología Agropecuaria (INTA). Estación Experimental Agropecuaria Rafaela; ArgentinaFil: Iglesias, Alberto Alvaro. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Santa Fe. Instituto de Agrobiotecnologia del Litoral. Universidad Nacional del Litoral. Facultad de Bioquímica y Ciencias Biológicas. Instituto de Agrobiotecnología del Litoral; ArgentinaFil: Guerrero, Sergio Adrian. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Santa Fe. Instituto de Agrobiotecnologia del Litoral. Universidad Nacional del Litoral. Facultad de Bioquímica y Ciencias Biológicas. Instituto de Agrobiotecnología del Litoral; ArgentinaFil: Arias, Diego Gustavo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Santa Fe. Instituto de Agrobiotecnologia del Litoral. Universidad Nacional del Litoral. Facultad de Bioquímica y Ciencias Biológicas. Instituto de Agrobiotecnología del Litoral; Argentina2018-08-09T13:19:28Z2018-08-09T13:19:28Z2014-04info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfhttps://www.sciencedirect.com/science/article/pii/S0300908413003982http://hdl.handle.net/20.500.12123/30290300-9084https://doi.org/10.1016/j.biochi.2013.11.002Biochimie 99 : 44-53 (April 2014)reponame:INTA Digital (INTA)instname:Instituto Nacional de Tecnología Agropecuariaenginfo:eu-repo/semantics/restrictedAccess2025-09-29T13:44:23Zoai:localhost:20.500.12123/3029instacron:INTAInstitucionalhttp://repositorio.inta.gob.ar/Organismo científico-tecnológicoNo correspondehttp://repositorio.inta.gob.ar/oai/requesttripaldi.nicolas@inta.gob.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:l2025-09-29 13:44:23.921INTA Digital (INTA) - Instituto Nacional de Tecnología Agropecuariafalse
dc.title.none.fl_str_mv Biochemical characterization of thioredoxin reductase from Babesia bovis
title Biochemical characterization of thioredoxin reductase from Babesia bovis
spellingShingle Biochemical characterization of thioredoxin reductase from Babesia bovis
Regner, Erika Lucía
Babesia bovis
Babesiosis
Enfermedades de los Animales
Etiología
Glutation
Animal Diseases
Aetiology
Glutathione
Thioredoxin
title_short Biochemical characterization of thioredoxin reductase from Babesia bovis
title_full Biochemical characterization of thioredoxin reductase from Babesia bovis
title_fullStr Biochemical characterization of thioredoxin reductase from Babesia bovis
title_full_unstemmed Biochemical characterization of thioredoxin reductase from Babesia bovis
title_sort Biochemical characterization of thioredoxin reductase from Babesia bovis
dc.creator.none.fl_str_mv Regner, Erika Lucía
Thompson, Carolina Soledad
Iglesias, Alberto Alvaro
Guerrero, Sergio Adrian
Arias, Diego Gustavo
author Regner, Erika Lucía
author_facet Regner, Erika Lucía
Thompson, Carolina Soledad
Iglesias, Alberto Alvaro
Guerrero, Sergio Adrian
Arias, Diego Gustavo
author_role author
author2 Thompson, Carolina Soledad
Iglesias, Alberto Alvaro
Guerrero, Sergio Adrian
Arias, Diego Gustavo
author2_role author
author
author
author
dc.subject.none.fl_str_mv Babesia bovis
Babesiosis
Enfermedades de los Animales
Etiología
Glutation
Animal Diseases
Aetiology
Glutathione
Thioredoxin
topic Babesia bovis
Babesiosis
Enfermedades de los Animales
Etiología
Glutation
Animal Diseases
Aetiology
Glutathione
Thioredoxin
dc.description.none.fl_txt_mv This paper addresses the identification, cloning, expression, purification and functional characterization of thioredoxin reductase from Babesia bovis, the etiological agent of babesiosis. The work deals with in vitro steady state kinetic studies and other complementary analyses of the thioredoxin reductase found in the pathogenic protist. Thioredoxin reductase from B. bovis was characterized as a homodimeric flavoprotein that catalyzes the NADPH-dependent reduction of Trx with a high catalytic efficiency. Moreover, the enzyme exhibited a disulfide reductase activity using DTNB as substrate, being this activity highly sensitive to inhibition by Eosin B. The thioredoxin reductase/thioredoxin system can reduce oxidized glutathione and S-nitrosoglutathione. Our in vitro data suggest that antioxidant defense in B. bovis could be supported by this enzyme. We have performed an enzymatic characterization, searching for targets for rational design of inhibitors. This work contributes to the better understanding of the redox biochemistry occurring in the parasite.
EEA Rafaela
Fil: Regner, Erika Lucía. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Santa Fe. Instituto de Agrobiotecnologia del Litoral. Universidad Nacional del Litoral. Facultad de Bioquímica y Ciencias Biológicas. Instituto de Agrobiotecnología del Litoral; Argentina
Fil: Thompson, Carolina Soledad. Instituto Nacional de Tecnología Agropecuaria (INTA). Estación Experimental Agropecuaria Rafaela; Argentina
Fil: Iglesias, Alberto Alvaro. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Santa Fe. Instituto de Agrobiotecnologia del Litoral. Universidad Nacional del Litoral. Facultad de Bioquímica y Ciencias Biológicas. Instituto de Agrobiotecnología del Litoral; Argentina
Fil: Guerrero, Sergio Adrian. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Santa Fe. Instituto de Agrobiotecnologia del Litoral. Universidad Nacional del Litoral. Facultad de Bioquímica y Ciencias Biológicas. Instituto de Agrobiotecnología del Litoral; Argentina
Fil: Arias, Diego Gustavo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Santa Fe. Instituto de Agrobiotecnologia del Litoral. Universidad Nacional del Litoral. Facultad de Bioquímica y Ciencias Biológicas. Instituto de Agrobiotecnología del Litoral; Argentina
description This paper addresses the identification, cloning, expression, purification and functional characterization of thioredoxin reductase from Babesia bovis, the etiological agent of babesiosis. The work deals with in vitro steady state kinetic studies and other complementary analyses of the thioredoxin reductase found in the pathogenic protist. Thioredoxin reductase from B. bovis was characterized as a homodimeric flavoprotein that catalyzes the NADPH-dependent reduction of Trx with a high catalytic efficiency. Moreover, the enzyme exhibited a disulfide reductase activity using DTNB as substrate, being this activity highly sensitive to inhibition by Eosin B. The thioredoxin reductase/thioredoxin system can reduce oxidized glutathione and S-nitrosoglutathione. Our in vitro data suggest that antioxidant defense in B. bovis could be supported by this enzyme. We have performed an enzymatic characterization, searching for targets for rational design of inhibitors. This work contributes to the better understanding of the redox biochemistry occurring in the parasite.
publishDate 2014
dc.date.none.fl_str_mv 2014-04
2018-08-09T13:19:28Z
2018-08-09T13:19:28Z
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 https://www.sciencedirect.com/science/article/pii/S0300908413003982
http://hdl.handle.net/20.500.12123/3029
0300-9084
https://doi.org/10.1016/j.biochi.2013.11.002
url https://www.sciencedirect.com/science/article/pii/S0300908413003982
http://hdl.handle.net/20.500.12123/3029
https://doi.org/10.1016/j.biochi.2013.11.002
identifier_str_mv 0300-9084
dc.language.none.fl_str_mv eng
language eng
dc.rights.none.fl_str_mv info:eu-repo/semantics/restrictedAccess
eu_rights_str_mv restrictedAccess
dc.format.none.fl_str_mv application/pdf
dc.source.none.fl_str_mv Biochimie 99 : 44-53 (April 2014)
reponame:INTA Digital (INTA)
instname:Instituto Nacional de Tecnología Agropecuaria
reponame_str INTA Digital (INTA)
collection INTA Digital (INTA)
instname_str Instituto Nacional de Tecnología Agropecuaria
repository.name.fl_str_mv INTA Digital (INTA) - Instituto Nacional de Tecnología Agropecuaria
repository.mail.fl_str_mv tripaldi.nicolas@inta.gob.ar
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score 12.559606

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