Kinetic and structural characterization of a typical 2-cysteine peroxiredoxin from Leptospira interrogans exhibiting redox sensitivity

Autores
Arias, Diego Gustavo; Reinoso, Anahí; Sasoni, Natalia; Hartman, Matias Daniel; Iglesias, Alberto Alvaro; Guerrero, Sergio Adrian
Año de publicación
2014
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Little is known about the mechanisms by which Leptospira interrogans, the causative agent of
leptospirosis,copes with oxidative stress at the time it establishes persistent infection with in its human host. Were port the molecular cloning of a gene encoding a 2-Cys peroxiredoxin (LinAhpC) from this bacterium. After bioinformatic analysis we found that LinAhpC contains the characteristic GGIG and YF motifs present in peroxiredoxins that are sensitive to overoxidation (mainly eukaryotic proteins).These motifs are absent in insensitive prokaryotic enzymes. Recombinant LinAhpC showed activity as a thioredoxin peroxidase with sensitivity to overoxidation by H2O2 (Chyp1% 30 mM at pH 7.0and 30 °C). So far, Anabaena 2-Cysperoxiredoxin, Helicobacter pylori AhpC, and LinAhpC are the only prokaryotic enzymes studied with these characteristics.The properties determined for LinAhpC suggest that the protein could be critical for the antioxidant defense capacity in L. interrogans.
Fil: Arias, Diego Gustavo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Santa Fe. Instituto de Agrobiotecnologia del Litoral; Argentina
Fil: Reinoso, Anahí. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Santa Fe. Instituto de Agrobiotecnologia del Litoral; Argentina
Fil: Sasoni, Natalia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Santa Fe. Instituto de Agrobiotecnologia del Litoral; Argentina
Fil: Hartman, Matias Daniel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Santa Fe. Instituto de Agrobiotecnologia del Litoral; Argentina
Fil: Iglesias, Alberto Alvaro. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Santa Fe. Instituto de Agrobiotecnologia del Litoral; Argentina
Fil: Guerrero, Sergio Adrian. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Santa Fe. Instituto de Agrobiotecnologia del Litoral; Argentina
Materia
Leptospirainterrogans
Redox-Sensitive Peroxiredoxin
Thioredoxin System
Peroxide
Free Radicals
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:11336/8991
Acceder
id CONICETDig_a763ef1bf1ed0264b377885cb3026526
oai_identifier_str oai:ri.conicet.gov.ar:11336/8991
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Kinetic and structural characterization of a typical 2-cysteine peroxiredoxin from Leptospira interrogans exhibiting redox sensitivityArias, Diego GustavoReinoso, AnahíSasoni, NataliaHartman, Matias DanielIglesias, Alberto AlvaroGuerrero, Sergio AdrianLeptospirainterrogansRedox-Sensitive PeroxiredoxinThioredoxin SystemPeroxideFree Radicalshttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Little is known about the mechanisms by which Leptospira interrogans, the causative agent of<br />leptospirosis,copes with oxidative stress at the time it establishes persistent infection with in its human host. Were port the molecular cloning of a gene encoding a 2-Cys peroxiredoxin (LinAhpC) from this bacterium. After bioinformatic analysis we found that LinAhpC contains the characteristic GGIG and YF motifs present in peroxiredoxins that are sensitive to overoxidation (mainly eukaryotic proteins).These motifs are absent in insensitive prokaryotic enzymes. Recombinant LinAhpC showed activity as a thioredoxin peroxidase with sensitivity to overoxidation by H2O2 (Chyp1% 30 mM at pH 7.0and 30 °C). So far, Anabaena 2-Cysperoxiredoxin, Helicobacter pylori AhpC, and LinAhpC are the only prokaryotic enzymes studied with these characteristics.The properties determined for LinAhpC suggest that the protein could be critical for the antioxidant defense capacity in L. interrogans.Fil: Arias, Diego Gustavo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Santa Fe. Instituto de Agrobiotecnologia del Litoral; ArgentinaFil: Reinoso, Anahí. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Santa Fe. Instituto de Agrobiotecnologia del Litoral; ArgentinaFil: Sasoni, Natalia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Santa Fe. Instituto de Agrobiotecnologia del Litoral; ArgentinaFil: Hartman, Matias Daniel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Santa Fe. Instituto de Agrobiotecnologia del Litoral; ArgentinaFil: Iglesias, Alberto Alvaro. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Santa Fe. Instituto de Agrobiotecnologia del Litoral; ArgentinaFil: Guerrero, Sergio Adrian. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Santa Fe. Instituto de Agrobiotecnologia del Litoral; ArgentinaElsevier2014-09info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/8991Arias, Diego Gustavo; Reinoso, Anahí; Sasoni, Natalia; Hartman, Matias Daniel; Iglesias, Alberto Alvaro; et al.; Kinetic and structural characterization of a typical 2-cysteine peroxiredoxin from Leptospira interrogans exhibiting redox sensitivity; Elsevier; Free Radical Biology And Medicine; 77; 9-2014; 30-400891-5849enginfo:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0891584914004055info:eu-repo/semantics/altIdentifier/doi/10.1016/j.freeradbiomed.2014.08.014info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-15T14:56:05Zoai:ri.conicet.gov.ar:11336/8991instacron: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 14:56:05.861CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Kinetic and structural characterization of a typical 2-cysteine peroxiredoxin from Leptospira interrogans exhibiting redox sensitivity
title Kinetic and structural characterization of a typical 2-cysteine peroxiredoxin from Leptospira interrogans exhibiting redox sensitivity
spellingShingle Kinetic and structural characterization of a typical 2-cysteine peroxiredoxin from Leptospira interrogans exhibiting redox sensitivity
Arias, Diego Gustavo
Leptospirainterrogans
Redox-Sensitive Peroxiredoxin
Thioredoxin System
Peroxide
Free Radicals
title_short Kinetic and structural characterization of a typical 2-cysteine peroxiredoxin from Leptospira interrogans exhibiting redox sensitivity
title_full Kinetic and structural characterization of a typical 2-cysteine peroxiredoxin from Leptospira interrogans exhibiting redox sensitivity
title_fullStr Kinetic and structural characterization of a typical 2-cysteine peroxiredoxin from Leptospira interrogans exhibiting redox sensitivity
title_full_unstemmed Kinetic and structural characterization of a typical 2-cysteine peroxiredoxin from Leptospira interrogans exhibiting redox sensitivity
title_sort Kinetic and structural characterization of a typical 2-cysteine peroxiredoxin from Leptospira interrogans exhibiting redox sensitivity
dc.creator.none.fl_str_mv Arias, Diego Gustavo
Reinoso, Anahí
Sasoni, Natalia
Hartman, Matias Daniel
Iglesias, Alberto Alvaro
Guerrero, Sergio Adrian
author Arias, Diego Gustavo
author_facet Arias, Diego Gustavo
Reinoso, Anahí
Sasoni, Natalia
Hartman, Matias Daniel
Iglesias, Alberto Alvaro
Guerrero, Sergio Adrian
author_role author
author2 Reinoso, Anahí
Sasoni, Natalia
Hartman, Matias Daniel
Iglesias, Alberto Alvaro
Guerrero, Sergio Adrian
author2_role author
author
author
author
author
dc.subject.none.fl_str_mv Leptospirainterrogans
Redox-Sensitive Peroxiredoxin
Thioredoxin System
Peroxide
Free Radicals
topic Leptospirainterrogans
Redox-Sensitive Peroxiredoxin
Thioredoxin System
Peroxide
Free Radicals
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Little is known about the mechanisms by which Leptospira interrogans, the causative agent of<br />leptospirosis,copes with oxidative stress at the time it establishes persistent infection with in its human host. Were port the molecular cloning of a gene encoding a 2-Cys peroxiredoxin (LinAhpC) from this bacterium. After bioinformatic analysis we found that LinAhpC contains the characteristic GGIG and YF motifs present in peroxiredoxins that are sensitive to overoxidation (mainly eukaryotic proteins).These motifs are absent in insensitive prokaryotic enzymes. Recombinant LinAhpC showed activity as a thioredoxin peroxidase with sensitivity to overoxidation by H2O2 (Chyp1% 30 mM at pH 7.0and 30 °C). So far, Anabaena 2-Cysperoxiredoxin, Helicobacter pylori AhpC, and LinAhpC are the only prokaryotic enzymes studied with these characteristics.The properties determined for LinAhpC suggest that the protein could be critical for the antioxidant defense capacity in L. interrogans.
Fil: Arias, Diego Gustavo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Santa Fe. Instituto de Agrobiotecnologia del Litoral; Argentina
Fil: Reinoso, Anahí. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Santa Fe. Instituto de Agrobiotecnologia del Litoral; Argentina
Fil: Sasoni, Natalia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Santa Fe. Instituto de Agrobiotecnologia del Litoral; Argentina
Fil: Hartman, Matias Daniel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Santa Fe. Instituto de Agrobiotecnologia del Litoral; Argentina
Fil: Iglesias, Alberto Alvaro. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Santa Fe. Instituto de Agrobiotecnologia del Litoral; Argentina
Fil: Guerrero, Sergio Adrian. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Santa Fe. Instituto de Agrobiotecnologia del Litoral; Argentina
description Little is known about the mechanisms by which Leptospira interrogans, the causative agent of<br />leptospirosis,copes with oxidative stress at the time it establishes persistent infection with in its human host. Were port the molecular cloning of a gene encoding a 2-Cys peroxiredoxin (LinAhpC) from this bacterium. After bioinformatic analysis we found that LinAhpC contains the characteristic GGIG and YF motifs present in peroxiredoxins that are sensitive to overoxidation (mainly eukaryotic proteins).These motifs are absent in insensitive prokaryotic enzymes. Recombinant LinAhpC showed activity as a thioredoxin peroxidase with sensitivity to overoxidation by H2O2 (Chyp1% 30 mM at pH 7.0and 30 °C). So far, Anabaena 2-Cysperoxiredoxin, Helicobacter pylori AhpC, and LinAhpC are the only prokaryotic enzymes studied with these characteristics.The properties determined for LinAhpC suggest that the protein could be critical for the antioxidant defense capacity in L. interrogans.
publishDate 2014
dc.date.none.fl_str_mv 2014-09
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/11336/8991
Arias, Diego Gustavo; Reinoso, Anahí; Sasoni, Natalia; Hartman, Matias Daniel; Iglesias, Alberto Alvaro; et al.; Kinetic and structural characterization of a typical 2-cysteine peroxiredoxin from Leptospira interrogans exhibiting redox sensitivity; Elsevier; Free Radical Biology And Medicine; 77; 9-2014; 30-40
0891-5849
url http://hdl.handle.net/11336/8991
identifier_str_mv Arias, Diego Gustavo; Reinoso, Anahí; Sasoni, Natalia; Hartman, Matias Daniel; Iglesias, Alberto Alvaro; et al.; Kinetic and structural characterization of a typical 2-cysteine peroxiredoxin from Leptospira interrogans exhibiting redox sensitivity; Elsevier; Free Radical Biology And Medicine; 77; 9-2014; 30-40
0891-5849
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0891584914004055
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.freeradbiomed.2014.08.014
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
application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Elsevier
publisher.none.fl_str_mv Elsevier
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
_version_ 1846083096743510016
score 13.22299

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