Identification and Differential Activity of Glutathione STransferase Mu in Strains of Fasciola hepatica Susceptible and Resistant to Triclabendazole

Autores
Fernandez, Vanesa
Año de publicación
2017
Idioma
inglés
Tipo de recurso
parte de libro
Estado
versión publicada
Descripción
Fasciolahepatica is a helminth parasite that causes fascioliasis in domestic ruminants and humans. Economic losses due to its infection are estimated in US$ 2000?3000 million yearly. The anthelmintics are at present the only weapon against these parasitic helminths. The parasite resistance to different anthelmintics including that of F. hepatica to triclabendazole (TCBZ) is growing worldwide. Glutathione S‐transferases (GSTs) are enzymes involved in the detoxification of a wide range of substrates through chemical conjugation with glutathione, so that the product becomes more soluble in water, less toxic and easier to excrete. Eight GST isoenzymes are present in F. hepatica. Since the different isoenzymes do not necessarily have the same metabolic activity, in the present work, we evaluated the metabolic activity of total cytosolic GST and GST mu and GST pi isoenzymes in adult strains of F. hepatica susceptible (Cullompton) and resistant (Sligo and Oberon) to TCBZ of the highest metabolic activity of total GST. The genetic sequence database at the National Center for Biotechnical Information (NCBI) (GenBank ID: KF680281?KF680282) corresponding to the GST mu gene isolated from Cullompton strain (TCBZ‐susceptible) and (GenBank ID: KF680283?KF680284) corresponding to the GST mu gene isolated from Sligo strain (TCBZ‐resistant) in F. hepatica. Comparative analysis of both strains, Cullompton and Sligo, showed two nucleotide changes and change of one amino acid in the GST mu isoenzyme of the TCBZ‐resistant strain. These results together with the higher enzymatic activity of GST have a potential relevance as it contribute to the understanding the mechanisms that generate resistance to anthelmintics and the activity, metabolism, and disposition of these drugs in the parasite.
Fil: Fernandez, Vanesa. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tandil. Centro de Investigación Veterinaria de Tandil. Universidad Nacional del Centro de la Provincia de Buenos Aires. Centro de Investigación Veterinaria de Tandil. Provincia de Buenos Aires. Gobernación. Comision de Investigaciones Científicas. Centro de Investigación Veterinaria de Tandil; Argentina
Materia
FASCIOLA HEPATICA
GLUTATION S TRANFERASA
CONTROL
RESISTENCIA
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/103667
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/103667
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Identification and Differential Activity of Glutathione STransferase Mu in Strains of Fasciola hepatica Susceptible and Resistant to TriclabendazoleFernandez, VanesaFASCIOLA HEPATICAGLUTATION S TRANFERASACONTROLRESISTENCIAhttps://purl.org/becyt/ford/4.3https://purl.org/becyt/ford/4Fasciolahepatica is a helminth parasite that causes fascioliasis in domestic ruminants and humans. Economic losses due to its infection are estimated in US$ 2000?3000 million yearly. The anthelmintics are at present the only weapon against these parasitic helminths. The parasite resistance to different anthelmintics including that of F. hepatica to triclabendazole (TCBZ) is growing worldwide. Glutathione S‐transferases (GSTs) are enzymes involved in the detoxification of a wide range of substrates through chemical conjugation with glutathione, so that the product becomes more soluble in water, less toxic and easier to excrete. Eight GST isoenzymes are present in F. hepatica. Since the different isoenzymes do not necessarily have the same metabolic activity, in the present work, we evaluated the metabolic activity of total cytosolic GST and GST mu and GST pi isoenzymes in adult strains of F. hepatica susceptible (Cullompton) and resistant (Sligo and Oberon) to TCBZ of the highest metabolic activity of total GST. The genetic sequence database at the National Center for Biotechnical Information (NCBI) (GenBank ID: KF680281?KF680282) corresponding to the GST mu gene isolated from Cullompton strain (TCBZ‐susceptible) and (GenBank ID: KF680283?KF680284) corresponding to the GST mu gene isolated from Sligo strain (TCBZ‐resistant) in F. hepatica. Comparative analysis of both strains, Cullompton and Sligo, showed two nucleotide changes and change of one amino acid in the GST mu isoenzyme of the TCBZ‐resistant strain. These results together with the higher enzymatic activity of GST have a potential relevance as it contribute to the understanding the mechanisms that generate resistance to anthelmintics and the activity, metabolism, and disposition of these drugs in the parasite.Fil: Fernandez, Vanesa. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tandil. Centro de Investigación Veterinaria de Tandil. Universidad Nacional del Centro de la Provincia de Buenos Aires. Centro de Investigación Veterinaria de Tandil. Provincia de Buenos Aires. Gobernación. Comision de Investigaciones Científicas. Centro de Investigación Veterinaria de Tandil; ArgentinaIntechOpenAsao, ToshikiAsaduzzaman, Md2017info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/bookParthttp://purl.org/coar/resource_type/c_3248info:ar-repo/semantics/parteDeLibroapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/103667Fernandez, Vanesa; Identification and Differential Activity of Glutathione STransferase Mu in Strains of Fasciola hepatica Susceptible and Resistant to Triclabendazole; IntechOpen; 2017; 273-284978-953-51-3242-4CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.intechopen.com/books/amino-acid-new-insights-and-roles-in-plant-and-animal/identification-and-differential-activity-of-glutathione-stransferase-mu-in-strains-of-fasciola-hepatinfo:eu-repo/semantics/altIdentifier/doi/10.5772/intechopen.69189info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T10:11:15Zoai:ri.conicet.gov.ar:11336/103667instacron: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:34982025-09-03 10:11:16.39CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Identification and Differential Activity of Glutathione STransferase Mu in Strains of Fasciola hepatica Susceptible and Resistant to Triclabendazole
title Identification and Differential Activity of Glutathione STransferase Mu in Strains of Fasciola hepatica Susceptible and Resistant to Triclabendazole
spellingShingle Identification and Differential Activity of Glutathione STransferase Mu in Strains of Fasciola hepatica Susceptible and Resistant to Triclabendazole
Fernandez, Vanesa
FASCIOLA HEPATICA
GLUTATION S TRANFERASA
CONTROL
RESISTENCIA
title_short Identification and Differential Activity of Glutathione STransferase Mu in Strains of Fasciola hepatica Susceptible and Resistant to Triclabendazole
title_full Identification and Differential Activity of Glutathione STransferase Mu in Strains of Fasciola hepatica Susceptible and Resistant to Triclabendazole
title_fullStr Identification and Differential Activity of Glutathione STransferase Mu in Strains of Fasciola hepatica Susceptible and Resistant to Triclabendazole
title_full_unstemmed Identification and Differential Activity of Glutathione STransferase Mu in Strains of Fasciola hepatica Susceptible and Resistant to Triclabendazole
title_sort Identification and Differential Activity of Glutathione STransferase Mu in Strains of Fasciola hepatica Susceptible and Resistant to Triclabendazole
dc.creator.none.fl_str_mv Fernandez, Vanesa
author Fernandez, Vanesa
author_facet Fernandez, Vanesa
author_role author
dc.contributor.none.fl_str_mv Asao, Toshiki
Asaduzzaman, Md
dc.subject.none.fl_str_mv FASCIOLA HEPATICA
GLUTATION S TRANFERASA
CONTROL
RESISTENCIA
topic FASCIOLA HEPATICA
GLUTATION S TRANFERASA
CONTROL
RESISTENCIA
purl_subject.fl_str_mv https://purl.org/becyt/ford/4.3
https://purl.org/becyt/ford/4
dc.description.none.fl_txt_mv Fasciolahepatica is a helminth parasite that causes fascioliasis in domestic ruminants and humans. Economic losses due to its infection are estimated in US$ 2000?3000 million yearly. The anthelmintics are at present the only weapon against these parasitic helminths. The parasite resistance to different anthelmintics including that of F. hepatica to triclabendazole (TCBZ) is growing worldwide. Glutathione S‐transferases (GSTs) are enzymes involved in the detoxification of a wide range of substrates through chemical conjugation with glutathione, so that the product becomes more soluble in water, less toxic and easier to excrete. Eight GST isoenzymes are present in F. hepatica. Since the different isoenzymes do not necessarily have the same metabolic activity, in the present work, we evaluated the metabolic activity of total cytosolic GST and GST mu and GST pi isoenzymes in adult strains of F. hepatica susceptible (Cullompton) and resistant (Sligo and Oberon) to TCBZ of the highest metabolic activity of total GST. The genetic sequence database at the National Center for Biotechnical Information (NCBI) (GenBank ID: KF680281?KF680282) corresponding to the GST mu gene isolated from Cullompton strain (TCBZ‐susceptible) and (GenBank ID: KF680283?KF680284) corresponding to the GST mu gene isolated from Sligo strain (TCBZ‐resistant) in F. hepatica. Comparative analysis of both strains, Cullompton and Sligo, showed two nucleotide changes and change of one amino acid in the GST mu isoenzyme of the TCBZ‐resistant strain. These results together with the higher enzymatic activity of GST have a potential relevance as it contribute to the understanding the mechanisms that generate resistance to anthelmintics and the activity, metabolism, and disposition of these drugs in the parasite.
Fil: Fernandez, Vanesa. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tandil. Centro de Investigación Veterinaria de Tandil. Universidad Nacional del Centro de la Provincia de Buenos Aires. Centro de Investigación Veterinaria de Tandil. Provincia de Buenos Aires. Gobernación. Comision de Investigaciones Científicas. Centro de Investigación Veterinaria de Tandil; Argentina
description Fasciolahepatica is a helminth parasite that causes fascioliasis in domestic ruminants and humans. Economic losses due to its infection are estimated in US$ 2000?3000 million yearly. The anthelmintics are at present the only weapon against these parasitic helminths. The parasite resistance to different anthelmintics including that of F. hepatica to triclabendazole (TCBZ) is growing worldwide. Glutathione S‐transferases (GSTs) are enzymes involved in the detoxification of a wide range of substrates through chemical conjugation with glutathione, so that the product becomes more soluble in water, less toxic and easier to excrete. Eight GST isoenzymes are present in F. hepatica. Since the different isoenzymes do not necessarily have the same metabolic activity, in the present work, we evaluated the metabolic activity of total cytosolic GST and GST mu and GST pi isoenzymes in adult strains of F. hepatica susceptible (Cullompton) and resistant (Sligo and Oberon) to TCBZ of the highest metabolic activity of total GST. The genetic sequence database at the National Center for Biotechnical Information (NCBI) (GenBank ID: KF680281?KF680282) corresponding to the GST mu gene isolated from Cullompton strain (TCBZ‐susceptible) and (GenBank ID: KF680283?KF680284) corresponding to the GST mu gene isolated from Sligo strain (TCBZ‐resistant) in F. hepatica. Comparative analysis of both strains, Cullompton and Sligo, showed two nucleotide changes and change of one amino acid in the GST mu isoenzyme of the TCBZ‐resistant strain. These results together with the higher enzymatic activity of GST have a potential relevance as it contribute to the understanding the mechanisms that generate resistance to anthelmintics and the activity, metabolism, and disposition of these drugs in the parasite.
publishDate 2017
dc.date.none.fl_str_mv 2017
dc.type.none.fl_str_mv info:eu-repo/semantics/publishedVersion
info:eu-repo/semantics/bookPart
http://purl.org/coar/resource_type/c_3248
info:ar-repo/semantics/parteDeLibro
status_str publishedVersion
format bookPart
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/103667
Fernandez, Vanesa; Identification and Differential Activity of Glutathione STransferase Mu in Strains of Fasciola hepatica Susceptible and Resistant to Triclabendazole; IntechOpen; 2017; 273-284
978-953-51-3242-4
CONICET Digital
CONICET
url http://hdl.handle.net/11336/103667
identifier_str_mv Fernandez, Vanesa; Identification and Differential Activity of Glutathione STransferase Mu in Strains of Fasciola hepatica Susceptible and Resistant to Triclabendazole; IntechOpen; 2017; 273-284
978-953-51-3242-4
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://www.intechopen.com/books/amino-acid-new-insights-and-roles-in-plant-and-animal/identification-and-differential-activity-of-glutathione-stransferase-mu-in-strains-of-fasciola-hepat
info:eu-repo/semantics/altIdentifier/doi/10.5772/intechopen.69189
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv IntechOpen
publisher.none.fl_str_mv IntechOpen
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_ 1842270151543619584
score 13.13397

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