Characterization of glutathione S transferases from the plant-parasitic nematode, Bursaphelenchus xylophilus

Detalhes bibliográficos
Autor(a) principal: Espada, Margarida
Data de Publicação: 2016
Outros Autores: Jones, J.T., Mota, Manuel
Tipo de documento: Artigo
Idioma: por
Título da fonte: Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
Texto Completo: http://hdl.handle.net/10174/20438
https://doi.org/10.1163/15685411-00002985
Resumo: We have previously identified two secreted glutathione S-transferases (GST) expressed in the pharyngeal gland cell of Bursaphelenchus xylophilus, which are upregulated post infection of the host. This study examines the functional role of GSTs in B. xylophilus biology. We analysed the expression profiles of all predicted GSTs in the genome and the results showed that they belong to kappa and cytosolic subfamilies and the majority are upregulated post infection of the host. A small percentage is potentially secreted and none is downregulated post infection of the host. One secreted protein was confirmed as a functional GST and is within a cluster that showed the highest expression fold change in infection. This enzyme has a protective activity that may involve host defences, namely in the presence of terpenoid compounds and peroxide products. These results suggest that GSTs secreted into the host participate in the detoxification of host-derived defence compounds and enable successful parasitism.
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spelling Characterization of glutathione S transferases from the plant-parasitic nematode, Bursaphelenchus xylophilusdetoxification metabolism,plant-parasitic nematodeWe have previously identified two secreted glutathione S-transferases (GST) expressed in the pharyngeal gland cell of Bursaphelenchus xylophilus, which are upregulated post infection of the host. This study examines the functional role of GSTs in B. xylophilus biology. We analysed the expression profiles of all predicted GSTs in the genome and the results showed that they belong to kappa and cytosolic subfamilies and the majority are upregulated post infection of the host. A small percentage is potentially secreted and none is downregulated post infection of the host. One secreted protein was confirmed as a functional GST and is within a cluster that showed the highest expression fold change in infection. This enzyme has a protective activity that may involve host defences, namely in the presence of terpenoid compounds and peroxide products. These results suggest that GSTs secreted into the host participate in the detoxification of host-derived defence compounds and enable successful parasitism.Nematology2017-01-31T10:38:12Z2017-01-312016-01-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articlehttp://hdl.handle.net/10174/20438http://hdl.handle.net/10174/20438https://doi.org/10.1163/15685411-00002985por697-709mespada@uevora.ptndmmota@uevora.pt211Espada, MargaridaJones, J.T.Mota, Manuelinfo:eu-repo/semantics/openAccessreponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãoinstacron:RCAAP2024-01-03T19:10:23Zoai:dspace.uevora.pt:10174/20438Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-20T01:11:56.138885Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãofalse
dc.title.none.fl_str_mv Characterization of glutathione S transferases from the plant-parasitic nematode, Bursaphelenchus xylophilus
title Characterization of glutathione S transferases from the plant-parasitic nematode, Bursaphelenchus xylophilus
spellingShingle Characterization of glutathione S transferases from the plant-parasitic nematode, Bursaphelenchus xylophilus
Espada, Margarida
detoxification metabolism,
plant-parasitic nematode
title_short Characterization of glutathione S transferases from the plant-parasitic nematode, Bursaphelenchus xylophilus
title_full Characterization of glutathione S transferases from the plant-parasitic nematode, Bursaphelenchus xylophilus
title_fullStr Characterization of glutathione S transferases from the plant-parasitic nematode, Bursaphelenchus xylophilus
title_full_unstemmed Characterization of glutathione S transferases from the plant-parasitic nematode, Bursaphelenchus xylophilus
title_sort Characterization of glutathione S transferases from the plant-parasitic nematode, Bursaphelenchus xylophilus
author Espada, Margarida
author_facet Espada, Margarida
Jones, J.T.
Mota, Manuel
author_role author
author2 Jones, J.T.
Mota, Manuel
author2_role author
author
dc.contributor.author.fl_str_mv Espada, Margarida
Jones, J.T.
Mota, Manuel
dc.subject.por.fl_str_mv detoxification metabolism,
plant-parasitic nematode
topic detoxification metabolism,
plant-parasitic nematode
description We have previously identified two secreted glutathione S-transferases (GST) expressed in the pharyngeal gland cell of Bursaphelenchus xylophilus, which are upregulated post infection of the host. This study examines the functional role of GSTs in B. xylophilus biology. We analysed the expression profiles of all predicted GSTs in the genome and the results showed that they belong to kappa and cytosolic subfamilies and the majority are upregulated post infection of the host. A small percentage is potentially secreted and none is downregulated post infection of the host. One secreted protein was confirmed as a functional GST and is within a cluster that showed the highest expression fold change in infection. This enzyme has a protective activity that may involve host defences, namely in the presence of terpenoid compounds and peroxide products. These results suggest that GSTs secreted into the host participate in the detoxification of host-derived defence compounds and enable successful parasitism.
publishDate 2016
dc.date.none.fl_str_mv 2016-01-01T00:00:00Z
2017-01-31T10:38:12Z
2017-01-31
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://hdl.handle.net/10174/20438
http://hdl.handle.net/10174/20438
https://doi.org/10.1163/15685411-00002985
url http://hdl.handle.net/10174/20438
https://doi.org/10.1163/15685411-00002985
dc.language.iso.fl_str_mv por
language por
dc.relation.none.fl_str_mv 697-709
mespada@uevora.pt
nd
mmota@uevora.pt
211
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.publisher.none.fl_str_mv Nematology
publisher.none.fl_str_mv Nematology
dc.source.none.fl_str_mv reponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
instacron:RCAAP
instname_str Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
instacron_str RCAAP
institution RCAAP
reponame_str Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
collection Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
repository.name.fl_str_mv Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
repository.mail.fl_str_mv
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