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dc.contributor.authorEspada, Margarida
dc.contributor.authorJones, John T.
dc.contributor.authorMota, Manuel
dc.identifier.citationEspada , M , Jones , J T & Mota , M 2016 , ' Characterization of glutathione S-transferases from the pine wood nematode, Bursaphelenchus xylophilus ' , Nematology , vol. 18 , no. 6 , pp. 697-709 .
dc.identifier.otherPURE: 245238379
dc.identifier.otherPURE UUID: 435a6362-0610-4b14-aa1f-8cd27c4f2fe0
dc.identifier.otherBibtex: urn:a3042e1c0f716657cad0eeccce7b1c13
dc.identifier.otherScopus: 84982860375
dc.identifier.otherWOS: 000380378100005
dc.descriptionThis work was supported by the EU 7th Framework REPHRAME project (KBBE.2010.1.4-09) and by FEDER Funds through the Operational Programme for Competitiveness Factors – COMPETE and National Funds through FCT – Foundation for Science and Technology under the Strategic Projects PEst-C/AGR/UI0115/2011 and PEst-OE/AGR/UI0115/2014. ME is funded by the FCT (Fundação para a Ciência e a Tecnologia, IP) under the PhD grant (SFRH/BD/84541/2012). The James Hutton Institute receives funding from the Scottish Government.en
dc.description.abstractWe 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.
dc.rights© 2016, Koninklijke Brill NV, Leiden. This work has been made available online in accordance with the publisher’s policies. This is the author created, accepted version manuscript following peer review and may differ slightly from the final published version. The final published version of this work is available at /
dc.subjectDetoxification metabolismen
dc.subjectPlant-parasitic nematodeen
dc.subjectTerpenoid compoundsen
dc.subjectQH301 Biologyen
dc.titleCharacterization of glutathione S-transferases from the pine wood nematode, Bursaphelenchus xylophilusen
dc.typeJournal articleen
dc.contributor.institutionUniversity of St Andrews. School of Biologyen
dc.contributor.institutionUniversity of St Andrews. Biomedical Sciences Research Complexen
dc.description.statusPeer revieweden

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