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Characterization of glutathione S-transferases from the pine wood nematode, Bursaphelenchus xylophilus

Research output: Contribution to journalArticle

Author(s)

Margarida Espada, John T. Jones, Manuel Mota

School/Research organisations

Abstract

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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Details

Original languageEnglish
Pages (from-to)697-709
Number of pages13
JournalNematology
Volume18
Issue number6
Early online date10 May 2016
DOIs
Publication statusPublished - 2016

    Research areas

  • Detoxification metabolism, Effectors, Plant-parasitic nematode, Terpenoid compounds

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