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

In: Nematology
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  • 1 1NemaLab/ICAAM – Instituto de Ciências Agrárias e Ambientais Mediterrânicas, Universidade de Évora, Núcleo da Mitra, Ap. 94, 7002-554 Évora, Portugal
  • | 2 2Cell and Molecular Sciences Group, The James Hutton Institute, Invergowrie, Dundee DD2 5DA, UK
  • | 3 3School of Biology, University of St Andrews, North Haugh, St Andrews KY16 9TZ, UK
  • | 4 4Departamento de Ciências da Vida, Universidade Lusófona de Humanidades e Tecnologias, EPCV, C. Grande 376, 1749-024 Lisbon, Portugal
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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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