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

Margarida Espada; John T. Jones; Manuel Mota

doi:10.1163/15685411-00002985

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

Margarida Espada, John T. Jones, Manuel Mota

Research output: Contribution to journal › Article › peer-review

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.

Original language	English
Pages (from-to)	697-709
Number of pages	13
Journal	Nematology
Volume	18
Issue number	6
Early online date	10 May 2016
DOIs	https://doi.org/10.1163/15685411-00002985
Publication status	Published - 2016

Keywords

Detoxification metabolism
Effectors
Plant-parasitic nematode
Terpenoid compounds

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10.1163/15685411-00002985

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© 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 booksandjournals.brillonline.com / https://doi.org/10.1163/15685411-00002985
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title = "Characterization of glutathione S-transferases from the pine wood nematode, Bursaphelenchus xylophilus",

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.",

keywords = "Detoxification metabolism, Effectors, Plant-parasitic nematode, Terpenoid compounds",

author = "Margarida Espada and Jones, \{John T.\} and Manuel Mota",

note = "This 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 (Funda{\c c}{\~a}o para a Ci{\^e}ncia e a Tecnologia, IP) under the PhD grant (SFRH/BD/84541/2012). The James Hutton Institute receives funding from the Scottish Government.",

year = "2016",

doi = "10.1163/15685411-00002985",

language = "English",

volume = "18",

pages = "697--709",

journal = "Nematology",

issn = "1388-5545",

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number = "6",

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AU - Espada, Margarida

AU - Jones, John T.

AU - Mota, Manuel

N1 - This 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.

PY - 2016

Y1 - 2016

N2 - 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.

AB - 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.

KW - Detoxification metabolism

KW - Effectors

KW - Plant-parasitic nematode

KW - Terpenoid compounds

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DO - 10.1163/15685411-00002985

M3 - Article

SN - 1388-5545

VL - 18

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EP - 709

JO - Nematology

JF - Nematology

IS - 6

ER -

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

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Keywords

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