Meloidogyne graminicola protein disulfide isomerase may be a nematode effector and is involved in protection against oxidative damage

Abstract The rice root-knot nematode, Meloidogyne graminicola, is a serious pest in most rice-growing countries. Usually, nematodes employ antioxidants to counteract the harm of reactive oxygen species (ROS) and facilitate their infection. Here the gene encoding M. graminicola protein disulphide iso...

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Autores principales:	Zhong-ling Tian, Ze-hua Wang, Munawar Maria, Nan Qu, Jing-wu Zheng
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2019
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/d07cbe70a5a7446280afe07bbcbab117
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spelling	oai:doaj.org-article:d07cbe70a5a7446280afe07bbcbab1172021-12-02T16:08:27ZMeloidogyne graminicola protein disulfide isomerase may be a nematode effector and is involved in protection against oxidative damage10.1038/s41598-019-48474-w2045-2322https://doaj.org/article/d07cbe70a5a7446280afe07bbcbab1172019-08-01T00:00:00Zhttps://doi.org/10.1038/s41598-019-48474-whttps://doaj.org/toc/2045-2322Abstract The rice root-knot nematode, Meloidogyne graminicola, is a serious pest in most rice-growing countries. Usually, nematodes employ antioxidants to counteract the harm of reactive oxygen species (ROS) and facilitate their infection. Here the gene encoding M. graminicola protein disulphide isomerase (MgPDI) was identified. The deduced protein is highly conserved in the putative active-site Cys-Gly-His-Cys. In situ hybridization showed that MgPDI was specifically localized within esophageal glands of pre-parasitic second stage juveniles (J2s). MgPDI was significantly up-regulated in the late parasitic J2s. Characterization of the recombinant protein showed that the purified MgPDI exhibited similar activities to other oxidases/isomerases such as the refolding of the scrambled RNase and insulin disulfide reductase and the protection of plasmid DNA and living cells from ROS damage. In addition, silencing of MgPDI by RNA interference in the pre-parasitic J2s lowered their multiplication factor. MgPDI expression was up-regulated in the presence of exogenous H2O2, whereas MgPDI silencing resulted in an increase in mortality under H2O2 stress. MgPDI is localized in the apoplast when transient expression in Nicotiana benthamiana leaves. The results indicated that MgPDI plays important roles in the reproduction and pathogenicity of M. graminicola and it also contributes to protecting nematodes from exogenous H2O2 stress.Zhong-ling TianZe-hua WangMunawar MariaNan QuJing-wu ZhengNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 9, Iss 1, Pp 1-11 (2019)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Zhong-ling Tian Ze-hua Wang Munawar Maria Nan Qu Jing-wu Zheng Meloidogyne graminicola protein disulfide isomerase may be a nematode effector and is involved in protection against oxidative damage
description	Abstract The rice root-knot nematode, Meloidogyne graminicola, is a serious pest in most rice-growing countries. Usually, nematodes employ antioxidants to counteract the harm of reactive oxygen species (ROS) and facilitate their infection. Here the gene encoding M. graminicola protein disulphide isomerase (MgPDI) was identified. The deduced protein is highly conserved in the putative active-site Cys-Gly-His-Cys. In situ hybridization showed that MgPDI was specifically localized within esophageal glands of pre-parasitic second stage juveniles (J2s). MgPDI was significantly up-regulated in the late parasitic J2s. Characterization of the recombinant protein showed that the purified MgPDI exhibited similar activities to other oxidases/isomerases such as the refolding of the scrambled RNase and insulin disulfide reductase and the protection of plasmid DNA and living cells from ROS damage. In addition, silencing of MgPDI by RNA interference in the pre-parasitic J2s lowered their multiplication factor. MgPDI expression was up-regulated in the presence of exogenous H2O2, whereas MgPDI silencing resulted in an increase in mortality under H2O2 stress. MgPDI is localized in the apoplast when transient expression in Nicotiana benthamiana leaves. The results indicated that MgPDI plays important roles in the reproduction and pathogenicity of M. graminicola and it also contributes to protecting nematodes from exogenous H2O2 stress.
format	article
author	Zhong-ling Tian Ze-hua Wang Munawar Maria Nan Qu Jing-wu Zheng
author_facet	Zhong-ling Tian Ze-hua Wang Munawar Maria Nan Qu Jing-wu Zheng
author_sort	Zhong-ling Tian
title	Meloidogyne graminicola protein disulfide isomerase may be a nematode effector and is involved in protection against oxidative damage
title_short	Meloidogyne graminicola protein disulfide isomerase may be a nematode effector and is involved in protection against oxidative damage
title_full	Meloidogyne graminicola protein disulfide isomerase may be a nematode effector and is involved in protection against oxidative damage
title_fullStr	Meloidogyne graminicola protein disulfide isomerase may be a nematode effector and is involved in protection against oxidative damage
title_full_unstemmed	Meloidogyne graminicola protein disulfide isomerase may be a nematode effector and is involved in protection against oxidative damage
title_sort	meloidogyne graminicola protein disulfide isomerase may be a nematode effector and is involved in protection against oxidative damage
publisher	Nature Portfolio
publishDate	2019
url	https://doaj.org/article/d07cbe70a5a7446280afe07bbcbab117
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Meloidogyne graminicola protein disulfide isomerase may be a nematode effector and is involved in protection against oxidative damage

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