ArticleScientific reports2019
Meloidogyne graminicola protein disulfide isomerase may be a nematode effector and is involved in protection against oxidative damage.
Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 20 citations in OpenAlex.
- Transgenic hookworm secretes anti-tetrodotoxin human single chain antibody.Nature communications · 2026Article
- From germplasm to genomics: integrated breeding and omics approaches for enhancing rice root knot nematode resistance in Direct-Seeded Rice systems.Molecular biology reports · 2025Review
- Counter-attack of biocontrol agents: Environmentally benign Approaches against Root-knot nematodes (Heliyon · 2023Review
- Insights Into the Genetics of the Zhonghua 11 Resistance toFrontiers in plant science · 2022Article
- Review
- Effectors of Root-Knot Nematodes: An Arsenal for Successful Parasitism.Frontiers in plant science · 2021Review
- Identification and Characterization of a Novel Protein Disulfide Isomerase Gene (International journal of molecular sciences · 2020Article
- Genome structure and content of the rice root-knot nematode (Ecology and evolution · 2020Article
- Analyses of the Root-Knot Nematode (Pathogens (Basel, Switzerland) · 2020Article
- Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
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 H
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