Journal Article

The root‐knot nematode effector MiPDI1 targets a stress‐associated protein (SAP) to establish disease in Solanaceae and Arabidopsis

Mao, Zhenchuan, Almeida‐engler, Janice, Mejias, Joffrey, National Key Research and Development Program of China 2017YFD0200601, National Natural Science Foundation of China (NSFC) 31571987 31772138, ANR-11-LABX-0028,SIGNALIFE,Réseau d'Innovation sur les Voies de Signalisation en Sciences de la Vie, Ministere de lEnseignement Superieur, de la Recherche et de lInnovation (MENRT grant), Jian, Heng, Quentin, Michaël, INRA SPE, Chinese Academy of Agricultural Sciences (CAAS), China Scholarship Council 201606350083 201806350108, Department of Plant Pathology and Key Laboratory of Pest Monitoring and Green Management of the Ministry of Agriculture ; China Agricultural University Library, National Basic Research Program of China 2013CB127501, Liu, Qian, Favery, Bruno, INRA, Chen, Yongpan, Xie, Bingyan, Institut Sophia Agrobiotech (ISA) ; Université Nice Sophia Antipolis (1965 - 2019) (UNS)-Centre National de la Recherche Scientifique (CNRS)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE

2020

Overview

Large amounts of effectors are secreted by the oesophageal glands of plant-parasitic nematodes, but their molecular mode of action remains largely unknown. We characterized aMeloidogyne incognitaprotein disulphide isomerase (PDI)-like effector protein (MiPDI1) that facilitates nematode parasitism. In situhybridization showed thatMiPDI1was expressed specifically in the subventral glands ofM. incognita. It was significantly upregulated during parasitic stages. Immunolocalization demonstrated MiPDI1 secretionin plantaduring nematode migration and within the feeding cells. Host-induced silencing of theMiPDI1gene affected the ability of the nematode to infect the host, whereasMiPDI1expression inArabidopsisincreased susceptibility toM. incognita, providing evidence for a key role of MiPDI1 inM. incognitaparasitism. Yeast two-hybrid, bimolecular fluorescence complementation and coimmunoprecipitation assays showed that MiPDI1 interacted with a tomato stress-associated protein (SlSAP12) orthologous to the redox-regulated AtSAP12, which plays an important role in plant responses to abiotic and biotic stresses.SAP12silencing or knocking out inNicotiana benthamianaand Arabidopsis increased susceptibility toM. incognita. Our results suggest that MiPDI1 acts as a pathogenicity factor promoting disease by fine-tuning SAP-mediated responses at the interface of redox signalling, defence and stress acclimation in Solanaceae andArabidopsis.

• Publisher: Wiley,CCSD
• ISBN: 0005496029000