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The plant-parasitic nematode  Heterodera schachtii  is an obligate biotroph that induces syncytial feeding sites in roots of its hosts. Nematodes produce effectors that are secreted into the host and facilitate infection process. Here we identified  H. schachtii  protein disulphide isomerase (HsPDI) as a putative effector that interferes with the host’s redox status.  In situ  hybridization showed that  HsPdi  is specifically localized within esophageal glands of pre-parasitic second stage juveniles (J2).  HsPdi  is up-regulated in the early parasitic J2s. Silencing of  HsPdi  by RNA interference in the J2s hampers their development and leads to structural malfunctions in associated feeding sites induced in Arabidopsis roots. Expression of HsPDI in Arabidopsis increases plant’s susceptibility towards  H. schachtii .  HsPdi  expression is up-regulated in the presence of exogenous H 2 O 2 , whereas  HsPdi  silencing results in increased mortality under H 2 O 2  stress. Stable expression of HsPDI in Arabidopsis plants decreases ROS burst induced by flg22. Transiently expressed HsPDI in  N. benthamiana  leaves is localized in the apoplast. HsPDI plays an important role in the interaction between nematode and plant, probably through inducing local changes in the redox status of infected host tissue. It also contributes to protect the nematode from exogenous H 2 O 2  stress.

Identification and characterization of a putative protein disulfide isomerase (HsPDI) as an alleged effector of Heterodera schachtii