Plasmopara viticola Effector PvRXLR10 Targets a Host Phospholipase VvipPLA-IIδ2 to Suppress Plant Immunity in Grapevine.

Abstract

Plasmopara viticola that causes grapevine downy mildew disease in viticulture regions is among the 10 most relevant pathogens worldwide. It secretes a large arsenal of effectors to facilitate colonisation by perturbing host immunity. However, the underlying mechanisms by which P. viticola effectors disturb grapevine defence are still largely unknown. In this study, we report that PvRXLR10, an RXLR effector with a WY domain, promotes P. viticola infection in grapevine and Phytophthora parasitica colonisation in Nicotiana benthamiana. PvRXLR10 interacts with a host patatin-like protein VvipPLA-IIδ2 with phospholipase A2 activity. The WY domain of PvRXLR10 is not responsible for cell death suppression in N. benthamiana but is necessary for PvRXLR10 interaction with VvipPLA-IIδ2. Overexpression and RNAi-mediated suppression of VvipPLA-IIδ2 expression in Vitis vinifera consistently showed that this protein positively regulates plant immunity in response to P. viticola infection. Interestingly, we found that VvipPLA-IIδ2 partially associates with PvRXLR10 at the endoplasmic reticulum (ER). Reverse transcription-quantitative PCR (RT-qPCR) analysis showed that the expression of VvipPLA-IIδ2 was suppressed by PvRXLR10 during P. viticola infection. The overexpression of VvipPLA-IIδ2 in V. vinifera induced higher expression of genes related to jasmonic acid (JA) biosynthesis, signalling pathways and defence response. The evidence indicates the important roles of VvipPLA-IIδ2 in grapevine immunity and P. viticola effector PvRXLR10 targets this protein to promote its infection.