Abstract
EDS1 (Enhanced Disease Susceptibility 1) plays a crucial role in both effector‐triggered immunity activation and plant basal defence. However, whether pathogen effectors can target EDS1 or an EDS1‐related pathway to manipulate immunity is rarely reported. In this study, we identified a Phytophthora capsici Avirulence Homolog (Avh) RxLR (Arg‐any amino acid‐Leu‐Arg) effector PcAvh103 that interacts with EDS1. We demonstrated that PcAvh103 can facilitate P. capsici infection and is required for pathogen virulence. Furthermore, genetic evidence showed that PcAvh103 contributes to virulence through targeting EDS1. Finally, PcAvh103 specifically interacts with the lipase domain of EDS1 and can promote the disassociation of EDS1–PAD4 (Phytoalexin Deficient 4) complex in planta. Together, our results revealed that the P. capsici RxLR effector PcAvh103 targets host EDS1 to suppress plant immunity, probably through disrupting the EDS1–PAD4 immune signalling pathway.
Highlights
Oomycetes are a lineage of eukaryotic microorganisms phylogenetically related to diatoms and brown algae in the kingdom Stramenopila (Jiang and Tyler, 2012)
Our results reveal that the P. capsici RxLR effector PcAvh103 targets host EDS1 for virulence, probably through disrupting the association of EDS1 and Phytoalexin Deficient 4 (PAD4)
Few studies have reported that pathogen effectors target EDS1 or an EDS1-related pathway to manipulate immunity
Summary
Oomycetes are a lineage of eukaryotic microorganisms phylogenetically related to diatoms and brown algae in the kingdom Stramenopila (Jiang and Tyler, 2012). Statistical analysis showed that the lesion diameters in leaves inoculated with T105 and T76 were reduced to 46% and 69% relative to that inoculated with T48, respectively (Figure 3c) Together, these results suggest that PcAvh103 is required for P. capsici virulence. No obvious difference in disease lesions was observed after inoculation treatment, and the quantitative assay displayed a similar amount of pathogen biomass in infected leaves for WT, T48, and T105 (Figure 4b). These results indicate that PcAvh103 contributes to P. capsici virulence by targeting EDS1. These findings demonstrate that PcAvh103 competes with PAD4 to bind to EDS1, disrupting the formation of the EDS1–PAD4 complex
Sign-in/Register to view highlights & summary Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call
