The stripe rust effector Pst3180.3 inhibits the transcriptional activity of TaMYB4L to modulate wheat immunity and analyzes the key active sites of the interaction conformation.

Puccinia striiformis f. sp. tritici (Pst) has a wide range and serious damage, which severely threatens global wheat production. In this study, we focused on an effector protein Pst3180.3, which was induced to be highly expressed during the Pst infection stage. The N-terminal 19 amino acid of Pst3180.3 was verified to function as a signal peptide and transferred to cytoplasm and nucleus of wheat following Pst infection. Transient overexpression of Pst3180.3 in Nicotiana benthamiana inhibited programmed cell death triggered via BAX. The instantaneous silencing of Pst3180.3 by BSMV- HIGS significantly reduced the number of uredinia and increased accumulation of reactive oxygen species. Those results indicated that Pst3180.3 is an important pathogenic factor of Pst. Interaction of Pst3180.3 with a transcription factor TaMYB4L in host was confirmed through yeast two-hybrid, luciferase complementation, and co-immunoprecipitation. Virus-induced gene silencing of TaMYB4L weakened the resistance to Pst, indicated that TaMYB4L may be involved in the positive regulation of plant immunity. Dual-luciferase assays revealed that Pst3180.3 inhibited the transcriptional activity of TaMYB4L. Meanwhile, molecular docking analysis identified the key residue sites for the interaction and binding between Pst3180.3 and MYB4L. Those results demonstrated that Pst3180.3 binds to TaMYB4L and interacts to inhibit wheat resistance to Pst infection.