biostudies-literatureLi JChina Agriculture Research System from the Ministry of Agriculture of the P.R. ChinaNingbo Science and Technology Innovation 2025 Major Project, ChinaK.C. Wong Magna Funding Ningbo Universitye1010412https://www.ebi.ac.uk/biostudies/studies/S-EPMC8959173biostudies-literatureUnknown18(3)Successful pathogen infection in plant depends on a proper interaction between the invading pathogen and its host. Post-translational modification (PTM) plays critical role(s) in plant-pathogen interaction. However, how PTM of viral protein regulates plant immunity remains poorly understood. Here, we found that S162 and S165 of Chinese wheat mosaic virus (CWMV) cysteine-rich protein (CRP) are phosphorylated by SAPK7 and play key roles in CWMV infection. Furthermore, the phosphorylation-mimic mutant of CRP (CRPS162/165D) but not the non-phosphorylatable mutant of CRP (CRPS162/165A) interacts with RNA-binding protein UBP1-associated protein 2C (TaUBA2C). Silencing of TaUBA2C expression in wheat plants enhanced CWMV infection. In contrast, overexpression of TaUBA2C in wheat plants inhibited CPLoS pathogensPhosphorylated viral protein evades plant immunity through interfering the function of RNA-binding protein.PMC8959173CARS-03Q21C140013Yang JLi JChen JFeng HLiu PLiu SChen XHe LfalsePhosphorylated viral protein evades plant immunity through interfering the function of RNA-binding protein.Successful pathogen infection in plant depends on a proper interaction between the invading pathogen and its host. Post-translational modification (PTM) plays critical role(s) in plant-pathogen interaction. However, how PTM of viral protein regulates plant immunity remains poorly understood. Here, we found that S162 and S165 of Chinese wheat mosaic virus (CWMV) cysteine-rich protein (CRP) are phosphorylated by SAPK7 and play key roles in CWMV infection. Furthermore, the phosphorylation-mimic mutant of CRP (CRPS162/165D) but not the non-phosphorylatable mutant of CRP (CRPS162/165A) interacts with RNA-binding protein UBP1-associated protein 2C (TaUBA2C). Silencing of TaUBA2C expression in wheat plants enhanced CWMV infection. In contrast, overexpression of TaUBA2C in wheat plants inhibited C2022-01-01T00:00:00Z2022 Mar2025-04-22T07:49:38.202Z2025-04-05T22:18:09.177ZS-EPMC89591733529449710.1371/journal.ppat.1010412