{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Li J"],"funding":["China Agriculture Research System from the Ministry of Agriculture of the P.R. China","Ningbo Science and Technology Innovation 2025 Major Project, China","K.C. Wong Magna Funding Ningbo University"],"pagination":["e1010412"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC8959173"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["18(3)"],"pubmed_abstract":["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 C"],"journal":["PLoS pathogens"],"pubmed_title":["Phosphorylated viral protein evades plant immunity through interfering the function of RNA-binding protein."],"pmcid":["PMC8959173"],"funding_grant_id":["CARS-03","Q21C140013"],"pubmed_authors":["Yang J","Li J","Chen J","Feng H","Liu P","Liu S","Chen X","He L"],"additional_accession":[]},"is_claimable":false,"name":"Phosphorylated viral protein evades plant immunity through interfering the function of RNA-binding protein.","description":"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 C","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Mar","modification":"2025-04-22T07:49:38.202Z","creation":"2025-04-05T22:18:09.177Z"},"accession":"S-EPMC8959173","cross_references":{"pubmed":["35294497"],"doi":["10.1371/journal.ppat.1010412"]}}