Open AccessPhosphorylated viral protein evades plant immunity through interfering the function of RNA-binding protein
Author(s) -
Juan Li,
Huimin Feng,
Shuang Liu,
Peng Liu,
Xuan Chen,
Jin Yang,
Long He,
Jianhua Guo,
Jianping Chen
Publication year - 2022
Publication title -
plos pathogens
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.719
H-Index - 206
eISSN - 1553-7374
pISSN - 1553-7366
DOI - 10.1371/journal.ppat.1010412
Subject(s) - biology , phosphorylation , rna , mutant , pathogen , chromatin , gene silencing , microbiology and biotechnology , rna silencing , small interfering rna , immunity , rna binding protein , rna interference , dna , immune system , gene , biochemistry , genetics
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 (CRP S162/165D ) but not the non-phosphorylatable mutant of CRP (CRP S162/165A ) 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 CWMV infection. TaUBA2C inhibits CWMV infection through recruiting the pre-mRNA of TaNPR1 , TaPR1 and TaRBOHD to induce cell death and H 2 O 2 production. This effect can be supressed by CRP S162/165D through changing TaUBA2C chromatin-bound status and attenuating it’s the RNA- or DNA-binding activities. Taken together, our findings provide new knowledge on how CRP phosphorylation affects CWMV infection as well as the arms race between virus and wheat plants.