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 CWMV infection. TaUBA2C inhibits CWMV infection through recruiting the pre-mRNA of TaNPR1, TaPR1 and TaRBOHD to induce cell death and H2O2 production. This effect can be supressed by CRPS162/165D 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.
Highlights
Post-translational modification (PTM) can greatly modify protein functions, including the functions involved in the responses against abiotic and/or biotic stresses [1,2]
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
We found that S162 and S165 of CWMV cysteine-rich protein (CRP) are phosphorylated by SAPK7 in vivo and in vitro
Summary
Post-translational modification (PTM) can greatly modify protein functions, including the functions involved in the responses against abiotic and/or biotic stresses [1,2]. These include protein phosphorylation [3–5], sumoylation [6], ubiquitination [7], glycosylation [8], N-Myristoylation [5], and S-acylation [9]. Among these PTMs, protein phosphorylation is considered as one of the most studied PTMs and plays vital roles in many cellular processes [10]. Numerous studies have indicated that after phosphorylation, many viral proteins can enhance or suppress virus infection in plants. The phosphorylated Barley stripe mosaic virus (BSMV) γb protein has been shown to suppress RNA silencing and virus infection-induced cell death in plants [4]. The Casein Kinase 1 (CK1)-mediated phosphorylation of the serine-rich motif in Barley yellow striate mosaic virus (BYSMV) phosphoprotein is essential for viral replication [12]. How protein phosphorylation modulates virus pathogenicity in plants is still largely unknown
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