Hypovirus-Induced Phosphorylation of CpIre1 Modulates Unfolded Protein Response and Virulence in Cryphonectria parasitica.

ABSTRACT: The chestnut blight fungus Cryphonectria parasitica and its hypovirus constitute a valuable model for investigating fungal pathogenesis and cross-kingdom virus-host interplay. To investigate how hypovirus regulates protein function at the phosphorylation level in C. parasitica, we performed a comparative phosphoproteomic analysis in the fungus with or without Cryphonectria hypovirus 1 (CHV1) infection. Comparative profiling between the wild-type (EP155) and hypovirus-infected (EP155/CHV1-EP713) strains revealed 700 differentially phosphorylated sites (174 upregulated, 526 downregulated). Among these, the serine 896 and 897 sites on the endoplasmic reticulum (ER) stress-sensing protein CpIre1 drew our particular attention, as hypovirus-induced phosphorylation targets. Western blot analysis

SUBMITTER: Zhao L 

PROVIDER: S-EPMC12907514 | biostudies-literature | 2026 Feb

REPOSITORIES: biostudies-literature