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

Lijiu Zhao1,2, Feng Wang1, Fengyue Chen1

  • 1State Key Laboratory for Conservation and Utilization of Subtropical Agro-Bioresources, College of Life Science and Technology, Guangxi University, Nanning, China.

Molecular Plant Pathology
|February 16, 2026
PubMed

Insights

Cryphonectria parasitica hypovirus 1 (CHV1) infection alters fungal protein phosphorylation, particularly CpIre1. This phosphorylation is crucial for fungal traits, stress response, and efficient virus replication, revealing a host reprogramming mechanism.

Area of Science:

  • Mycology
  • Virology
  • Molecular Biology

Background:

  • Chestnut blight fungus Cryphonectria parasitica and its hypovirus (CHV1) offer a model for studying fungal pathogenesis and virus-host interactions.
  • Understanding how viruses manipulate host cell functions, like protein phosphorylation, is key to deciphering infection mechanisms.

Purpose of the Study:

  • To investigate the role of Cryphonectria hypovirus 1 (CHV1) in regulating protein phosphorylation in C. parasitica.
  • To identify specific host proteins and phosphorylation sites targeted by CHV1.
  • To elucidate the impact of these modifications on fungal biology and viral replication.

Main Methods:

  • Comparative phosphoproteomic analysis between wild-type and CHV1-infected C. parasitica strains.
  • Western blot analysis to confirm protein phosphorylation.
  • Site-specific mutagenesis of identified phosphorylation sites on CpIre1.
  • Reverse-transcription-quantitative PCR (RT-qPCR) to assess gene expression and viral RNA levels.

Main Results:

  • Over 700 differentially phosphorylated sites were identified, with 174 upregulated and 526 downregulated upon CHV1 infection.
  • Phosphorylation of the endoplasmic reticulum (ER) stress-sensing protein CpIre1 at Ser-896 and Ser-897 was significantly influenced by CHV1-encoded proteins (p29, p40, p48).
  • CpIre1 phosphorylation is essential for fungal traits, virulence, stress tolerance, ER homeostasis, and efficient CHV1 replication, with phospho-deficient mutants showing impaired viral RNA accumulation.

Conclusions:

  • CHV1 infection induces significant changes in the phosphoproteome of C. parasitica, notably targeting CpIre1.
  • The phosphorylation of CpIre1 by viral proteins is critical for modulating fungal ER stress response, pathogenicity, and host-virus interactions.
  • This study reveals a novel mechanism of host reprogramming by CHV1 through targeted post-translational modification of CpIre1, impacting both fungal and viral biology.
Keywords:
Cryphonectria parasiticaCpIre1hypovirusphosphorylationunfolded protein responsevirulence

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