Related Experiment Video

Updated: Feb 24, 2026

Genome-wide Analysis of Histone Modifications Distribution using the Chromatin Immunoprecipitation Sequencing Method in Magnaporthe oryzae
09:25

Genome-wide Analysis of Histone Modifications Distribution using the Chromatin Immunoprecipitation Sequencing Method in Magnaporthe oryzae

Published on: June 2, 2021

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ERAD Component MoHrd3 Facilitates Pathogenicity and Establishes a Direct Regulation on Autophagy in Magnaporthe

Huiqing Xia1, Yunna Zheng1, Nan Yang1

  • 1State Key Laboratory of Agricultural and Forestry Biosecurity, MARA Key Lab of Pest Monitoring and Green Management, College of Plant Protection, China Agricultural University, Beijing, China.

Advanced Science (Weinheim, Baden-Wurttemberg, Germany)
|February 23, 2026
PubMed

Insights

ER-associated degradation (ERAD) protein MoHrd3 regulates autophagy in the rice blast fungus. This ERAD-autophagy connection is vital for pathogen growth and infection, revealing new mechanisms for controlling this devastating plant disease.

Area of Science:

  • Molecular Biology
  • Plant Pathology
  • Cellular Biology

Background:

  • ER-associated degradation (ERAD) and autophagy are critical for ER protein homeostasis.
  • The interplay between ERAD and autophagy remains poorly understood.
  • Magnaporthe oryzae causes significant crop losses in rice and wheat.

Purpose of the Study:

  • To investigate the role of ERAD in regulating autophagy in Magnaporthe oryzae.
  • To elucidate the molecular mechanisms connecting ERAD and autophagy in fungal pathogenicity.
  • To identify novel targets for controlling rice and wheat blast disease.

Main Methods:

  • Gene deletion and characterization of MoHrd3 in M. oryzae.
  • Analysis of autophagy levels and autophagosome-vacuole fusion.
  • Co-immunoprecipitation assays to study protein interactions (MoHrd3, MoAtg8, MoYpt7).
  • Assessment of pathogenicity in MoHrd3 mutants.

Main Results:

  • MoHrd3 deletion impairs fungal growth, conidiation, and pathogenicity.
  • Loss of MoHrd3 reduces autophagy and disrupts autophagosome-vacuole fusion.
  • MoHrd3 acts as a bridge between MoAtg8 (autophagosome) and MoYpt7 (vacuole), facilitating organelle fusion.
  • MoHrd3 also targets MoPth11 for autophagic degradation, essential for appressorium formation.

Conclusions:

  • MoHrd3 directly links ERAD and autophagy pathways in M. oryzae.
  • The MoHrd3-mediated ERAD-autophagy interaction is crucial for fungal pathogenicity.
  • This study reveals novel insights into protein quality control mechanisms in plant pathogens.
Keywords:
ERADMoAtg8MoHrd3autophagymagnaporthe oryzaepathogenicity

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