Related Experiment Video

Updated: Mar 9, 2026

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

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Autophagy-related protein MoAtg14 is involved in differentiation, development and pathogenicity in the rice blast

Xiao-Hong Liu1, Ya-Hui Zhao1, Xue-Ming Zhu1

  • 1State Key Laboratory for Rice Biology, Biotechnology Institute, Zhejiang University, Hangzhou, 310058, China.

Scientific Reports
|January 10, 2017
PubMed

Insights

The study identifies MoAtg14, a crucial protein in rice blast fungus (M. oryzae), essential for autophagy and pathogenicity. Deleting MoAtg14 disrupts cellular processes, leading to a complete loss of virulence.

Area of Science:

  • Molecular Biology
  • Cell Biology
  • Mycology

Background:

  • Autophagy is a fundamental cellular process for degrading cytoplasmic components via the vacuole/lysosome.
  • MoAtg14, a novel protein in Magnaporthe oryzae (M. oryzae), is identified as a divergent homolog of yeast Atg14 and mammalian BARKOR.

Purpose of the Study:

  • To investigate the function of the uncharacterized MoAtg14 protein in M. oryzae.
  • To elucidate the role of MoAtg14 in autophagy, cellular homeostasis, and pathogenicity.

Main Methods:

  • Gene deletion to create a MoAtg14 deletion mutant (ΔMoatg14).
  • Phenotypic analysis of the mutant, including colony morphology, conidiation, and virulence assays.
  • Microscopic examination of autophagy markers (GFP-MoAtg8) and MoAtg14 localization (GFP-MoAtg14).
  • Analysis of intracellular components like glycogen and lipid bodies.

Main Results:

  • The ΔMoatg14 mutant displayed severe defects: collapsed colonies, reduced conidiation, and complete loss of virulence.
  • Autophagy was blocked in the mutant, evidenced by interrupted degradation of GFP-MoAtg8.
  • Delayed glycogen breakdown, fewer lipid bodies, reduced appressorium turgor, and impaired conidial autophagic cell death were observed.
  • GFP-MoAtg14 co-localized with GFP-MoAtg8, indicating its role in autophagosome formation.
  • A conserved N-terminal coiled-coil domain in MoAtg14 was predicted to mediate interaction with MoAtg6.

Conclusions:

  • MoAtg14 is indispensable for autophagy and pathogenicity in M. oryzae.
  • The coiled-coil domain of MoAtg14 is critical for its function in autophagy and virulence.
  • Understanding MoAtg14's role provides insights into fungal pathogenesis mechanisms.

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