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Acyl-coenzyme A binding protein MoAcb1 regulates conidiation and pathogenicity in Magnaporthe oryzae

Na Cao1, Xue-Ming Zhu2, Jian-Dong Bao2

  • 1College of Biotechnology, Tianjin University of Science and Technology, Tianjin, China.

Frontiers in Microbiology
|May 15, 2023
PubMed

Insights

Researchers identified MoAcb1, a protein involved in fatty acid metabolism, in the rice blast fungus Magnaporthe oryzae. Disrupting MoAcb1 impaired fungal growth, development, and pathogenicity, revealing its crucial role in ER-phagy.

Area of Science:

  • * Molecular Mycology
  • * Plant Pathology
  • * Fungal Pathogenesis

Background:

  • * Magnaporthe oryzae causes rice blast, a major threat to global food security.
  • * Acyl-CoA binding (ACB) proteins are vital for fatty acid metabolism in eukaryotes.
  • * The function of ACB proteins in plant-pathogenic fungi remains largely unexplored.

Purpose of the Study:

  • * To investigate the role of Acyl-CoA binding protein homolog (MoAcb1) in Magnaporthe oryzae.
  • * To elucidate MoAcb1's function in fungal development, pathogenicity, and cellular processes.

Main Methods:

  • * Gene disruption of MoACB1 in M. oryzae.
  • * Phenotypic analysis of Moacb1 mutants (growth, conidiation, appressorium development).
  • * Immunoblotting and chemical drug sensitivity assays to assess ER-phagy involvement.

Main Results:

  • * MoACB1 disruption led to delayed hyphal growth and reduced conidial production.
  • * Moacb1 mutants exhibited delayed appressorium development and impaired glycogen accumulation.
  • * MoAcb1 was implicated in endoplasmic reticulum autophagy (ER-phagy) through immunoblotting and drug sensitivity tests.

Conclusions:

  • * MoAcb1 is essential for conidia germination, appressorium development, and pathogenicity in M. oryzae.
  • * MoAcb1 plays a significant role in regulating autophagy processes within the fungus.
  • * This study highlights MoAcb1 as a potential target for controlling rice blast disease.
Keywords:
ER-phagyMagnaporthe oryzaeacyl-coenzyme A binding proteinappressorium developmentpathogenicity

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