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The ArfGAP protein MoGlo3 regulates the development and pathogenicity of Magnaporthe oryzae

Shengpei Zhang1, Xiu Liu1, Lianwei Li1

  • 1Department of Plant Pathology, College of Plant Protection, Nanjing Agricultural University, and Key Laboratory of Integrated Management of Crop Diseases and Pests, Ministry of Education, Nanjing 210095, People's Republic of China.

Environmental Microbiology
|May 16, 2017
PubMed

Insights

Researchers identified MoGlo3, an ArfGAP protein, crucial for vesicle transport in the rice blast fungus Magnaporthe oryzae. Its absence impairs growth, development, and pathogenicity by affecting endocytosis and stress responses.

Area of Science:

  • Molecular Biology
  • Mycology
  • Cell Biology

Background:

  • ADP ribosylation factor (Arf) and coat protein complex I (COPI) regulate vesicle transport.
  • Arf GTPase-activating proteins (ArfGAPs) and guanine exchange factors (ArfGEFs) control Arf activity, vesicle formation, COPI trafficking, and Golgi maintenance.
  • Membrane trafficking plays a critical role in the pathogenesis of Magnaporthe oryzae.

Purpose of the Study:

  • To investigate the function of MoGlo3, an ArfGAP protein in Magnaporthe oryzae.
  • To understand the role of MoGlo3 in vesicle transport, fungal physiology, and pathogenicity.
  • To determine the importance of specific MoGlo3 domains for its function.

Main Methods:

  • Identification and characterization of MoGlo3 in Magnaporthe oryzae.
  • Complementation assays using yeast Glo3p.
  • Subcellular localization studies of MoGlo3.
  • Gene deletion mutant analysis (ΔMoglo3).
  • Assessment of fungal growth, development, and pathogenicity.
  • Analysis of endocytosis, reactive oxygen species scavenging, and endoplasmic reticulum stress response.

Main Results:

  • MoGlo3, homologous to yeast Glo3p, partially complements yeast Glo3p function.
  • MoGlo3 localizes to the Golgi, dependent on the BoCCS domain.
  • MoGlo3 is highly expressed during conidiation and early infection stages.
  • The ΔMoglo3 mutant exhibits defects in vegetative growth, conidiation, sexual development, endocytosis, ROS scavenging, and ER stress response.
  • MoGlo3 is essential for appressorium function and pathogenicity.
  • The GAP, BoCCS, and GRM domains are critical for MoGlo3 function.

Conclusions:

  • MoGlo3 is a vital ArfGAP involved in membrane trafficking in Magnaporthe oryzae.
  • Normal membrane trafficking mediated by MoGlo3 is essential for fungal physiology and pathogenicity.
  • MoGlo3 plays a significant role in regulating endocytosis, stress responses, and developmental processes, ultimately impacting the virulence of the rice blast fungus.

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