A fungal core effector exploits the OsPUX8B.2-OsCDC48-6 module to suppress plant immunity

Xuetao Shi1,2, Xin Xie1, Yuanwen Guo1

  • 1State Key Laboratory for Biology of Plant Diseases and Insect Pests, Institute of Plant Protection, Chinese Academy of Agricultural Sciences, Beijing, 100193, China.

Nature Communications
|March 23, 2024
PubMed

Insights

Magnaporthe oryzae

Area of Science:

  • Plant-pathogen interactions
  • Molecular plant-pathology
  • Protein quality control mechanisms

Background:

  • Ubiquitin regulatory X (UBX) domain proteins are cofactors of Cell Division Cycle 48 (CDC48) involved in protein quality control.
  • The role of UBX proteins in host-microbe interactions is not well understood.
  • Magnaporthe oryzae is a fungal pathogen that causes rice blast disease.

Purpose of the Study:

  • To investigate the role of UBX-containing proteins in rice immunity against Magnaporthe oryzae.
  • To elucidate the mechanism by which the fungal effector MoNLE1 interacts with rice proteins.

Main Methods:

  • Yeast two-hybrid assays to identify protein interactions.
  • Co-immunoprecipitation to confirm protein binding.
  • Quantitative real-time PCR to analyze gene expression.
  • Confocal microscopy to observe protein localization.

Main Results:

  • MoNLE1, a Magnaporthe oryzae effector, suppresses rice immunity by targeting OsPUX8B.2.
  • OsPUX8B.2's UBX domain is crucial for its interaction with OsATG8 and OsCDC48-6, regulating its stability via the 26S proteasome.
  • OsPUX8B.2 and OsCDC48-6 enhance rice immunity, while OsBHT negatively regulates defense against blast fungus.
  • MoNLE1 induces OsPUX8B.2 degradation and disrupts its interaction with OsBHT.

Conclusions:

  • MoNLE1 virulence relies on disrupting the OsPUX8B.2-OsCDC48-6 complex, leading to immune suppression.
  • Engineering intracellular proteins resistant to MoNLE1 could confer broad and durable blast resistance in plants.

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