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Updated: Jun 30, 2025

Screening and Identification of RNA Silencing Suppressors from Secreted Effectors of Plant Pathogens
Published on: February 3, 2020
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.
Abstract:
Proteins containing a ubiquitin regulatory X (UBX) domain are cofactors of Cell Division Cycle 48 (CDC48) and function in protein quality control. However, whether and how UBX-containing proteins participate in host-microbe interactions remain unclear. Here we show that MoNLE1, an effector from the fungal pathogen Magnaporthe oryzae, is a core virulence factor that suppresses rice immunity by specifically interfering with OsPUX8B.2. The UBX domain of OsPUX8B.2 is required for its binding to OsATG8 and OsCDC48-6 and controls its 26 S proteasome-dependent stability. OsPUX8B.2 and OsCDC48-6 positively regulate plant immunity against blast fungus, while the high-temperature tolerance heat-shock protein OsBHT, a putative cytoplasmic substrate of OsPUX8B.2-OsCDC48-6, negatively regulates defense against blast infection. MoNLE1 promotes the nuclear migration and degradation of OsPUX8B.2 and disturbs its association with OsBHT. Given the high conservation of MoNLE1 among fungal isolates, plants with broad and durable blast resistance might be generated by engineering intracellular proteins resistant to MoNLE1.
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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