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Updated: Apr 14, 2026

A Fluorescence-based Assay of Phospholipid Scramblase Activity
Published on: September 20, 2016
The lipid flippase MoNeo1 mediates vesicle trafficking and pathogenicity in Magnaporthe oryzae
Yan Cai1, Xiuwei Huang1, Yufan Nie1
1State Key Laboratory of Agricultural and Forestry Biosecurity & Key Lab of Biopesticide and Chemical Biology, Ministry of Education, College of Plant Protection, Fujian Agriculture and Forestry University, Fuzhou, 350002, China.
Abstract:
The rice blast fungus Magnaporthe oryzae poses a major threat to global rice production. In this study, we characterized MoNeo1, a P4-ATPase flippase, as a key regulator of fungal development and pathogenicity. Deletion of MoNEO1 significantly impaired hyphal growth, conidiation, and appressorium function, and resulted in greatly reduced virulence. Lipidome profiling showed that MoNeo1 is essential for lipid homeostasis. The mutant exhibited significant accumulation of phosphatidylcholine, phosphatidylethanolamine, and phosphatidylserine, in addition to altered concentrations of phosphatidic acid and storage lipids. We further demonstrated that MoNeo1 physically interacts with the retromer subunit MoVps35, and that its subcellular localization at the interface between the trans-Golgi network and endosomes depends on retromer-mediated retrograde transport. Remarkably, MoNeo1 is required for the stability and proper transport of the SNARE protein MoSnc1, an important mediator of effector secretion. Our findings demonstrated MoNeo1 as a central hub that integrates lipid dynamics with vesicle transport to support fungal pathogenesis.
Insights
The P4-ATPase flippase MoNeo1 is crucial for the rice blast fungus Magnaporthe oryzae's growth and infection. It regulates lipid homeostasis and vesicle transport, impacting pathogenicity.
Area of Science:
- Plant pathology
- Molecular biology
- Mycology
Background:
- The rice blast fungus Magnaporthe oryzae is a significant threat to global rice production.
- Understanding the molecular mechanisms underlying fungal development and pathogenicity is critical for disease control.
Purpose of the Study:
- To characterize the role of MoNeo1, a P4-ATPase flippase, in the pathogenicity of Magnaporthe oryzae.
- To investigate the relationship between MoNeo1, lipid homeostasis, and vesicle transport in the fungus.
Main Methods:
- Gene deletion and phenotypic analysis of the MoNEO1 mutant.
- Lipidome profiling to assess changes in lipid composition.
- Co-immunoprecipitation and subcellular localization studies to investigate protein interactions and transport pathways.
Main Results:
- Deletion of MoNEO1 severely impaired fungal growth, conidiation, appressorium formation, and virulence.
- MoNeo1 is essential for maintaining lipid homeostasis, with mutants showing altered levels of various phospholipids and storage lipids.
- MoNeo1 interacts with the retromer component MoVps35 and its localization depends on retromer-mediated transport.
- MoNeo1 is required for the stability and transport of the SNARE protein MoSnc1, essential for effector secretion.
Conclusions:
- MoNeo1 acts as a key regulator of fungal development and pathogenicity in Magnaporthe oryzae.
- The P4-ATPase flippase MoNeo1 integrates lipid dynamics with vesicle transport machinery to facilitate fungal pathogenesis.
- Targeting MoNeo1 could be a potential strategy for controlling rice blast disease.
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