The lipid flippase MoNeo1 mediates vesicle trafficking and pathogenicity in Magnaporthe oryzae.

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.