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.

Stress Biology
|April 13, 2026
PubMed

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.

Related Concept Videos

Membrane Asymmetry Regulating Transporters01:19

Membrane Asymmetry Regulating Transporters

Enzymes like flippase, floppase, and scramblase transfer phospholipids from one layer to another in the membrane, thereby affecting membrane asymmetry.
Flippase
Eukaryotic flippases are type-IV P-type ATPases or P4-ATPases belonging to P-type ATPase family proteins that are membrane-bound pumps involved in the ATP-mediated transport of ions and molecules across the membrane. Flippases flip specific phospholipids from the outer to the inner leaflet of a membrane. All P4-ATPases have one...
8.0K
Membrane Fluidity01:26

Membrane Fluidity

Membrane fluidity is explained by the fluid mosaic model of the cell membrane, which describes the plasma membrane structure as a mosaic of components—including phospholipids, cholesterol, proteins, and carbohydrates—that gives the membrane a fluid character.
Mosaic nature of the membrane
The mosaic characteristic of the membrane helps the plasma membrane remain fluid. The integral proteins and lipids exist as separate but loosely-attached molecules in the membrane. The membrane is...
18.2K
Membrane Fluidity01:23

Membrane Fluidity

Cell membranes are composed of phospholipids, proteins, and carbohydrates loosely attached to one another through chemical interactions. Molecules are generally able to move about in the plane of the membrane, giving the membrane its flexible nature called fluidity. Two other features of the membrane contribute to membrane fluidity: the chemical structure of the phospholipids and the presence of cholesterol in the membrane.
179.8K
Export of Misfolded Proteins out of the ER01:32

Export of Misfolded Proteins out of the ER

After folding, the ER assesses the quality of secretory and membrane proteins. The correctly folded proteins are cleared by the calnexin cycle for transport to their final destination, while misfolded proteins are held back in the ER lumen. The ER chaperones attempt to unfold and refold the misfolded proteins but sometimes fail to achieve the correct native conformation. Such terminally misfolded proteins are then exported to the cytosol by ER-associated degradation or ERAD pathway for...
5.7K
Pinching-off of Coated Vesicles01:32

Pinching-off of Coated Vesicles

Vesicle budding is orchestrated by distinct cytosolic proteins such as adaptor proteins, coat proteins, and GTPases. To initiate vesicle budding, membrane-bending proteins containing crescent-shaped BAR domains bind to the lipid heads in the bilayer and distort the membrane to form a protein-coated vesicle bud. Adaptors proteins such as AP2 for clathrin-coated vesicles can nucleate on the deformed membrane. Finally, coat proteins such as clathrin or COPI and COPII assemble into a coat forming...
4.5K
Mechanism of Filopodia Formation01:39

Mechanism of Filopodia Formation

Filopodia are thin, actin-rich cellular protrusions that play an important role in many fundamental cellular functions. They vary in their occurrence, length, and positioning in different cell types, suggesting their diverse roles.
Their main function is to guide migrating cells during normal tissue morphogenesis or cancer metastasis by recognizing and making initial contacts with the extracellular matrix. However, they can also act as stationary cell anchors or help to establish communication...
3.5K