Related Experiment Video
Updated: Jul 19, 2025

The Plant Infection Test: Spray and Wound-Mediated Inoculation with the Plant Pathogen Magnaporthe Grisea
Published on: August 4, 2018
A lipid droplet-associated protein Nem1 regulates appressorium function for infection of Magnaporthe oryzae
Deng Chen1, Xuan Cai1, Junjie Xing2
1State Key Laboratory of Agricultural Microbiology and Provincial Key Laboratory of Plant Pathology of Hubei Province, College of Plant Science and Technology, Huazhong Agricultural University, Wuhan, 430070 China.
Abstract:
Lipid droplets are important storages in fungal conidia and can be used by plant pathogenic fungi for infection. However, the regulatory mechanism of lipid droplets formation and the utilization during fungal development and infection are largely unknown. Here, in Magnaporthe oryzae, we identified a lipid droplet-associated protein Nem1 that played a key role in lipid droplets biogenesis and utilization. Nem1 was highly expressed in conidia, but lowly expressed in appressoria, and its encoded protein was localized to lipid droplets. Deletion of NEM1 resulted in reduced numbers of lipid droplets and decreased content of diacylglycerol (DAG) or triacylglycerol (TAG). NEM1 was required for asexual development especially conidia production. The Δnem1 mutant was nearly loss of virulence to host plants due to defects in appressorial penetration and invasive growth. Remarkably, Nem1 was regulated by the TOR signaling pathway and involved in the autophagy process. The Ser303 residue of Nem1 could be phosphorylated by the cAMP-PKA signaling pathway and was important for biological function of Nem1. Together, our study revealed a regulatory mechanism of lipid biogenesis and metabolism during the conidium and appressorium formation of the rice blast fungus.
Supplementary Information:
The online version contains supplementary material available at 10.1007/s42994-023-00098-5.
Insights
This study identifies Nem1, a key protein regulating lipid droplet formation and use in the rice blast fungus. Nem1 is crucial for fungal development, infection, and lipid metabolism, offering insights into plant pathogenic fungi.
Area of Science:
- Mycology
- Plant Pathology
- Molecular Biology
Background:
- Lipid droplets are vital energy stores in fungal conidia for plant pathogen infection.
- The regulation of lipid droplet formation and utilization in fungi remains poorly understood.
Purpose of the Study:
- To investigate the role of lipid droplet-associated protein Nem1 in the rice blast fungus, *Magnaporthe oryzae*.
- To elucidate the regulatory mechanisms of lipid droplet biogenesis and metabolism during fungal development and infection.
Main Methods:
- Gene deletion and characterization of *NEM1* in *Magnaporthe oryzae*.
- Analysis of lipid droplet biogenesis, lipid content (DAG, TAG), asexual development, and virulence.
- Investigation of Nem1 regulation by TOR and cAMP-PKA signaling pathways and its involvement in autophagy.
Main Results:
- Nem1 is localized to lipid droplets and crucial for their biogenesis and lipid content.
- Deletion of *NEM1* impairs conidia production, appressorial penetration, and virulence.
- Nem1 function is regulated by TOR and cAMP-PKA signaling pathways and linked to autophagy.
Conclusions:
- Nem1 plays a critical role in regulating lipid metabolism and droplet dynamics in *Magnaporthe oryzae*.
- Understanding Nem1's function provides insights into fungal development, pathogenicity, and potential targets for disease control.
More Related Videos
07:36Visualizing Early Infection Sites of Rice Blast Disease Magnaporthe oryzae on Barley Hordeum vulgare Using a Basic Microscope and a Smartphone
Published on: March 17, 2023
09:25Genome-wide Analysis of Histone Modifications Distribution using the Chromatin Immunoprecipitation Sequencing Method in Magnaporthe oryzae
Published on: June 2, 2021
Related Concept Videos
Regulation of the Unfolded Protein Response
Gene Regulation During Sporulation
Export of Misfolded Proteins out of the ER
Regulation of Nuclear Protein Sorting
Nonsense-mediated mRNA Decay
Usually, Upf3 binds to an Exon Junction Complex (EJC) at mRNA splice sites. If a ribosome fully translates the mRNA,...