The vacuolar sorting protein AoVps18 regulates mycelial growth, secondary metabolism, and trap formation by modulating the morphology of vacuoles, mitochondria, and lipid droplets in Arthrobotrys oligospora

ABSTRACT: The vacuolar sorting protein AoVps18 is a subunit shared between the HOPS and CORVET complexes and plays essential regulatory roles in vacuole formation. Arthrobotrys oligospora is a common nematode-trapping (NT) fungus that immobilizes and degrades nematodes by forming ingenious traps. In this study, we characterized the function of AoVps18 using gene knockout, phenotypic analysis, transcriptome, and untargeted metabolomics. The ∆Aovps18 mutants exhibited increased mycelial septa and reduced nuclei, disrupting the cell cycle and consequently slowing mycelial growth. Deletion of Aovps18 impaired the morphology of vacuoles, mitochondria, and lipid droplets, resulting in downregulated ATP contents. Both sporulation and trap formation were absent in the mutants, leading to a complete loss of pathogenicity. In the ΔAovps18 mutant strain, 6965 compounds were downregulated and 4044 compounds were upregulated, including reduced levels of three nematode chemotaxis agents: BA, SA, and 6-MOSA. Co-analysis of the transcriptome and metabolome revealed 15 KEGG pathways regulated by AoVps18. By integrating phenotypic analysis, gene expression data, and protein-protein and DNA-protein interactions, we found that AoVps18 is positively regulated by AoSte12 and negatively regulated by AoFus3. This study elucidates the function of Aovps18 in A. oligospora, explores multiple factors affecting pathogenicity, identifies several nematodes chemokines, and provides new insights into the pathogenic mechanisms of NT fungi. These findings offer a theoretical basis for developing biocontrol agents against nematodes.

ORGANISM(S): Orbilia oligospora

PROVIDER: GSE272020 | GEO | 2026/08/08

REPOSITORIES: GEO