Glucose-6-Phosphate Isomerase FgGPI, a β Tubulin-Interacting Protein, Is Indispensable for Fungal Development and Deoxynivalenol Biosynthesis in .

Glucose-6-phosphate isomerase (GPI) is ubiquitous in most organisms, catalyzing the reversible isomerization of glucose-6-phosphate and fructose-6-phosphate. In this study, we investigated biological and genetic functions of in the phytopathogen . We found that hyphal growth, conidial germination, and septa formation were significantly inhibited in deletion mutant ∆FgGPI. was also positively associated with glucose metabolism, ATP biosynthesis, and carbon source utilization. In addition, pyruvate production, deoxynivalenol (DON) biosynthesis, and virulence were reduced in ∆FgGPI. A coimmunoprecipitation assay demonstrated that FgGPI interacts with Fgβ. More importantly, the coimmunoprecipitation assay showed that carbendazim-resistant substitutions in β tubulin could reduce the interaction intensity between FgGPI and Fgβ, thereby increasing FgGPI expression and accelerating DON biosynthesis in carbendazim-resistant strains. Taken together, our work revealed the indispensable role of in fungal developmental processes, DON biosynthesis, and pathogenicity in .