Glucose-6-Phosphate Isomerase FgGPI, a β2 Tubulin-Interacting Protein, Is Indispensable for Fungal Development and Deoxynivalenol Biosynthesis in Fusarium graminearum

Abstract

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 FgGPI in the phytopathogen Fusarium graminearum. We found that hyphal growth, conidial germination, and septa formation were significantly inhibited in FgGPI deletion mutant ∆FgGPI. 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 Fgβ2. More importantly, the coimmunoprecipitation assay showed that carbendazim-resistant substitutions in β2 tubulin could reduce the interaction intensity between FgGPI and Fgβ2, thereby increasing FgGPI expression and accelerating DON biosynthesis in carbendazim-resistant strains. Taken together, our work revealed the indispensable role of FgGPI in fungal developmental processes, DON biosynthesis, and pathogenicity in F. graminearum.