MoSNF1 regulates sporulation and pathogenicity in the rice blast fungus Magnaporthe oryzae.

The protein kinase Snf1 is a major component of the glucose derepression pathway in yeast and a regulator of gene expression for the cell wall degrading enzyme (CWDE) in some plant pathogenic fungi. To address the molecular function of Snf1 in Magnaporthe oryzae, which causes the rice blast disease, MoSNF1 was cloned and functionally characterized using gene knock-out strategies. MoSNF1 functionally complemented the growth defect of the yeast snf1 mutant on a non-fermenting carbon source. However, the growth rate of the Deltamosnf1 mutant on various carbon sources was reduced independent of glucose, and the expression of the CWDE genes in the mutant was induced during derepressing condition like the wild type. The pre-penetration stage including conidial germination and appressorium formation of the Deltamosnf1 was largely impaired, and the pathogenicity of the Deltamosnf1 was significantly reduced. Most strikingly, the Deltamosnf1 mutant produced only a few conidia and had a high frequency of abnormally shaped conidia compared to the wild type. Our results suggest that MoSNF1 is a functional homolog of yeast Snf1, but its contribution to sporulation, vegetative growth and pathogenicity is critical in M. oryzae.