Functional analysis of MoSnf7 in Magnaporthe oryzae.

Snf7 is the core subunit protein of the yeast endosomal sorting complex required for transport (ESCRT) complex, which plays important roles in endocytosis and autophagy. In this study, we characterized MoSnf7 in Magnaporthe oryzae, a homolog of yeast Snf7, the core protein of ESCRT-III subcomplex. Like Snf7, MoSnf7 also localizes next to the vacuoles. Deletion of MoSNF7 resulted in significant decrease in vegetative growth and pathogenicity. Further analyses of ΔMosnf7 mutants showed that they were defective in endocytosis, sexual and asexual development, turgor pressure maintenance of appressorium at hyphal tips, and cell wall integrity. Additional assays for the localization and degradation of GFP-MoAtg8 in ΔMosnf7 mutants showed that they were defective in autophagy pathway. Based on the roles of yeast Snf7 in endocytosis and autophagy, we propose that the decreased vegetative growth and pathogenicity of ΔMosnf7 rice blast fungus M. oryzae, was partly due to the conservative roles of MoSnf7 in vesicle trafficking and autophagy pathway.