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Many functions of vacuole depend on the activity of vacuolar ATPase which is essential to maintain an acidic lumen and create the driving forces for massive fluxes of ions and metabolites through vacuolar membrane. In filamentous fungusMagnaportheoryzae    , subcellular colocalization and quinacrine staining suggested that the V 1 V 0  domains of V-ATPase were fully assembled and the vacuoles were kept acidic during infection-related developments. Targeted gene disruption of  MoVMA11  gene, encoding the putative c’ subunit of V-ATPase, impaired vacuolar acidification and mimicked the phenotypes of yeast V-ATPase mutants in the poor colony morphology, abolished asexual and sexual reproductions, selective carbon source utilization, and increased calcium and heavy metals sensitivities, however, not in the typical pH conditional lethality. Strikingly, aerial hyphae of the  MoVMA11  null mutant intertwined with each other to form extremely thick filamentous structures. The results also implicated that  MoVMA11  was involved in cell wall integrity and appressorium formation. Abundant non-melanized swollen structures and rare, small appressoria without penetration ability were produced at the hyphal tips of the  ΔMovma11  mutant on onion epidermal cells. Finally, the  MoVMA11  null mutant lost pathogenicity on both intact and wounded host leaves. Overall, our data indicated that  MoVMA11 , like other fungal  VMA  genes, is associated with numerous cellular functions and highlighted that V-ATPase is essential for infection-related morphogenesis and pathogenesis inM.  oryzae    .

Involvement of MoVMA11, a Putative Vacuolar ATPase c’ Subunit, in Vacuolar Acidification and Infection-Related Morphogenesis of Magnaporthe oryzae