Pleiotropic roles of O-mannosyltransferase MoPmt4 in development and pathogenicity of Magnaporthe oryzae.

Abstract

In fungi, O-mannosylation is one type of conserved protein modifications that add the carbohydrate residues to specific residues of target proteins by protein O-mannosyltransferases. Previously, three members of O-mannosyltransferases were identified in Magnaporthe oryzae, with MoPmt2 playing important roles in fungal growth and pathogenicity. However, the biological roles of the rest Pmt proteins remain unclear. In this study, to understand if O-mannosyltransferases are crucial for fungal pathogenicity of M. oryzae, the Pmt-coding genes MoPmt1 and MoPmt4 were separately disrupted and their roles in pathogenesis were analyzed. Of the two genes, only MoPmt4 is specifically required for full virulence of M. oryzae. Deletion of MoPmt4 resulted in defects on radial growth, with more branching hyphae and septa as compared to Guy11. The MoPmt4 mutant was severely impaired not only in conidiation, but also in both penetration and biotrophic invasion in susceptible rice plants. This mutant also had defects in suppression of host-derived ROS-mediated plant defense responses that might be ascribed from the reduced activities of extracellular enzymes. Furthermore, like their fungi counterparts, MoPmt4 localized in the ER and had O-mannosyltransferase activity. Domain disruption analysis indicated that mannosyltransferase activity regulated by PMT domain of MoPmt4 is crucial for fungal development and pathogenicity of M. oryzae. Taken together, these data suggest that MoPmt4 is a protein O-mannosyltransferase essential for fungal development and full virulence of M. oryzae.