The hemibiotrophic pathogen Colletotrichum gloeosporioides is the causal agent of poplar anthracnose and causes considerable economic losses. This fungus infects its host through a specialized structure called an appressorium. In a previous study, we demonstrated that the mitogen-activated protein kinase (MAPK) CgMk1 plays a critical role in appressorium formation and pathogenicity. In this study, we identified three upstream components of CgMk1, the putative adaptor protein CgSte50, MAPKKK CgSte11, and MAPKK CgSte7, and showed that CgSte50, CgSte11, and CgSte7 positively regulate the phosphorylation of CgMk1. Deletion of CgSte50, CgSte11, and CgSte7 resulted in the loss of appressorium formation, penetration of the cellophane membrane, invasive growth and pathogenicity, similar to the defects observed in the CgMk1 mutant. CgSte50, CgSte11, CgSte7 and CgMk1 were also required for polarity during conidial germination. At the initial stage of appressorium formation, the accumulation of reactive oxygen species (ROS) was altered in the CgSte50, CgSte11, CgSte7 and CgMk1 deletion mutants compared with that in wild type (WT). Furthermore, the CgSte50, CgSte11, CgSte7 and CgMk1 deletion mutants manifested pleiotropic defects during vegetative growth; all mutants exhibited albino colonies, and the aerial hyphae had reduced hydrophobicity. In the mutants, autolysis was detected at the colony edge, and septum formation in the hyphae was elevated compared with that in the WT hyphae. Moreover, deletion of CgSte50, CgSte11, CgSte7 and CgMk1 affected vegetative growth under nitrogen-limiting and osmotic stress conditions. CgSte50, CgSte11, and CgSte7 but not CgMk1 were required for the oxidative stress response. Taken together, these results indicate that the CgMk1 MAPK cascade plays vital roles in various important functions in C. gloeosporioides.
Keywords: Appressorium; Colletotrichum gloeosporioides; Mitogen-activated protein kinase; Mk1; Pathogenicity.
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