summary
l n-linked protein glycosylation is a conserved and essential modification mediating protein processing and quality control in the endoplasmic reticulum (er), but how this contributes to the infection cycle of phytopathogenic fungi is largely unknown.
l in this study, we discovered that inhibition of protein n-glycosylation severely affected vegetative growth, hyphal tip development, conidial germination, appressorium formation, and, ultimately, the ability of the maize (zea mays) anthracnose pathogen colletotrichum graminicola to infect its host.
l quantitative proteomics analysis showed that n-glycosylation can coordinate protein o-glycosylation, glycosylphosphatidylinositol anchor modification, and endoplasmic reticulum quality control (erqc) by directly targeting the proteins from the corresponding pathway in the er. we performed a functional study of the n-glycosylation pathway-related protein cgalg3 and of the erqc pathway-related protein cgcnx1, which demonstrated that n-glycosylation of er chaperone proteins is essential for effector stability, secretion, and pathogenicity of c. graminicola.
l our study provides concrete evidence for the regulation of effector protein stability and secretion by n-glycosylation.
new phytologist, if=9.4
https://nph.onlinelibrary.wiley.com/doi/full/10.1111/nph.19213
