Effector secretion and stability in the maize anthracnose pathogen Colletotrichum graminicola requires N-linked protein glycosylation and the ER chaperone pathway

文献类型： 外文期刊

第一作者： Mei, Jie

作者： Mei, Jie;Li, Zhiqiang;Liu, Wende;Mei, Jie;Zhou, Shaoqun;Chen, Xiao-Lin;Chen, Xiao-Lin;Wilson, Richard A.

作者机构：

关键词： Colletotrichum graminicola; endoplasmic reticulum quality control (ERQC); N-glycosylation; quantitative proteomics; unfolded protein response (UPR)

期刊名称：NEW PHYTOLOGIST （ 影响因子：9.4； 五年影响因子：10.5 ）

ISSN： 0028-646X

年卷期： 2023 年

页码：

收录情况： SCI

摘要： center dot 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. center dot 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. center dot 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. center dot Our study provides concrete evidence for the regulation of effector protein stability and secretion by N-glycosylation.

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