N-glycosylation of the protein disulfide isomerase Pdi1 ensures full Ustilago maydis virulence.

ABSTRACT: Fungal pathogenesis depends on accurate secretion and location of virulence factors which drive host colonization. Protein glycosylation is a common posttranslational modification of cell wall components and other secreted factors, typically required for correct protein localization, secretion and function. Thus, the absence of glycosylation is associated with animal and plant pathogen avirulence. While the relevance of protein glycosylation for pathogenesis has been well established, the main glycoproteins responsible for the loss of virulence observed in glycosylation-defective fungi have not been identified. Here, we devise a proteomics approach to identify such proteins and use it to demonstrate a role for the highly conserved protein disulfide isomerase Pdi1 in virulence. We show that

SUBMITTER: Marin-Menguiano M 

PROVIDER: S-EPMC6881057 | biostudies-literature | 2019 Nov

REPOSITORIES: biostudies-literature