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

• DOI: 10.1371/journal.ppat.1007687
• Publication Date: 2019-11-15T14:36:36Z
• Authors: Miriam Marín-Meng...; Ismael Moreno-Sán...; Ramón R. Barrales; Alfonso Fernández...; José Ignacio Ibeas
• Keywords: Ustilago; N-linked glycosylation

Fungal pathogenesis depends on accurate secretion and location of virulence factors which drive host colonization. Protein glycosylation is a common posttranslational modification cell wall components other secreted factors, typically required for correct protein localization, function. Thus, the absence associated with animal plant pathogen avirulence. While relevance has been well established, main glycoproteins responsible loss observed in glycosylation-defective fungi have not identified. Here, we devise proteomics approach to identify such proteins use it demonstrate role highly conserved disulfide isomerase Pdi1 virulence. We show that efficient N-glycosylation, promotes folding into conformation, full pathogenic development corn smut fungus Ustilago maydis. Remarkably, defects are reminiscent those seen cells suggesting N-glycosylation necessary factors. All these observations, together fact RNA expression levels rise upon program induction, suggest important normal U. Our results provide new insights fungal pathogenesis.