ArticlePLoS pathogens2019
N-glycosylation of the protein disulfide isomerase Pdi1 ensures full Ustilago maydis virulence.
Article in PLoS pathogens, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 54 citations in OpenAlex.
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- Biocontrol potential of phyllosphere fungi from diseased leaves against Colletotrichum gloeosporioides and Pseudocryphonectria elaeocarpicola.Archives of microbiology · 2026Article
- Protein Extraction Methods for Ustilago maydis.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Emerging roles of protein modifications in sexual reproduction and pathogenesis of filamentous fungi.Frontiers in microbiology · 2026Review
- Functions ofJournal of fungi (Basel, Switzerland) · 2025Review
- Chromosome-level comparative genomics and host-specific fungal transcriptomics uncover adaptive virulence strategies in the sugarcane smut pathogen.BMC genomics · 2025Article
- Genomic insights into the virulence repertoire and hemibiotrophic lifestyle of the grapevine black rot pathogen Phyllosticta ampelicida.G3 (Bethesda, Md.) · 2025Article
- N-Glycosylation-The Behind-the-Scenes 'Manipulative Hand' of Plant Pathogen Invasiveness.Molecular plant pathology · 2025Review
- Structural and Functional Analysis of the Lectin-like Protein Llp1 Secreted byJournal of fungi (Basel, Switzerland) · 2025Article
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- Genetic diversity and molecular evolution of 3-carboxymuconate cyclase (Gp60-70), the major antigen in pathogenicMycology · 2025Article
- N-glycosylation of the envelope glycoprotein I is essential for the proliferation and virulence of the duck plague virus.Veterinary research · 2024Article
- Regulatory insight for a Zn2Cys6 transcription factor controlling effector-mediated virulence in a fungal pathogen of wheat.PLoS pathogens · 2024Article
- Uncovering the Antifungal Potential of Plant-Associated Cultivable Bacteria from the Aral Sea Region against Phytopathogenic Fungi.Pathogens (Basel, Switzerland) · 2024Article
- Evaluation of biotechnological processing through solid-state fermentation of oilseed cakes on extracts bioactive potential.Biotechnology letters · 2023Article
- Structural and functional analysis of the cerato-platanin-like protein Cpl1 suggests diverging functions in smut fungi.Molecular plant pathology · 2023Article
- Antifungal activity of volatile and non-volatile metabolites of endophytes ofFrontiers in plant science · 2023Article
- Transcriptome Comparison between Two Strains ofJournal of fungi (Basel, Switzerland) · 2022Article
- Review
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
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 efficient Pdi1 N-glycosylation, which promotes folding into the correct protein conformation, is required for full pathogenic development of the corn smut fungus Ustilago maydis. Remarkably, the observed virulence defects are reminiscent of those seen in glycosylation-defective cells suggesting that the N-glycosylation of Pdi1 is necessary for the full secretion of virulence factors. All these observations, together with the fact that Pdi1 protein and RNA expression levels rise upon virulence program induction, suggest that Pdi1 glycosylation is important for normal pathogenic development in U. maydis. Our results provide new insights into the role of glycosylation in fungal pathogenesis.
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