Abstract

Protein O-mannosyltransferases (Pmts) comprise a group of proteins that add mannoses to substrate proteins at the endoplasmic reticulum. This post-translational modification is important for the faithful transfer of nascent glycoproteins throughout the secretory pathway. Most fungi genomes encode three O-mannosyltransferases, usually named Pmt1, Pmt2, and Pmt4. In pathogenic fungi, Pmts, especially Pmt4, are key factors for virulence. Although the importance of Pmts for fungal pathogenesis is well established in a wide range of pathogens, questions remain regarding certain features of Pmts. For example, why does the single deletion of each pmt gene have an asymmetrical impact on host colonization? Here, we analyse the origin of Pmts in fungi and review the most important phenotypes associated with Pmt mutants in pathogenic fungi. Hence, we highlight the enormous relevance of these glycotransferases for fungal pathogenic development.

Highlights

  • Glycosylation is a post-translational protein modification in which specific sugar donor molecules are synthesized, added to specific amino acids in target proteins, and processed during their transfer throughout the secretory pathway [1]

  • We further explored the possible origin of Pmt1 from a previously established ancestral form, Pmt2 or Pmt4

  • We investigated the relationships between the three Protein O-mannosyltransferases (Pmts) from different species (Homo sapiens, Drosophila melanogaster, S. cerevisiae, and U. maydis) through the domains that compose them (Figure 3a)

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Summary

Introduction

Glycosylation is a post-translational protein modification in which specific sugar donor molecules are synthesized, added to specific amino acids in target proteins, and processed during their transfer throughout the secretory pathway [1]. Crucial elements for infection have been identified in the glycosylation pathways of the smut fungus Ustilago maydis [15,16,17], a maize pathogen These key factors are all conserved in other smut fungi but not in their hosts. 2. Protein Glycosylation in Fungi Based on studies over the past three decades in the budding yeast Saccharomyces cerevisiae, the pioneer model organism for the characterization of protein glycosylation pathways, two major types of glycosylation can be defined in fungi: N-glycosylation and O-mannosylation (Figure 1a). Protein Glycosylation in Fungi Based on studies over the past three decades in the budding yeast Saccharomyces cerevisiae, the pioneer model organism for the characterization of protein glycosylation pathways, two major types of glycosylation can be defined in fungi: N-glycosylation and O-mannosylation (Figure 1a) Both take place at the endoplasmic reticulum (ER) and Golgi apparatus [18,19]

N-Glycosylation
O-Mannosylation and the Pmt Family
The Structure of Pmts
The Origin of Fungi-Specific Pmt1 Might Be Pmt4
The Addition of a Third Pmt in Fungi
The Role of Pmts in Fungal Pathogenesis
Pmt2 and Its Essential Role for Cell Viability
Conclusions
Findings
Methods
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