Structural, Evolutionary, and Functional Analysis of the Protein O-Mannosyltransferase Family in Pathogenic Fungi

Journal of Fungi

DamienP. Devos¹  Alfonso Fernández-Álvarez¹  JoséIgnacio Ibeas¹  MaríaDolores Pejenaute-Ochoa¹  Carlos Santana-Molina¹ 

[1] Andalusian Center for Developmental Biology (Pablo de Olavide University/Consejo Superior de Investigaciones Científicas/Junta de Andalucía), 41013 Sevilla, Spain;

关键词: Pmt;    Ustilago maydis;    glycosylation;    appressorium;    pathogens;   

DOI  :  10.3390/jof7050328

来源: DOAJ

【 摘 要 】

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.

【 授权许可】

Unknown