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Related Experiment Videos

O-glycosylation.

J F Ernst1, S K Prill

  • 1Institut für Mikrobiologie, Heinnch-Heine-Universität Düsseldorf, Germany. ernstj@rz.uni-duesseldorf.de

Medical Mycology
|January 22, 2002
PubMed
Summary
This summary is machine-generated.

O-glycosylation in Candida albicans, mediated by protein mannosyltransferases (Pmt-proteins), impacts fungal virulence, antifungal resistance, and cell morphology. These processes are crucial for pathogenic traits and represent potential antifungal targets.

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Area of Science:

  • Biochemistry
  • Mycology
  • Molecular Biology

Background:

  • O-glycosylation is a critical post-translational modification in eukaryotes.
  • In fungi, O-glycosylation is initiated by protein mannosyltransferases (Pmt-proteins) in the ER and completed by mannosyltransferases (Mnt-proteins) in the Golgi.
  • Candida albicans is a significant human fungal pathogen where O-glycosylation plays a role in virulence.

Purpose of the Study:

  • To review recent findings on O-glycosylation in Candida albicans.
  • To compare O-glycosylation processes in C. albicans with those in Saccharomyces cerevisiae.
  • To highlight the role of O-glycosylation in fungal virulence and its potential as an antifungal target.

Main Methods:

  • Review of recent literature on O-glycosylation in Candida albicans.

Related Experiment Videos

  • Comparative analysis of O-glycosylation pathways between C. albicans and Saccharomyces cerevisiae.
  • Discussion of the functional impact of Pmt-proteins on fungal traits.

    • Main Results:

    • The Pmt-family in C. albicans has five isoforms, with Pmt1p and Pmt6p being extensively studied.
    • O-glycosylation is essential for modifying secreted and cell-wall proteins.
    • O-glycosylation affects yeast-hyphal dimorphism, antifungal resistance, adherence to host cells, and systemic infection virulence.

    Conclusions:

    • O-glycosylation significantly influences multiple virulence factors of Candida albicans.
    • Pmt-protein activity is directly and indirectly linked to C. albicans pathogenicity.
    • O-glycosylation pathways represent promising targets for novel antifungal drug development.