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Cited by 200Fungal and yeast genetics researchGlycosylation and Glycoproteins ResearchAntifungal resistance and susceptibility

Mnt1p and Mnt2p of Candida albicans Are Partially Redundant α-1,2-Mannosyltransferases That Participate in O-Linked Mannosylation and Are Required for Adhesion and Virulence

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Munro, Carol A., Bates, Steven, Buurman, Ed T., Hughes, H. Bleddyn, MacCallum, Donna M., Bertram, Gwyneth, Atrih, Abdel, Ferguson, Michael A.J. +8 more·2005·Journal of Biological Chemistry
DOI 10.1074/jbc.m411413200PMC PMC3749086
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Abstract

The MNT1 gene of the human fungal pathogen Candida albicans is involved in O-glycosylation of cell wall and secreted proteins and is important for adherence of C. albicans to host surfaces and for virulence. Here we describe the molecular analysis of CaMNT2, a second member of the MNT1-like gene family in C. albicans. Mnt2p also functions in O-glycosylation. Mnt1p and Mnt2p encode partially redundant alpha-1,2-mannosyltransferases that catalyze the addition of the second and third mannose residues in an O-linked mannose pentamer. Deletion of both copies of MNT1 and MNT2 resulted in reduction in the level of in vitro mannosyltransferase activity and truncation of O-mannan. Both the mnt2Delta and mnt1Delta single mutants were significantly reduced in adherence to human buccal epithelial cells and Matrigel-coated surfaces, indicating a role for O-glycosylated cell wall proteins or O-mannan itself in adhesion to host surfaces. The double mnt1Deltamnt2Delta mutant formed aggregates of cells that appeared to be the result of abnormal cell separation. The double mutant was attenuated in virulence, underlining the importance of O-glycosylation in pathogenesis of C. albicans infections.

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  • Cell wall and extracellular matrix polysaccharides have mechanistic roles implicated in protection of Candida species from host response and drug therapies.

    “Cell wall and extracellular matrix polysaccharides have mechanistic roles implicated in the protection of Candida species from host response and drug therapies (13–16).”

    From Dual function of <i>Candida auris</i> mannosyltransferase, MNT5, in biofilm community protection from antifungal therapy and the host (2025) · cites this paper as [15]

    The introduction (indexed under Abstract; page unavailable) says C. albicans cell-wall components participate in host-response immunomodulation and adhesion, supporting a role in host interactions. The Results section on wall-damaging agents reports sensitivity to laboratory inhibitors, not protection from drug therapies. The paper does not establish a protective role for extracellular-matrix polysaccharides, and its findings concern C. albicans rather than Candida species generally. (LLM, conf=0.84)

    Experimental — accuracy not yet measured

  • Cell wall mannan masks immunostimulatory cell wall components preventing host cell recognition.

    “Similarly, cell wall mannan masks immunostimulatory cell wall components preventing host cell recognition (15, 21).”

    From Dual function of <i>Candida auris</i> mannosyltransferase, MNT5, in biofilm community protection from antifungal therapy and the host (2025) · cites this paper as [15]

    The introductory passage (labeled Abstract in our copy; page unavailable) says the outer cell-wall layer is enriched in mannoproteins and that the cell surface participates in immunomodulation. Neither that passage nor the Discussion passages say that mannan masks immunostimulatory components or prevents host-cell recognition; searches for masking and immune recognition found no such statement. (LLM, conf=0.76)

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Authors
Munro, C. A., Bates, S., Buurman, E. T., Hughes, H. B., MacCallum, D. M., Bertram, G., Atrih, A., Ferguson, M. A. J., Bain, J. M., Brand, A., Hamilton, S., Westwater, C., Thomson, L. M., Brown, A. J. P., Odds, F. C., & Gow, N. A. R.
Affiliations
  • University of Aberdeen (GB)
  • University of Dundee (GB)
Corresponding author
Gow, Neil A.R.
ORCID
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
2005-01
Volume
280
Issue
2
Pages
1051-1060
ISSN
0021-9258 (ISSN-L)
DOI
10.1074/jbc.m411413200
PMC
PMC3749086
OpenAlex
W2163567142
Cited by
200
References
5
Citations by year
2026: 5 · 2025: 8 · 2024: 16 · 2023: 5 · 2022: 6 · 2021: 4 · 2020: 11 · 2019: 8 · 2018: 11 · 2017: 10 · 2016: 10 · 2015: 8 · 2014: 14 · 2013: 9 · 2012: 12
FWCI
2.61
Type
journal article
Language
en
Open access
Licence
Locations
  • Journal of Biological Chemistry (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • Discovery Research Portal (University of Dundee) (publishedVersion)
  • Europe PMC (PubMed Central) (acceptedVersion)
  • PubMed Central (acceptedVersion)
Funders
Wellcome Trust (063204)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fungal and yeast genetics research
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glycosylation and Glycoproteins Research
  • Health Sciences › Medicine › Infectious Diseases › Antifungal resistance and susceptibility
Keywords
Candida albicans, O-glycosylation, gene redundancy, fungal adhesion, virulence, buccal epithelial cells, cell aggregation
MeSH terms
Candida albicans, Cell Adhesion, Cell Wall, Fungal Proteins, Mannose, Mannosyltransferases, Methylation, Molecular Sequence Data, Polysaccharides, Mass Spectrometry, Virulence, Gene Deletion, Virulence Factors, Cell Shape, Cell Proliferation

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