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

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 fam...

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Bibliographic Details
Published in:The Journal of biological chemistry 2005-01, Vol.280 (2), p.1051-1060
Main Authors: Munro, Carol A., Bates, Steven, Buurman, Ed T., Hughes, H. Bleddyn, MacCallum, Donna M., Bertram, Gwyneth, Atrih, Abdel, Ferguson, Michael A.J., Bain, Judith M., Brand, Alexandra, Hamilton, Suzanne, Westwater, Caroline, Thomson, Lynn M., Brown, Alistair J.P., Odds, Frank C., Gow, Neil A.R.
Format: Article
Language:English
Subjects:
Candida albicans
Candida albicans - chemistry
Candida albicans - cytology
Candida albicans - enzymology
Candida albicans - pathogenicity
Cell Adhesion
Cell Proliferation
Cell Shape
Cell Wall - chemistry
Cell Wall - metabolism
Fungal Proteins - genetics
Fungal Proteins - isolation & purification
Fungal Proteins - metabolism
Gene Deletion
Mannose - metabolism
Mannosyltransferases - deficiency
Mannosyltransferases - genetics
Mannosyltransferases - isolation & purification
Mannosyltransferases - metabolism
Mass Spectrometry
Methylation
Molecular Sequence Data
Polysaccharides - analysis
Polysaccharides - chemistry
Virulence - physiology
Virulence Factors - genetics
Virulence Factors - isolation & purification
Virulence Factors - metabolism
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Summary: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 α-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 mnt2Δ and mnt1Δ 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 mnt1Δmnt2Δ 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.
ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.M411413200