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

• Published in: The Journal of biological chemistry 2005-01, Vol.280 (2), p.1051
• Main Authors: Carol A. Munro, Steven Bates, Ed T. Buurman, H. Bleddyn Hughes, Donna M. MacCallum, Gwyneth Bertram, Abdel Atrih, Michael A. J. Ferguson, Judith M. Bain, Alexandra Brand, Suzanne Hamilton, Caroline Westwater, Lynn M. Thomson, Alistair J. P. Brown, Frank C. Odds, Neil A. R. Gow
• Format: Article
• Language: English
• ISSN: 0021-9258; 1083-351X
• DOI: 10.1074/jbc.M411413200

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 mnt2 Δ and mnt1 Δ 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 mnt1 Δ mnt2 Δ 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.