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J. Biol. Chem., Vol. 280, Issue 2, 1051-1060, January 14, 2005

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

From the ^aSchool of Medical Sciences, Institute of Medical Sciences, University of Aberdeen, Foresterhill, Aberdeen AB25 2ZD United Kingdom and the ^dSchool of Life Sciences, Wellcome Trust Building, University of Dundee, Dundee DD1 4NH, United Kingdom

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 -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 and mnt1 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 mnt1mnt2 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.

Received for publication, October 6, 2004 , and in revised form, November 1, 2004.

^* This work was supported by Grants 063204 and 72263 from the Wellcome Trust. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBank^TM/EBI Data Bank with accession number(s) X89263.

^b The first two authors contributed equally.

^c Present address: AstraZeneca R&D Boston, 35 Gatehouse Drive Waltham, MA 02451.

^e Supported by Grants 62387 and 71463 from the Wellcome Trust.

^f Present address: 6-178 Molecular and Cellular Biology Building, 420 Washington Ave. S.E., University of Minnesota, Minneapolis, MN 55455.

^g Present address: Division of Medical Mycology, Dept. of Microbiology and Immunology, Medical University of South Carolina, Charleston, SC 29403.

^h Present address: Dept. of Medical Microbiology, Polwarth Bldg., University of Aberdeen, AB25 2ZD, UK.

ⁱ To whom correspondence should be addressed. Tel.: 44-1224-555879; Fax.: 44-1224-555844; E-mail: n.gow{at}abdn.ac.uk.

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