Eukaryotic Cell
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EC Accepts, published online ahead of print on 12 October 2007
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6/12/2184    most recent
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Eukaryotic Cell doi:10.1128/EC.00350-07
Copyright (c) 2007, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved.

The endoplasmic reticulum {alpha}-glycosidases of Candida albicans are required for N-glycosylation, cell wall integrity and normal host-fungus interaction

Héctor M. Mora-Montes, Steven Bates, Mihai G. Netea, Diana F. Díaz-Jiménez, Everardo López-Romero, Samuel Zinker, Patricia Ponce-Noyola, Bart Jan Kullberg, Alistair J.P. Brown, Frank C. Odds, Arturo Flores-Carreón, and Neil A. R. Gow*

Instituto de Investigación en Biología Experimental, Facultad de Química, Universidad de Guanajuato, Apartado postal 187, Guanajuato, Gto. CP 36000, México. School of Medical Sciences, Institute of Medical Sciences, University of Aberdeen, Foresterhill, Aberdeen AB25 2ZD, United Kingdom. Department of Medicine, Radboud University Nijmegen Medical Center, 6500 HB Nijmegen, The Netherlands. Departamento de Genética y Biología Molecular, CINVESTAV del IPN, Apartado Postal 14-740, México, D.F. 07000, México

* To whom correspondence should be addressed. Email: n.gow{at}abdn.ac.uk.


  Abstract

The cell surface of Candida albicans is enriched in highly glycosylated mannoproteins that are involved in the interaction with the host tissues. N-glycosylation is a post-translational modification that is initiated in the endoplasmic reticulum, where the Glc3Man9GlcNAc2 N-glycan is processed by {alpha}-glucosidases I and II, and {alpha}1,2-mannosidase to generate Man8GlcNAc2. This N-oligosaccharide is then elaborated in the Golgi to form N-glycans with highly branched outer chains rich in mannose. In Saccharomyces cerevisiae, CWH41, ROT2 and MNS1 encode for {alpha}-glucosidase I, {alpha}-glucosidase II catalytic subunit and {alpha}1,2-mannosidase, respectively. We disrupted the C. albicans CWH41, ROT2 and MNS1 homologs to determine the importance of N-oligosaccharide processing on the N-glycan outer chain elongation and the host-fungal interaction. Yeast cells of Cacwh41{Delta}, Carot2{Delta} and Camns1{Delta} null mutants tended to aggregate, displayed reduced growth rates, had a lower content of cell wall phosphomannan and other changes in cell wall composition, underglycosylated {beta}-N-acetylhexosaminidase, and had a constitutively activated PKC-Mkc1 cell wall integrity pathway. They were also attenuated in virulence in a murine model of systemic infection and stimulated an altered pro- and anti-inflammatory cytokines profile from human monocytes. Therefore N-oligosaccharide processing by ER glycosidases is required for cell wall integrity and for host-fungus interactions.






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