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Infection and Immunity, November 2004, p. 6230-6236, Vol. 72, No. 11
0019-9567/04/$08.00+0 DOI: 10.1128/IAI.72.11.6230-6236.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.
Departments of Pathology,1 Microbiology, University of Virginia Health System, Charlottesville, Virginia2
Received 22 April 2004/ Returned for modification 20 May 2004/ Accepted 26 July 2004
Cell surface hydrophobicity contributes to the pathogenesis of the opportunistic fungal pathogen Candida albicans. Previous work demonstrated a correlation between hydrophobicity status and changes in the acid-labile, phosphodiester-linked ß-1,2-oligomannoside components of the N-linked glycans of cell wall mannoprotein. Glycan composition also defines the two major serotypes, A and B, of C. albicans strains. Here, we show that the cell surface hydrophobicity of the two serotypes is qualitatively different, suggesting that the serotypes may differ in how they modulate cell surface hydrophobicity status. The cell wall mannoproteins from hydrophilic and hydrophobic cells of both serotypes were compared to determine whether the glycan differences due to serotype affect the glycan differences due to hydrophobicity status. Composition analysis showed that the protein, hexose, and phosphate contents of the mannoprotein fraction did not differ significantly among the strains tested. Electrophoretic profiles of the acid-labile mannan differed only with hydrophobicity status, not serotype, though some strain-specific differences were observed. Furthermore, a newly available ß-1,2-oligomannoside ladder allowed unambiguous identification of acid-labile mannan components. Finally, to assess whether the acid-stable mannan also affects cell surface hydrophobicity status, this fraction was fragmented into its component branches by acetolysis. The electrophoretic profiles of the acid-stable branches were very similar regardless of hydrophobicity status. However, differences were observed between serotypes. These results support and extend our current model that modification of the acid-labile ß-1,2-oligomannoside chain length but not modification of the acid-stable region is one common mechanism by which switching of cell surface hydrophobicity status of C. albicans strains occurs.
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