Cell wall mannan and cell surface hydrophobicity in Candida albicans serotype A and B strains.
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 beta-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 beta-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 beta-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.
Masuoka
James
J
Department of Pathology, University of Virginia Health System, Charlottesville 22908-0904, USA. jm2n@virginia.edu
Hazen
Kevin C
KC
D002176:Candida albicans / Q000145:classification* / Q000254:growth & development / Q000472:pathogenicity; D002462:Cell Membrane / Q000502:physiology*; D002473:Cell Wall / Q000737:chemistry* / Q000378:metabolism; D005656:Fungal Proteins; D015966:Gene Expression Regulation, Fungal; D006031:Glycosylation; D006863:Hydrogen-Ion Concentration; D057927:Hydrophobic and Hydrophilic Interactions; D008351:Mannans / Q000737:chemistry* / Q000378:metabolism; D008562:Membrane Glycoproteins / Q000737:chemistry; D012703:Serotyping
D005656:Fungal Proteins; D008351:Mannans; D008562:Membrane Glycoproteins; C025363:mannoproteins