The cell wall architecture of Candida albicans wild-type cells and cell wall-defective mutants
Article first published online: 5 APR 2002
Volume 35, Issue 3, pages 601–611, February 2000
How to Cite
Kapteyn, J. C., Hoyer, L. L., Hecht, J. E., Müller, W. H., Andel, A., Verkleij, A. J., Makarow, M., Van Den Ende, H. and Klis, F. M. (2000), The cell wall architecture of Candida albicans wild-type cells and cell wall-defective mutants. Molecular Microbiology, 35: 601–611. doi: 10.1046/j.1365-2958.2000.01729.x
- Issue published online: 5 APR 2002
- Article first published online: 5 APR 2002
In Candida albicans wild-type cells, the β1,6-glucanase-extractable glycosylphosphatidylinositol (GPI)-dependent cell wall proteins (CWPs) account for about 88% of all covalently linked CWPs. Approximately 90% of these GPI-CWPs, including Als1p and Als3p, are attached via β1,6-glucan to β1,3-glucan. The remaining GPI-CWPs are linked through β1,6-glucan to chitin. The β1,6-glucanase-resistant protein fraction is small and consists of Pir-related CWPs, which are attached to β1,3-glucan through an alkali-labile linkage. Immunogold labelling and Western analysis, using an antiserum directed against Saccharomyces cerevisiae Pir2p/Hsp150, point to the localization of at least two differentially expressed Pir2 homologues in the cell wall of C. albicans. In mnn9Δ and pmt1Δ mutant strains, which are defective in N- and O-glycosylation of proteins respectively, we observed enhanced chitin levels together with an increased coupling of GPI-CWPs through β1,6-glucan to chitin. In these cells, the level of Pir-CWPs was slightly upregulated. A slightly increased incorporation of Pir proteins was also observed in a β1,6-glucan-deficient hemizygous kre6Δ mutant. Taken together, these observations show that C. albicans follows the same basic rules as S. cerevisiae in constructing a cell wall and indicate that a cell wall salvage mechanism is activated when Candida cells are confronted with cell wall weakening.