The cell wall architecture of Candida albicans wild-type cells and cell wall-defective mutants

Mol Microbiol. 2000 Feb;35(3):601-11. doi: 10.1046/j.1365-2958.2000.01729.x.


In Candida albicans wild-type cells, the beta1, 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 beta1,6-glucan to beta1,3-glucan. The remaining GPI-CWPs are linked through beta1,6-glucan to chitin. The beta1,6-glucanase-resistant protein fraction is small and consists of Pir-related CWPs, which are attached to beta1,3-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 mnn9Delta and pmt1Delta 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 beta1,6-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 beta1, 6-glucan-deficient hemizygous kre6Delta 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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Aminoglycosides*
  • Anti-Bacterial Agents / pharmacology
  • Antifungal Agents / pharmacology
  • Candida albicans / cytology*
  • Candida albicans / drug effects
  • Candida albicans / genetics*
  • Cell Wall / chemistry
  • Cell Wall / genetics
  • Cell Wall / metabolism
  • Chitin / chemistry
  • Chitin / metabolism
  • Fungal Proteins / genetics
  • Fungal Proteins / metabolism*
  • Glucans / chemistry
  • Glucans / metabolism
  • Glycosylphosphatidylinositols / chemistry
  • Glycosylphosphatidylinositols / metabolism
  • Membrane Proteins / genetics
  • Membrane Proteins / metabolism*
  • Mutation*
  • Saccharomyces cerevisiae Proteins*
  • beta-Glucans*


  • ALS1 protein, Candida albicans
  • ALS3 protein, Candida albicans
  • Aminoglycosides
  • Anti-Bacterial Agents
  • Antifungal Agents
  • Fungal Proteins
  • Glucans
  • Glycosylphosphatidylinositols
  • KRE6 protein, S cerevisiae
  • Membrane Proteins
  • Saccharomyces cerevisiae Proteins
  • beta-Glucans
  • Chitin
  • beta-1,6-glucan
  • nikkomycin