Glucosylation of cell wall proteins in regenerating spheroplasts of Candida albicans

FEMS Microbiol Lett. 1995 May 15;128(3):271-7. doi: 10.1111/j.1574-6968.1995.tb07535.x.


The cell wall of Candida albicans contains mannoproteins that are covalently associated with beta-1,6-glucan. When spheroplasts were allowed to regenerate a new cell wall, initially non-glucosylated cell wall proteins accumulated in the medium. While the spheroplasts became osmotically stable, beta-1,6-glucosylated proteins could be identified in their cell wall by SDS-extraction or beta-1,3-glucanase digestion. At later stages of regeneration, beta-1,3-glucosylated proteins were also found. Hence, incorporation of proteins into the cell wall is accompanied by extracellular coupling to beta-1,6-/beta-1,3-glucan. The SDS-extractable glucosylated proteins probably represent degradation products of wall proteins rather than their precursors. Tunicamycin delayed, but did not prevent the formation of beta-1,6-glucosylated proteins, demonstrating that beta-1,6-glucan is not attached to N-glycosidic side-chains of wall proteins.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Candida albicans / growth & development
  • Candida albicans / immunology
  • Candida albicans / metabolism*
  • Cell Compartmentation
  • Cell Wall / immunology
  • Cell Wall / metabolism*
  • Fungal Proteins / biosynthesis*
  • Glucans / biosynthesis
  • Glucose / metabolism*
  • Glycoproteins / biosynthesis*
  • Glycosylation
  • Protein Processing, Post-Translational
  • Spheroplasts / growth & development
  • Spheroplasts / immunology
  • Spheroplasts / metabolism
  • beta-Glucans*


  • Fungal Proteins
  • Glucans
  • Glycoproteins
  • beta-Glucans
  • beta-1,6-glucan
  • Glucose