Wall mannoproteins of the yeast and mycelial cells of Candida albicans: nature of the glycosidic bonds and polydispersity of their mannan moieties

J Gen Microbiol. 1988 Aug;134(8):2393-403. doi: 10.1099/00221287-134-8-2393.


Zymolyase released between 20 and 25% of the total protein from purified walls of yeast (Y) and mycelial (M) cells of Candida albicans. The material released contained 92% carbohydrate (86% mannose and 6% glucose) and 7% protein. Over 85% of the carbohydrate was N-glycosidically linked to the protein and the rest (less than 15%) was linked O-glycosidically. Highly polydisperse, high molecular mass mannoproteins, resolved by electrophoresis as four defined bands in Y cells and two bands in M cells, had both types of sugar chains. A 34 kDa species found in both types of cells had a single 2.5 kDa N-glycosidically linked sugar chain and a 31.5 kDa protein moiety. Polydispersity in the high molecular mass mannoproteins was due to the N-linked sugar chains (mannan) with a molecular mass between 500 kDa and 20 kDa (average 100 kDa) in Y cells and between 400 kDa and 20 kDa (average 50 kDa) in M cells. Three mannoproteins of 34, 30 and 29 kDa secreted by protoplasts were associated with the high molecular mass mannoproteins, suggesting that this type of interaction might be related to the regeneration of the cell wall.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Candida albicans / cytology*
  • Candida albicans / metabolism
  • Cell Wall / metabolism
  • Chromatography, Gel
  • Fungal Proteins / metabolism*
  • Glycosides / metabolism
  • Hydrolases / metabolism
  • Mannans / metabolism
  • Membrane Glycoproteins / metabolism*
  • Protoplasts / metabolism


  • Fungal Proteins
  • Glycosides
  • Mannans
  • Membrane Glycoproteins
  • mannoproteins
  • zymolyase
  • Hydrolases