Beta-1,2-linked Oligomannosides Inhibit Candida Albicans Binding to Murine Macrophage

J Leukoc Biol. 1996 Jul;60(1):81-7. doi: 10.1002/jlb.60.1.81.


Interaction of Candida albicans with cells of the macrophage lineage was examined by using heat-killed (HK) and live yeast cells. Laminarin, an analogue of the cell wall beta-glucans, strongly inhibited HK yeasts adherence to J774 cell line but had no effect on live yeast binding. Phosphopeptidomannan (PPM) from Saccharomyces cerevisiae had a limited effect on the binding of both HK and live yeasts but significant inhibition was achieved by the use of C. albicans PPM. The role of beta-1,2-oligomannosides was examined with regard to their exclusive presence within C. albicans PPM. PPM acid labile beta-1,2-oligomannosides or a synthetic beta-1,2-mannotetraose, inhibited yeasts binding in a manner comparable to the original PPM. These latter results were confirmed by using mouse peritoneal macrophages, thus suggesting a general role for beta-1,2-oligomannosides in the adherence of the yeast to the macrophage membrane.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Candida albicans / drug effects
  • Candida albicans / physiology*
  • Carbohydrate Conformation
  • Carbohydrate Sequence
  • Hot Temperature
  • Macrophages / drug effects
  • Macrophages / physiology*
  • Mannans / pharmacology
  • Mice
  • Molecular Sequence Data
  • Oligosaccharides / pharmacology*
  • Phagocytosis / drug effects*
  • Phosphopeptides / pharmacology
  • Saccharomyces cerevisiae


  • Mannans
  • Oligosaccharides
  • Phosphopeptides
  • oligomannoside
  • phosphopeptidomannan