Beta-1,2-linked oligomannosides inhibit Candida albicans binding to murine macrophage

• Published in: Journal of leukocyte biology Vol. 60; no. 1; pp. 81 - 87
• Main Authors: Fradin, Chantal, Jouault, Thierry, Mallet, Astrid, Mallet, Jean‐Maurice, Camus, Daniel, Sinaÿ, Pierre, Poulain, Daniel
• Format: Journal Article
• Language: English
• Published: United States Society for Leukocyte Biology 01.07.1996
• Subjects: Animals; Candida albicans; Candida albicans - drug effects; Candida albicans - physiology; Carbohydrate Conformation; Carbohydrate Sequence; Hot Temperature; interaction; Macrophages - drug effects; Macrophages - physiology; Mannans - pharmacology; Mice; Molecular Sequence Data; Oligosaccharides - pharmacology; Phagocytosis - drug effects; Phosphopeptides - pharmacology; receptors; Saccharomyces cerevisiae; yeast
• ISSN: 0741-5400; 1938-3673
• 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 β‐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 β‐1,2‐oligomannosides was examined with regard to their exclusive presence within C. albicans PPM. PPM acid labile β‐1,2‐oligomannosides or a synthetic β‐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 β‐1,2‐oligomannosides in the adherence of the yeast to the macrophage membrane.