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β‐1,2‐linked oligomannosides Inhibit Candida albicans binding to murine macrophage
Author(s) -
Fradin Chantal,
Jouault Thierry,
Mallet Astrid,
Mallet JeanMaurice,
Camus Daniel,
Sinaÿ Pierre,
Poulain Daniel
Publication year - 1996
Publication title -
journal of leukocyte biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.819
H-Index - 191
eISSN - 1938-3673
pISSN - 0741-5400
DOI - 10.1002/jlb.60.1.81
Subject(s) - candida albicans , yeast , laminarin , biology , corpus albicans , macrophage , saccharomyces cerevisiae , microbiology and biotechnology , biochemistry , in vitro , polysaccharide
Abstract 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.