FIMBRIA-MEDIATED ADHERENCE OF CANDIDA-ALBICANS TO GLYCOSPHINGOLIPID RECEPTORS ON HUMAN BUCCAL EPITHELIAL-CELLS

Candida albicans is an opportunist fungal pathogen that has the abilit y to adhere to host cell surface receptors via a number of adhesins. Y u et al. (L. Yu, K. K.Lee, K. Fns, p. C. Doig, M. R. Carpenter, W. Sta ddon, R. S. Hedges, W. Paranchych, and R. T. Irvin, Infect. Immun. 62: 2834-2842, 1994) described the purification and initial characterizati on of a fimbrial adhesin from C. albicans. In this paper, we show that C. albicans fimbriae also bind to asialo-GM(1), [gangliotetraosylcera mide: beta Gal(1-3)beta GalNAc(1-4) beta Gal(1-4)beta Glc(1-1)Cer] imm obilized on microtiter plates in a saturable and concentration-depende nt manner. C. albicans fimbrial binding to exfoliated human buccal epi thelial cells (BECs) was inhibited by asialo-GM(1) in in vitro binding assays. The fimbriae interact with the glycosphingolipid receptors vi a the carbohydrate portion of the receptors, since fimbriae were obser ved to bind to synthetic beta GalNAc(1-4)beta Gal-protein conjugates a nd the disaccharide was able to inhibit binding of fimbriae to BECs in in vitro binding assays. We conclude from these results that the C. a lbicans yeast form expresses a fimbrial adhesin that binds to glycosph ingolipids displayed on the surface of human BECs.