COVALENT ASSOCIATION OF BETA-1,3-GLUCAN WITH BETA-1,6-GLUCOSYLATED MANNOPROTEINS IN CELL-WALLS OF CANDIDA-ALBICANS

Yeast and hyphal walls of Candida albicans were extracted with sodium dodecyl sulfate (SDS). Some of the extracted proteins reacted with a s pecific beta-1,6-glucan antiserum but not with a beta-1,3-glucan antis erum. They lost their beta-1,6-glucan epitope after treatment with ice -cold aqueous hydrofluoric acid, suggesting that beta-1,6-glucan was l inked to the protein through a phosphodiester bridge. When yeast and h yphal walls extracted with SDS were subsequently extracted with a pure beta-1,3-glucanase, several mannoproteins that were recognized by bot h the beta-1,6-glucan antiserum and the beta-1,3-glucan antiserum were released. Both epitopes were sensitive to aqueous hydrofluoric acid t reatment, suggesting that beta-1,3-glucan and beta-1,6-glucan are link ed to proteins by phosphodiester linkages. The possible role of beta-g lucans in the retention of cell wall proteins is discussed.