STRUCTURAL MANNOPROTEINS RELEASED BY BETA-ELIMINATION FROM CANDIDA-ALBICANS CELL-WALLS

Mild alkaline solutions (beta-elimination), after removing the non-cov alently bonded wall materials by hot SDS, released 13% and 26% of rema ining wall proteins from mycelial and yeast cells of Candida albicans, respectively. When the p-elimination was carried out after digestion of the walls with chitinase, four-fold more proteinaceous materials we re released from mycelium and a similar amount in yeast walls. The sol ubilized materials were shown to be highly polydisperse, and endo-glyc osidase H reduced their polydispersity and molecular masses, revealing different electrophoretic patterns in yeast and mycelial cell walls. The solubilized mycelial proteins carried N-glycosidic sugar chains an d the epitopes recognized by two monoclonal antibodies were preserved, although showing a different behaviour in yeast walls. These results are consistent with the idea that significant amounts of intrinsic O-g lycosylated mannoproteins are interconnected in the walls of C. albica ns.