Changes in the cell surface of the dimorphic forms of Candida albicans by treatment with hydrolytic enzymes

The release of acid phosphatase and polysaccharide-peptide complexes by hydrolytic enzymes from the surface of the blastospore and mycelial forms of Candida albicans has been examined in cells from 4 h and 18 h cultures and the results correlated with the appearance of the treated cells in the electron microscope. Treatment with dithiothreitol was necessary for the degradative action of the enzymes to occur. Material released by all the treatments used had a similar qualitative composition, but the proportions of mannan, glucan, peptide and acid phosphatase varied with different treatments and with the type of cell examined. I,3-beta-Glucanase was required for major changes in the cell wall to be effected, but a significant amount of material was released with a chitinase preparation containing some protease activity. Protoplasts were obtained from all types of cell using Cytophaga lytic enzyme L1 which had I,3-beta-glucanase and protease activity, but the purified I,3-beta-glucanase and protease prepared from Streptomyces violaceus cultures required the presence of a chitinase before protoplasts were released. The bonding association between the major components which comprise the cell wall, and the spatial distribution of these macromolecules, varies appreciably between the two dimorphic forms and with the age of the culture.