Mormeneo S, Marcilla A, Iranzo M, Sentandreu R
Departament de Microbiología, Facultat de Farmàcia, Universitat de València, Burjassot, Spain.
FEMS Microbiol Lett. 1994 Oct 15;123(1-2):131-6. doi: 10.1111/j.1574-6968.1994.tb07212.x.
Mild alkaline solutions (beta-elimination), after removing the non-covalently bonded wall materials by hot SDS, released 13% and 26% of remaining wall proteins from mycelial and yeast cells of Candida albicans, respectively. When the beta-elimination was carried out after digestion of the walls with chitinase, four-fold more proteinaceous materials were released from mycelium and a similar amount in yeast walls. The solubilized materials were shown to be highly polydisperse, and endo-glycosidase 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 and 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-glycosylated mannoproteins are interconnected in the walls of C. albicans.
