A monoclonal antibody to a cell wall component of Candida albicans.

A heterologous fusion between mouse myeloma cells and rat lymphocytes resulted in the isolation of a rat immunoglobulin M monoclonal antibody with both agglutinating and precipitating activity. Indirect immunofluorescence and direct agglutination tests showed that the corresponding antigen was present in the cell wall of the three Candida species considered to be the most pathogenic, C. albicans, C. tropicalis, and C. glabrata, and also in the cell wall of C. guilliermondii. The antigen appeared to be predominantly polysaccharide in nature. Precipitation by counterimmunoelectrophoresis suggested that the epitope is shared by at least two separate molecules with different electrophoretic mobilities. Presence of this epitope varied from strain to strain within a given species and may be related to the morphological stage in the cell cycle. Antigen was shown to be present in the cytoplasm, in the periplasmic space, and at the cell surface of C. albicans. Indirect immunofluorescence also suggested that antigen is excreted from the cell.