Preparation of monoclonal antibodies reactive with beta-1,2-linked oligomannosyl residues in the phosphomannan-protein complex of Candida albicans NIH B-792 strain.

Hybridomas obtained by fusing the spleen cells of BALB/c female mice hyperimmunized with heat-killed yeast-form cells of Candida albicans NIH B-792 strain and a mouse myeloma cell line, P3X63Ag8.653, produced antibodies to beta-1,2-linked oligomannosyl residues in the phosphomannan-protein complex of the parent cells. Most of these monoclonal antibodies were IgM, but about 10% of the hybridomas produced IgG1 immunoglobulins. Ascites fluid from BALB/c mice inoculated with an IgG1-producing hybridoma showed different precipitability with the phosphomannan-protein complexes of three representative C. albicans strains, with NIH B-792 (serotype B) greater than NIH A-207 (serotype A) greater than J-1012 (serotype A, formerly serotype C). In contrast, a rabbit polyclonal antiserum to C. albicans NIH B-792 cells was unable to distinguish these same complexes. This ascites fluid agglutinated the heat-killed cells of three Candida strains, but not those of three others or of Torulopsis glabrata IFO 0622. The other ascites fluids, containing antibodies of the IgM class, agglutinated cells from three C. albicans strains and also C. tropicalis IFO 0587 cells.