COMPLEX INTERACTION BETWEEN DIFFERENT PROTEINACEOUS COMPONENTS WITHINTHE CELL-WALL STRUCTURE OF CANDIDA-ALBICANS

We have previously described a monoclonal antibody, MAb DC3:H10, which recognized an epitope preferentially expressed on the surface of Cand ida albicans germ tubes. In the present study we examined the MAb-reac tive material further. Immunoblot analysis of the material purified pa rtially by Sephadex G-200 and DEAE-Sephacel chromatography reacted wit h antibodies to the C. albicans C3d receptor (CR2). In an ELISA, MAb D C3:H10 captured antigen that was recognized by both anti-CR2 and anti- mp58 fibrinogen binding mannoprotein polyclonal antibodies. The MAb DC 3:H10 failed to compete with either of these antisera in an ELISA. Ind irect immunofluorescence (IIF) analysis showed differences in surface distribution for the MAb DC3:H10, the CR2, and the mp 58 epitopes. Dua l labeling IIF experiments showed MAb DC3:H10 binding to be unaffected by binding of fibrinogen or anti-mp58 antibody. However, the binding patterns of MAb DC3:H10 were modified in the presence of anti-CR2 anti body, suggesting a complex interaction between these cell wall compone nts.