Polyclonal antibodies (pAbs) and monoclonal antibodies (mAbs), raised against mannoprotein components from ATCC 26555 (serotype A) blastoconidia and mycelial cell walls, were used to investigate antigenic similarities among wall mannoproteins from other serotype A and B strains, and from and . Radioactively labelled walls isolated from cells grown at either 28 °C or 37 °C were digested with a β-glucanase complex (Zymolyase 20T) to release cell-wall-bound mannoproteins. Numerous molecular species with different electrophoretic mobilities were released from the various isolates. Differences appeared to be related to both the organism and the growth temperature. Among the major protein components solubilized were mannoproteins larger than 100 kDa (high molecular mass mannoproteins), heterogeneous in size in most cases. Antigenic homology was detected among the cell wall high molecular mass mannoproteins of the two serotype A isolates, whereas significant qualitative and quantitative differences were detected between serotype A and serotype B cell-wall-bound antigenic profiles. Moreover, and wall antigenic determinants were not recognized by the preparations of pAbs and mAbs raised against walls. A mannoprotein with a molecular mass of 33-34 kDa was present in the enzymic wall digests of all the organisms studied. When probed with pAbs raised against the protein moiety of the 33 kDa cell wall mannoprotein of , antigenic cross-reactivity was observed in all cases except . There appear to be significant antigenic differences between the mannoproteins of different isolates of , and between those of and other species.


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