Binding of a monoclonal antibody, mAb293, to cell-surface glycoproteins of Polysphondylium pallidum is known to be blocked by L-fucose, and Fab of this antibody has been shown to inhibit intercellular adhesion of aggregation-competent cells. Mutants with delayed expression of the carbohydrate epitope, ep293, recognized by the antibody, have been shown to be retarded and altered in cell aggregation. The present study shows that ep293 is a modification of carbohydrate structure that is subject to regulation not only in mutant but also in wild-type cells; ep293 is expressed at an early stage of exponential growth in wild-type and only after 12 h of starvation in mutant PN6002. Proteins are already glycosylated before the epitope is expressed. The developmental regulation of pallidin, a lectin known to be an unglycosylated protein, was investigated in parallel with ep293 using a monoclonal antibody. Pallidin was expressed at about the same time as the carbohydrate epitope in cells of the wild-type as well as the mutant. These results indicate a regulatory signal to which various events are coupled. Induction of ep293 and expression of pallidin are two of these events, and mutants such as PN6002 are altered in the timing of the signal.

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