Characteristics of two CD75-related cell-surface expressed antigens of human lymphocytes.

The structure of cell surface carbohydrates expressed on human leukocytes is dependent on the cell's developmental stage, differentiation, and activation. Although modification of oligosaccharide side chains by sialylation is quite common, antigenic determinants on lymphocytes associated with the presence of sialoglycans are still incompletely defined. In the study presented here, monoclonal antibodies (mAbs) were used to characterize two novel but related cell surface carbohydrate antigens. One antigen, denominated as B8, is largely masked by sialyl residues on most lymphocytes, while it is detectable on the majority of B cells. Treatment with sialidase resulted in the exposure of B8 on the surface of blood cells including lymphocytes. Although the second carbohydrate antigen, C1, was sialidase-sensitive, its molecular properties and cellular distribution place it in close vicinity to B8. B8(+) as well as C1(+) lymphocytes were found predominantly in the mantle zone of secondary follicles of tonsillar tissue. These findings raised the possibility that B8 and C1 are closely related to a category of carbohydrate antigens previously classified as CDw76 (recently assigned to CD75s). MAbs directed against B8 or C1 precipitated 34, 37, 43, and 200kDa glycoproteins from tonsillar lymphocytes, indicating that identical cell surface proteins are associated with both antigens. In contrast to B8, however, the expression of C1 was increased on lymphocytes upon activation. Together the results suggest that CD75-related epitopes are distinct molecular entities which may be exposed on glycoproteins and are differently expressed on lymphocytes.