Characterization of T8 epitopes by enzymatic digestion, crossblocking, and involvement in cell-mediated lympholysis.
Eleven monoclonal antibodies, directed versus the T8 glycoprotein, were compared using enzyme digestion, phylogenetic comparisons, cross-blocking of antibody binding, and blocking of specific cell-mediated lympholysis (CML). It was found that none of the 11 anti-T8 antibodies tested define the same epitope on the T8 glycoprotein. Some of these antibodies react, however, with closely related structures, as shown by cross-blocking of antibody binding and similar enzyme sensitivity of the epitopes. Moreover, these structural related epitopes show a similar involvement in the effector phase of CML reactions, since the antibodies to these neighboring epitopes inhibit the same CML reactions. Thus, it is possible to apply structural and functional criteria to define "regions" on the T8 glycoprotein, some of which are consistently involved in CML reactions, some never, and some of these regions appear to be involved in specific effector-target cell combinations only.
D000818:Animals; D000911:Antibodies, Monoclonal; D000954:Antigens, Surface / Q000276:immunology*; D001667:Binding, Competitive; D003602:Cytotoxicity, Immunologic; D000939:Epitopes; D006801:Humans; D007111:Immunity, Cellular; D008251:Macaca / Q000276:immunology; D010447:Peptide Hydrolases; D013045:Species Specificity; D013329:Structure-Activity Relationship; D013602:T-Lymphocytes, Cytotoxic / Q000276:immunology*
D000911:Antibodies, Monoclonal; D000954:Antigens, Surface; D000939:Epitopes; D010447:Peptide Hydrolases