Role of nominal antigen and Ia antigen in the binding of antigen-specific T lymphocytes to macrophages.
We have previously demonstrated that when primed T lymphocytes were repeatedly incubated on monolayers of antigen-pulsed macrophages (M phi), the cells that failed to adhere to the monolayer demonstrated a marked depletion of their proliferative response that was specific both for the antigen used for pulsing the M phi and for Ia determinants on the M phi. In order to further analyze the contribution of the nominal antigen and Ia antigens to the physical binding of T lymphocytes to M phi, we have attempted to block the absorption of T lymphocytes to M phi with a large excess of soluble antigen and with anti-Ia sera. Our results demonstrate that anti-Ia sera inhibit but that soluble antigen augments the binding of specific T lymphocytes to M phi. The implications of these findings for "dual recognition" and "linked recognition" models of T lymphocyte receptors are discussed.
D000818:Animals; D000937:Antigen-Antibody Reactions; D000941:Antigens; D001665:Binding Sites; D004136:Dinitrobenzenes / Q000276:immunology; D000939:Epitopes; D006168:Guinea Pigs; D006649:Histocompatibility Antigens; D008264:Macrophages / Q000276:immunology*; D010047:Ovalbumin / Q000276:immunology; D013601:T-Lymphocytes / Q000276:immunology*; D014301:Trinitrobenzenes / Q000276:immunology; D014373:Tuberculin / Q000276:immunology
D000941:Antigens; D004136:Dinitrobenzenes; D000939:Epitopes; D006649:Histocompatibility Antigens; D014301:Trinitrobenzenes; D014373:Tuberculin; D010047:Ovalbumin