Epitope and functional specificity of monoclonal antibodies to mouse interferon-gamma: the synthetic peptide approach.

摘要: Spleen cells from hamsters immunized with recombinant mouse interferon-gamma (IFN-gamma) were fused myeloma cells, resulting in the production of four anti-IFN-gamma monoclonal antibodies. Binding 125I-IFN-gamma by these protein A-bound antibodies was specifically blocked cold IFN-gamma. three also a synthetic peptide corresponding to N-terminal 1-39 amino acids IFN-gamma, whereas C-terminal (95-133) had no effect on binding. The specificity confirmed their specific binding 125I-N-terminal (1-39) peptide. One inhibited both antiviral and macrophage priming (for tumor cell killing) activities other two either biologic function. selectivity inhibition IFN-gamma function not due differential ability bind Blocking experiments suggest that epitope specificities could be determined conformational or topographic structure An exact determination antibody provide insight into structural basis for role domain Polyclonal peptides macrophage-priming All membrane receptor did block inhibit data domains play an important its functions, possibly cooperative manner.