Antigen recognition and antibody specificity. Carrier specificity and genetic control of anti-dinitrophenyl-oligolysine antibody.
The exact specifiicity of anti-DNP antibody produced by Hartley guinea pigs immunized with a series of defined alpha,DNP and epsilon,DNP-oligolysines was studied by fluorescence quenching. All responder animals made anti-DNP antibody which recognized the precise chain length, +/- 1 lysyl residue, of the DNP-oligolysines used to induce the immune response as measured by an increase in binding energy (-DeltaF degrees ) for that antigen. The ability of the immune system to detect the smallest possible change in oligolysine chain length suggests that the anti-hapten antibody-forming cell possesses a highly specific recognition system for carrier conformation. When DNP-oligolysines are incorporated in an adjuvant containing M. tuberculosis H37Rv, both responder and nonresponder produce anti-DNP antibody, but only the responder develops delayed skin sensitivity. In addition to their failure to develop delayed hypersensitivity, nonresponders produced anti-DNP oligolysine antibody which did not show the increase in -DeltaF degrees for the immunizing antigen characteristic of responder antibody. These observations support a local environment hypothesis for antigen recognition at the level of the anti-hapten antibody-forming cell and suggest that the polylysine gene exerts its control at the same cell.
D000818:Animals; D000906:Antibodies; D000917:Antibody Formation; D000918:Antibody Specificity; D000941:Antigens; D004140:Dinitrophenols; D005453:Fluorescence; D005799:Genes, Dominant; D006168:Guinea Pigs; D007125:Immunogenetics; D008239:Lysine; D010455:Peptides; D011233:Precipitin Tests; D013053:Spectrophotometry
D000906:Antibodies; D000941:Antigens; D004140:Dinitrophenols; D010455:Peptides; D008239:Lysine