Antigen specificity and cross-reactivity of monoclonal anti-lysozyme antibodies.

Twenty-seven murine monoclonal anti-hen egg-white lysozyme (HEL) antibodies were tested with a panel of nine antigens; eight avian lysozymes and human lysozyme. The antibodies were arranged into 10 groups based on their antigen specificity and cross-reactivity. Antigenic determinants recognized by each group of antibodies were tentatively identified. They are located at different points of the HEL accessible surface in agreement with the notion that its entire surface has an antigenic potential. The affinity constants of antibodies representative of seven of the 10 groups range from 0.79 X 10(7) to 5.3 X 10(7) M-1. Heteroclitic antibodies occurring in some of the groups bind heterologous lysozymes with somewhat higher association constants than those for the homologous antigen (HEL). Their broader specificities do not correlate with overall lower association constants, but rather with the occurrence of public epitopes in the panel of avian lysozymes. Although the reaction of two antibodies with the solid-phase coupled antigen is not always additive, detailed interpretation of these results and the observation of actual ternary complexes Fab-HEL-Fab rules out the occurrence of conformational changes in the complexed antigen.