Autoantibodies of the IgM class against a human myeloma protein IgE(DES). II. Specificity.

Five different monoclonal IgE proteins, papain and pepsin fragments of myeloma protein IgE(DES) and particle-counting immunoassay were used to study in detail the epitope(s) of IgE(DES) involved in the agglutination with IgM anti-IgE(DES) antibodies. The specificity of these autoantibodies was restricted to IgE(DES) as they did not react with latex particles coated with four other IgE myeloma proteins. Antibodies reactive with latex-IgE other than latex-IgE(DES), when present, were also of restricted specificity as shown by criss-cross absorption experiments. These differences between IgE myeloma proteins could not be attributed to the light chain type nor to the Em(1)-allotype. The epitope(s) of IgE(DES) participating in the reaction was heat-resistant (56 degrees C, 2 h) and localized in the pepsin F(ab')2 epsilon fragment, but was absent in the papain Fc epsilon and Fab epsilon fragments. Further degradation by pepsin of the F(ab')2 epsilon fragment (molecular weight 145,000 daltons) to 5S epsilon (90,000 daltons) and Fc" epsilon fragments (30,000 daltons) destroyed the reacting epitope. These results indicate that the IgM antibodies were not directed against kappa chain or idiotypic determinants of IgE(DES), but to some epitope(s) in the undegraded hinge region. Therefore, it seems that some kind of antigenic heterogeneity, perhaps related to the carbohydrate moieties, is present in IgE myeloma proteins besides the known idiotypic, allotypic and isotypic ones.