Characterization of polyclonal allergen-specific IgE responses by affinity distributions.

Polyclonal IgE responses have been previously characterized by allergen-specific antibody levels and by identification of amino acid sequences related to immunodominant epitopes. However, the binding affinities related to these antibody families are not well known. Using sera from donors with known sensitivities to ragweed or house dust mite allergens, we studied the binding reactions between the purified allergens Amb a 1 and Der p 1 and allergen-specific IgE's by determining affinity distribution functions. The distributions of binding affinities only exhibited a few dominant reactions indicated by peaks in an affinity distribution display. In all the donors tested, there were two dominant peaks and in 2/3 of the cases there was a third peak for both Amb a 1 and Der p 1. We further characterized the polyclonal interactions between IgE and Der p 1 by inhibiting the specific binding of IgE using peptide fragments known to be constituents of Der p 1 epitopes. Each peptide inhibited only a single peak in the affinity distributions. It would appear that the peaks in the affinity distribution represent antibodies directed to single epitopes. These results suggest that in our atopic population the response is surprisingly uniform. The bulk of the IgE response (70-80%) is of high affinity (10(8)-10(11) M(-1)) and directed towards a few epitopes. The relative affinities towards epitopes seem to be determined by the structure of the epitope and not variations of individuals' immune responses.