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*
Institute of Immunology and Allergology, University of Bern, Inselspital, Bern, Switzerland; and
Novartis Forschungsinstitut, Vienna, Austria
We have previously described a mouse monoclonal
anti-human IgE antibody (BSW17) capable of recognizing
receptor-bound IgE without inducing mediator release from human
basophils or mast cells. Moreover, immune complexes of IgE and BSW17
are not able to bind to the IgE receptor. An initial attempt to map the
precise epitope recognized by this mAb by using Fc
-derived peptides
of variable length was unsuccessful. However, by screening random
peptide phage display libraries we isolated circular nona- and
octapeptides specifically recognized by BSW17. These constrained
peptides mimic at least a part of a conformational epitope and are thus
called mimotopes. These mimotopes, either phage displayed or
synthetically synthesized, did not react with any other anti-human
IgE antibody tested, but efficiently inhibited the binding of human IgE
to BSW17 only. The use of Rhodol-Green-labeled free cyclic peptide
proved that these interactions were not carrier dependent. Immunization
of rabbits with phage clones displaying the specific peptides on the
surface induced an anti-human IgE response specific for the epitope
of BSW17. Therefore, we conclude that such mimotopes or
mimotope-derived peptides might be used for vaccination to induce in
vivo a beneficial anti-IgE response as a novel immunotherapy.
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