The high-affinity receptor for IgE (FcεRI) on mast cells and basophils is a tetrameric complex, aßƔ2. Here we summarize the latest developments on the structure and function of this receptor. By genetic transfer, we have engineered a cell line secreting substantial amounts of a peptide containing exclusively the extracellular domain of the α-subunit. This domain by itself is sufficient to mediate high-affinity binding of IgE. Glycosylation and the presence of the other subunits are not necessary for the binding function. The Ɣ-subunit of FcεRI is part of other receptors such as FcˠRIII and the T cell receptor, and therefore is likely to play an important although still undefined functional role. A detailed knowledge of how the receptor interacts with IgE and induces cellular degranulation may lead to the design of new therapeutic approaches to allergic diseases. The potential strategies are discussed.
ASJC Scopus subject areas
- Immunology and Allergy