Inhibition of IgE-receptor interactions

Immunoglobulin E plays a central role in allergic disease and, as our understanding of the network of interactions between IgE and its receptors improves, new opportunities for therapeutic intervention emerge. IgE binding to its 'high-affinity' receptor, Fc epsilon RI, first identified on mast cells and now known to be expressed on a variety of other cell types, is the best characterised interaction, and has attracted most attention. The 'low affinity' receptor, Fc epsilon RII/CD23, first found on B-cells, appears to be part of a more complex network that has yet to be fully elucidated. Two recent advances concerning the IgE-Fc epsilon RI interaction are noteworthy. The first is the development of a monoclonal anti-IgE antibody, now in advanced clinical trials, which inhibits this interaction and certainly proves the viability of this approach. The second is the publication of the crystal structure of the complex between IgE and Fc epsilon RI, which opens the way for the first structure-based design of small molecule inhibitors.