Inhibition of IgE-receptor interactions

Immunoglobulin E plays a central role in allergic disease and, as our under standing of the network of interactions between IgE and its receptors impro ves, 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 bes t characterised interaction, and has attracted most attention. The 'low aff inity' 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 re cent advances concerning the IgE-Fc epsilon RI interaction are noteworthy. The first is the development of a monoclonal anti-IgE antibody, now in adva nced clinical trials, which inhibits this interaction and certainly proves the viability of this approach. The second is the publication of the crysta l structure of the complex between IgE and FceRI, which opens the way for t he first structure-based design of small molecule inhibitors.