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British Medical Bulletin 56:1004-1018 (2000)
© 2000 The British Council

research-article

Inhibition of lgE-receptor interactions

Brain J Sutton, Rebecca L Beavil and Andrew J Beavil

The Randall Centre for Molecular Mechanisms of Cell Function, King's College London London, UK

Correspondence to:Dr Brain J Sutton, The Raindall Centre for Molecular Mechanisms of Cell function, King's College London, New Hunt's House, Guy's Hospital Campus, London Bridge, London Se1 1UL UK

Abstract

Immunoglobulin E plays a central role in allergic disease and, as our undrestanding of the network of interactions between lgE and its receptors impproves, new opportunities for therapeutic intervention emerge. lgE binding to its ‘high-affinity’ receptor, FCRI, 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{varepsilon}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-FCRI interaction are noteworthy. The first is the development of a monoiclonal anti-lgE antibody, now in advanced clinical trials, which minhibits this interaction and certainly proves the viability of this approach. The second is the publication of the crystal structure of the complex between lgE and FC{varepsilon}RI, which opens the way for the first structure-based design of small molecule inhibitors.


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