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[The high-affinity IgE receptor: lessons from structural analysis].

Ulrich Blank·Marie-Hélène Jouvin·Claudine Guérin-Marchand·Jean-Pierre Kinet
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Abstract

The high affinity receptor for IgE, FcERI, is at the core of the allergic reaction. This receptor is expressed mainly on mast cells and basophils. Interaction of an allergen with its specific IgE bound to FcERI triggers cell activation, which induces the release of numerous mediators that are responsible for allergic manifestations. The recent increase in the prevalence of allergic diseases in developed countries has resulted in renewed efforts towards the development of new drugs. One of these is a humanised antibody directed against the IgE ligand. This antibody recognises specifically free but not FcERI-bound IgE thus preventing ligand binding and subsequent cell activation. This antibody has shown some efficacy in clinical trials involving patients with asthma and allergic rhinitis. The recent elucidation of the tridimensional structure of the complex between IgE and FcERI provides unexpected information regarding the mechanism of assembly of the complex, which now can be used to design small chemical compounds capable of specifically inhibiting this interaction.

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Amino Acid MotifsAnimalsAnti-Allergic AgentsAntibodies, Anti-IdiotypicAsthmaBasophilsClinical Trials as TopicDrug DesignHumansHypersensitivityImmunoglobulin EMacromolecular SubstancesMast CellsModels, MolecularProtein BindingProtein ConformationProtein Structure, TertiaryReceptors, IgEReceptors, IgGStructure-Activity RelationshipComparative StudyEnglish AbstractJournal ArticleReview

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Ulrich Blank, Marie-Hélène Jouvin, Claudine Guérin-Marchand, Jean-Pierre Kinet. 2003. [The high-affinity IgE receptor: lessons from structural analysis].. https://doi.org/10.1051/medsci%2F200319163

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