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Membrane IgE Binds and Activates FcRI in an Antigen-Independent Manner¹

Luca Vangelista^2,*,, Elisa Soprana, Michela Cesco-Gaspere, Paola Mandiola, Giulia Di Lullo^*,, Rita N. Fucci^*,, Franca Codazzi, Alessio Palini, Giovanni Paganelli, Oscar R. Burrone and Antonio G. Siccardi^*,

^* Department of Biology and Genetics, University of Milan, Milan, Italy; San Raffaele Scientific Institute, Milan, Italy; International Centre for Genetic Engineering and Biotechnology, Trieste, Italy; and European Institute of Oncology, Milan, Italy

Interaction of secretory IgE with FcRI is the prerequisite for allergen-driven cellular responses, fundamental events in immediate and chronic allergic manifestations. Previous studies reported the binding of soluble FcRI to membrane IgE exposed on B cells. In this study, the functional interaction between human membrane IgE and human FcRI is presented. Four different IgE versions were expressed in mouse B cell lines, namely: a truncation at the C2-C3 junction of membrane IgE isoform long, membrane IgE isoform long (without Ig/Ig BCR accessory proteins), and both BCRs (containing membrane IgE isoforms short and long). All membrane IgE versions activated a rat basophilic leukemia cell line transfected with human FcRI, as detected by measuring the release of both preformed and newly synthesized mediators. The interaction led also to Ca²⁺ responses in the basophil cell line, while membrane IgE-FcRI complexes were detected by immunoprecipitation. FcRI activation by membrane IgE occurs in an Ag-independent manner. Noteworthily, human peripheral blood basophils and monocytes also were activated upon contact with cells bearing membrane IgE. In humans, the presence of FcRI in several cellular entities suggests a possible membrane IgE-FcRI-driven cell-cell dialogue, with likely implications for IgE homeostasis in physiology and pathology.

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