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Protein Engineering, Vol. 15, No. 1, 51-57, January 2002
© 2002 Oxford University Press

A minimal receptor-Ig chimera of human Fc{varepsilon}RI {alpha}-chain efficiently binds secretory and membrane IgE

Luca Vangelista, Michela Cesco-Gaspere, Roberto Lorenzi,1 and Oscar Burrone,2

Molecular Immunology, International Centre for Genetic Engineering and Biotechnology, Area Science Park, Padriciano 99, 34012 Trieste, Italy

We constructed a soluble minimal receptor-Ig chimera in which the two extracellular domains of human Fc{varepsilon}RI {alpha}-chain (D1 and D2) were fused to the dimerizing C-terminal domain of human IgG1 heavy chain ({gamma}1-CH3). The protein was expressed and actively secreted by Chinese hamster ovary (CHO) cells as a fully glycosylated soluble dimeric protein. It showed efficient binding both to human membrane-bound IgE isoforms and to the two secretory IgE isoforms. Moreover, the dimeric receptor binds IgE with the expected 1:2 stoichiometry. The receptor-Ig chimera, in 2-fold molar excess, inhibited engagement of secretory IgE to rat basophilic leukemia cells expressing the human {alpha}ß{gamma} receptor. Full self-nature and inability to bind Fc{gamma} receptors make this protein an attractive candidate for clinical applications and a novel biotechnological tool for atopic allergy research.


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L. Vangelista, E. Soprana, M. Cesco-Gaspere, P. Mandiola, G. Di Lullo, R. N. Fucci, F. Codazzi, A. Palini, G. Paganelli, O. R. Burrone, et al.
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