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The Journal of Immunology, 2001, 166: 1781-1789.
Copyright © 2001 by The American Association of Immunologists

The Interaction of Fc{alpha}RI with IgA and Its Implications for Ligand Binding by Immunoreceptors of the Leukocyte Receptor Cluster1

Bruce D. Wines2, Caroline T. Sardjono2, Halina M. Trist, Chan-Sien Lay and P. Mark Hogarth3

The Helen M. Schutt Laboratory for Immunology and Biotechnology, Austin Research Institute, Austin Repatriation Medical Center, Heidelberg, Victoria, Australia

This study defines the molecular basis of the Fc{alpha}RI (CD89):IgA interaction, which is distinct from that of the other leukocyte Fc receptors and their Ig ligands. A comprehensive analysis using both cell-free (biosensor) and cell-based assays was used to define and characterize the IgA binding region of Fc{alpha}RI. Biosensor analysis of mutant Fc{alpha}RI proteins showed that residues Y35, Y81, and R82 were essential for IgA binding, and R52 also contributed. The role of the essential residues (Y35 and R82) was confirmed by analysis of mutant receptors expressed on the surface of mammalian cells. These receptors failed to bind IgA, but were detected by the mAb MY43, which blocks IgA binding to Fc{alpha}RI, indicating that its epitope does not coincide with these IgA binding residues. A homology model of the ectodomains of Fc{alpha}RI was generated based on the structures of killer Ig-like receptors, which share 30–34% identity with Fc{alpha}RI. Key structural features of killer Ig-like receptors are appropriately reproduced in the model, including the structural conservation of the interdomain linker and hydrophobic core (residues V17, V97, and W183). In this Fc{alpha}RI model the residues forming the IgA binding site identified by mutagenesis form a single face near the N-terminus of the receptor, distinct from other leukocyte Fc receptors where ligand binding is in the second domain. This taken together with major differences in kinetics and affinity for IgA:Fc{alpha}RI interaction that were observed depending on whether Fc{alpha}RI was immobilized or in solution suggest a mode of interaction unique among the leukocyte receptors.




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