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RI with IgA and Its Implications for Ligand Binding by Immunoreceptors of the Leukocyte Receptor Cluster1
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
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 FcRI. Biosensor analysis of
mutant FcRI 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 FcRI, indicating that its epitope does not coincide with
these IgA binding residues. A homology model of the ectodomains of
FcRI was generated based on the structures of killer Ig-like
receptors, which share 30–34% identity with FcRI. 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
FcRI 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:FcRI interaction that were observed
depending on whether FcRI was immobilized or in solution suggest a
mode of interaction unique among the leukocyte
receptors.
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