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Receptor Essential for Interaction with IgA1
Helen M. Schutt Laboratory for Immunology, The Austin Research Institute, Austin Repatriation Medical Centre, Heidelberg, Victoria, Australia
The FcR family contains multiple receptors for Igs, of which the
most distantly related (
20%) is the IgA receptor (human Fc
R),
being more homologous (35%) to another family of killer-inhibitory
receptor-related immunoreceptors with a 19q13.4 chromosomal location in
humans. This study of the FcR demonstrated that, like several IgG
receptors, FcR is a low affinity receptor for Ab
(Ka 106 M-1).
Rapid dissociation of the rsFcR:IgA complex
(t1/2 25 s) suggests that monomer
IgA would bind transiently to cellular FcRs, while IgA immune
complexes could bind avidly. Mutagenesis of histidyl 85 and arginyl 82,
in the FG loop of domain 1, demonstrated that these residues were
essential for the IgA-binding activity of FcR, while arginyl 87
makes a minor contribution to the binding activity of the receptor.
This site is unusual among the Fc receptors (Fc
RII, FcRIII, and
Fc
RI), in which the ligand binding site is in domain 2 rather than
domain 1, but like FcR, the FG loop comprises part of the ligand
binding site. The putative F and G strands flanking the FcR ligand
binding site are highly homologous in the other killer-inhibitory
receptor-related immunoreceptors, suggesting they comprise a conserved
structural element on which divergent FG loops are presented and
participate in the specific ligand interactions of each of these
receptors.
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