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J Biol Chem, Vol. 274, Issue 33, 23508-23514, August 13, 1999
From the Department of Molecular and Cellular Pathology, University
of Dundee Medical School, Ninewells Hospital,
Dundee DD1 9SY, United Kingdom
Cellular receptors for IgA (Fc
Identification of Residues in the CH2/CH3 Domain Interface of IgA
Essential for Interaction with the Human Fc
Receptor (FcR)
CD89
R) mediate
important protective functions. An extensive panel of site-directed
mutant IgAs was used to identify IgA residues critical for FcR
(CD89) binding and triggering. Although a tailpiece-deleted IgA1 was
able to bind and trigger CD89, antibodies featuring CH3 domain
exchanges between human IgA1 and IgG1 could not, indicating that both
domains but not the tailpiece are required for FcR recognition. To
further investigate the role of the interdomain region, numerous IgA1s, each with a point substitution in either of two interdomain loops (Leu-257
Gly-259 in C2; Pro-440Phe-443 in C3), were generated. With only one exception (G259R), substitutions produced either ablation
(L257R, P440A, A442R, F443R) or marked reduction (P440R) in CD89
binding and triggering. Further support for involvement of these
interdomain loops was provided by interspecies comparisons of IgA. Thus
a human IgA1 mutant, LA441-442MN, which mimicked the mouse IgA loop
sequence through substitution of two adjacent residues in the C3
loop, was found, like mouse IgA, not to bind CD89. In contrast, bovine
IgA1, identical to human IgA1 within these interdomain loops despite
numerous differences elsewhere in the Fc region, did bind CD89. We have
thus identified motifs in the interdomain region of IgA Fc critical for
FcR binding and triggering, significantly enhancing present
understanding of the molecular basis of the IgA-FcR interaction.
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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