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R (CD89) Binding of IgA1
* Immunotherapy Laboratory, Department of Immunology, University Medical Center,
Medarex Europe, and
Genmab, Utrecht, The Netherlands
IgA, the principal ligand for Fc
RI, exists in serum as monomeric
IgA and at mucosal sites as secretory IgA (SIgA). SIgA consists of
dimeric IgA linked by joining chain and secretory components. Human
polymorphonuclear leukocytes (PMN) and mouse PMN transgenic for human
FcRI exhibited spreading and elicited respiratory burst activity
upon interaction with either serum or SIgA. However, PMN devoid of the
2 integrin Mac-1 (Mac-1-/-) were unable to
bind SIgA, despite expression of FcRI. Consistent with this, serum
IgA stimulated Mac-1-/- PMN oxygen radical production, in
contrast to SIgA. Binding studies showed the secretory component, by
itself, to interact with Mac-1-expressing PMN, but not with
Mac-1-/- PMN. These data demonstrate an essential role
for Mac-1 in establishing SIgA-FcRI
interactions.
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