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Blood, 1 January 2001, Vol. 97, No. 1, pp. 205-213
IMMUNOBIOLOGY
Presentation of ovalbumin internalized via the immunoglobulin-A
Fc receptor is enhanced through Fc receptor  -chain
signaling
Li Shen,
Marjolein van
Egmond,
Karyn Siemasko,
Hong Gao,
Terri Wade,
Mark L. Lang,
Marcus Clark,
Jan G. J. van de Winkel, and
William F. Wade
From the Department of Immunology and Microbiology, Dartmouth
Medical School, Dartmouth-Hitchcock Medical Center, Lebanon, New
Hampshire; the Department of Immunology, University Hospital Utrecht,
Utrecht, The Netherlands; and the Department of Medicine, Rheumatology
Section, Division of Biological Sciences, and The Pritzker School of
Medicine, University of Chicago, Chicago, IL.
The mechanism of enhanced presentation of ovalbumin (OVA)
internalized as immunoglobulin A (IgA)-OVA via the IgA Fc receptor (Fc R) was analyzed by focusing on the role of the FcR-associated  chain. Comparison of B-cell transfectants expressing FcR plus wild-type (WT) chain or chain in which the
immunoreceptor tyrosine-based activation motif (ITAM) was altered by
tyrosine mutation or substitution with the ITAM of FcRIIA showed
that signaling-competent ITAM was not required for endocytosis of
IgA-OVA. However, antigen presentation was impaired by ITAM changes.
Signaling-competent -chain ITAM appeared necessary for transport of
ligated FcR to a lamp-1+ late endocytic compartment for
remodeling and/or activation of that compartment and also for efficient
degradation of IgA complexes. Moreover, FcR ligation also activated
efficient processing of nonreceptor-targeted antigen. The
results suggest that -chain signaling activates the antigen
processing compartment.
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