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RIIB11
Department of Biochemistry, Molecular Biology, and Cell Biology, Northwestern University, Evanston, IL 60208
The processing and presentation of Ag by Ag-specific B cells is
highly efficient due to the dual function of the B cell Ag receptor
(BCR) in both signaling for enhanced processing and endocytosing bound
Ag. The BCR for IgG (Fc
RIIB1) is a potent negative coreceptor of the
BCR that blocks Ag-induced B cell proliferation. Here we investigate
the influence of the FcRIIB1 on BCR-mediated Ag processing and show
that coligating the FcRIIB1 and the BCR negatively regulates both
BCR signaling for enhanced Ag processing and BCR-mediated Ag
internalization. Treatment of splenic B cells with F(ab')2
anti-Ig significantly enhances APC function compared with the
effect of whole anti-Ig; however, whole anti-Ig treatment is
effective when binding to the FcRIIB1 was blocked by a
FcRII-specific mAb. Processing and presentation of Ag covalently
coupled to anti-Ig were significantly decreased compared with Ag
coupled to F(ab')2anti-Ig; however, the processing of
the two Ag-Ab conjugates was similar in cells that did not express
FcRIIB1 and in splenic B cells treated with a FcRII-specific mAb
to block Fc binding. Internalization of monovalent Ag by B cells was
reduced in the presence of whole anti-Ig as compared with
F(ab')2 anti-Ig, but the internalized Ag was correctly
targeted to the class II peptide loading compartment. Taken together,
these results indicate that the FcRIIB1 is a negative regulator of
the BCR-mediated Ag-processing function.
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