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and Igß Are Required for Efficient Trafficking to Late Endosomes and to Enhance Antigen Presentation1
Sections of
*
Rheumatology and
Pathology, Department of Medicine, Committee on Immunology, University of Chicago, Chicago, IL 60637; and
Department of Cell Biology and Molecular Genetics, University of Maryland, College Park, MD 20742
The B cell Ag receptor (BCR) is a multimeric complex, containing
Ig
and Igß, capable of internalizing and delivering specific Ags
to specialized late endosomes, where they are processed into peptides
for loading onto MHC class II molecules. By this mechanism, the
presentation of receptor-selected epitopes to T cells is enhanced by
several orders of magnitude. Previously, it has been reported that,
under some circumstances, either Ig or Igß can facilitate the
presentation of Ags. However, we now demonstrate that if these Ags are
at low concentrations and temporally restricted, both Ig and Igß
are required. When compared with the BCR, chimeric complexes containing
either chain alone were internalized but failed to access the MHC class
II-enriched compartment (MIIC) or induce the aggregation and fusion of
its constituent vesicles. Furthermore, Ig/Igß complexes in which
the immunoreceptor tyrosine-based activation motif tyrosines of Ig
were mutated were also incapable of accessing the MIIC or of
facilitating the presentation of Ag. These data indicate that both
Ig and Igß contribute signaling, and possibly other functions, to
the BCR that are necessary and sufficient to reconstitute the
trafficking and Ag-processing enhancing capacities of the intact
receptor complex.
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