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*
Department of Biochemistry, Molecular Biology, and Cell Biology, Northwestern University, Evanston, IL 60208; and
Department of Microbiology, University of Maryland, College Park, MD 20742
Processing and presentation by Ag-specific B cells is initiated by
Ag binding to the B cell Ag receptor (BCR). Cross-linking of the BCR by
Ag results in a rapid targeting of the BCR and bound Ag to the MHC
class II peptide loading compartment (IIPLC). This accelerated delivery
of Ag may be essential in vivo during periods of rapid Ag-driven B cell
expansion and T cell-dependent selection. Here, we use both
immunoelectron microscopy and a nondisruptive protein chemical
polymerization method to define the intracellular pathway of the
targeting of Ags by the BCR. We show that following cross-linking, the
BCR is rapidly transported through transferrin receptor-containing
early endosomes to a LAMP-1+,
ß-hexosaminadase+, multivesicular compartment that is an
active site of peptide-class II complex assembly, containing both class
II-invariant chain complexes in the process of invariant chain
proteolytic removal as well as mature peptide-class II complexes. The
BCR enters the class II-containing compartment as an intact
mIg/Ig
/Igß complex bound to Ag. The pathway by which the BCR
targets Ag to the IIPLC appears not to be identical to that by which
Ags taken up by fluid phase pinocytosis traffick, suggesting that the
accelerated BCR pathway may be specialized and potentially
independently regulated.
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