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*
National Institute of Immunology, New Delhi, India;
National Centre for Biological Sciences, UAS-GKVK Campus, Bangalore, India; and
Department of Immunology, University of Washington School of Medicine, Seattle, WA 98195
Peptides from extracellular proteins presented on MHC class II are
mostly generated and loaded in endolysosomal compartments, but the
major pathways responsible for loading peptides from APC-endogenous
sources on MHC class II are as yet unclear. In this study, we show that
MHC class II molecules present peptides from proteins such as OVA or
conalbumin introduced into the cytoplasm by hyperosmotic pinosome
lysis, with efficiencies comparable to their presentation via
extracellular fluid-phase endocytosis. This cytosolic presentation
pathway is sensitive to proteasomal inhibitors, whereas the
presentation of exogenous Ags taken up by endocytosis is not.
Inhibitors of nonproteasomal cytosolic proteases can also inhibit MHC
class II-restricted presentation of cytosolically delivered protein,
without inhibiting MHC class I-restricted presentation from the same
protein. Cytosolic processing of a soluble fusion protein containing
the peptide epitope I-E
52–68 yields an epitope that is
similar to the one generated during constitutive presentation of I-E
as an endogenous transmembrane protein, but is subtly different from
the one generated in the exogenous pathway. Constitutive MHC class
II-mediated presentation of the endogenous transmembrane protein I-E
is also specifically inhibited over time by inhibitors of cytosolic
proteolysis. Thus, Ag processing in the cytoplasm appears to be
essential for the efficient presentation of endogenous proteins, even
transmembrane ones, on MHC class II, and the proteolytic pathways
involved may differ from those used for MHC class I-mediated
presentation.
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