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Cutting Edge |
Departments of
* Cell Biology and
Pathology, Duke University Medical Center, Durham, NC 27710
GRP94(gp96) elicits CD8+ T cell responses against
its bound peptides, a process requiring access of its associated
peptides into the MHC class I cross-presentation pathway of APCs. Entry
into this pathway requires receptor-mediated endocytosis, and CD91
(low-density lipoprotein receptor-related protein) has been reported to
be the receptor mediating GRP94 uptake into APC. However, a direct role
for CD91 in chaperone-based peptide Ag re-presentation has not been
demonstrated. We investigated the contribution of CD91 to GRP94 cell
surface binding, internalization, and trafficking in APCs. Whereas a
clear role for CD91 in 
2-macroglobulin binding and
uptake was readily obtained, the addition of excess CD91 ligand,
activated 2-macroglobulin, or receptor-associated
protein, an antagonist of all known CD91 ligands, did not affect GRP94
cell surface binding, receptor-mediated endocytosis, or peptide
re-presentation. These data identify a CD91-independent, GRP94
internalization pathway that functions in peptide Ag
re-presentation.
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