Cutting edge: CD91-independent cross-presentation of GRP94(gp96)-associated peptides.
Published
Journal Article
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 alpha(2)-macroglobulin binding and uptake was readily obtained, the addition of excess CD91 ligand, activated alpha(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.
Full Text
Duke Authors
Cited Authors
- Berwin, B; Hart, JP; Pizzo, SV; Nicchitta, CV
Published Date
- May 1, 2002
Published In
Volume / Issue
- 168 / 9
Start / End Page
- 4282 - 4286
PubMed ID
- 11970968
Pubmed Central ID
- 11970968
International Standard Serial Number (ISSN)
- 0022-1767
Digital Object Identifier (DOI)
- 10.4049/jimmunol.168.9.4282
Language
- eng
Conference Location
- United States