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- Title
The ER aminopeptidase ERAP1 enhances or limits antigen presentation by trimming epitopes to 8-9 residues.
- Authors
York, Ian A; Chang, Shih-Chung; Saric, Tomo; Keys, Jennifer A; Favreau, Janice M; Goldberg, Alfred L; Rock, Kenneth L
- Abstract
Endoplasmic reticulum (ER) aminopeptidase 1 (ERAP1) appears to be specialized to produce peptides presented on class I major histocompatibility complex molecules. We found that purified ERAP1 trimmed peptides that were ten residues or longer, but spared eight-residue peptides. In vivo, ERAP1 enhanced production of an eight-residue ovalbumin epitope from precursors extended on the NH2 terminus that were generated either in the ER or cytosol. Purified ERAP1 also trimmed nearly half the nine-residue peptides tested. By destroying such nine-residue peptides in normal human cells, ERAP1 reduced the overall supply of antigenic peptides. However, after interferon-gamma treatment, which causes proteasomes to produce more NH2-extended antigenic precursors, ERAP1 increased the supply of peptides for MHC class I antigen presentation.
- Publication
Nature immunology, 2002, Vol 3, Issue 12, p1177
- ISSN
1529-2908
- Publication type
Journal Article
- DOI
10.1038/ni860