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The ER aminopeptidase ERAP1 enhances or limits antigen presentation by trimming epitopes to 8-9 residues.

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.

journal_name

Nat Immunol

journal_title

Nature immunology

authors

York IA,Chang SC,Saric T,Keys JA,Favreau JM,Goldberg AL,Rock KL

doi

10.1038/ni860

keywords:

subject

Has Abstract

pub_date

2002-12-01 00:00:00

pages

1177-84

issue

12

eissn

1529-2908

issn

1529-2916

pii

ni860

journal_volume

3

pub_type

杂志文章

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