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- Title
The carboxypeptidase ACE shapes the MHC class I peptide repertoire.
- Authors
Shen, Xiao Z; Billet, Sandrine; Lin, Chentao; Okwan-Duodu, Derick; Chen, Xu; Lukacher, Aron E; Bernstein, Kenneth E
- Abstract
The surface presentation of peptides by major histocompatibility complex (MHC) class I molecules is critical to CD8+ T cell-mediated adaptive immune responses. Aminopeptidases have been linked to the editing of peptides for MHC class I loading, but carboxy-terminal editing is thought to be due to proteasome cleavage. By analysis of wild-type mice and mice genetically deficient in or overexpressing the dipeptidase angiotensin-converting enzyme (ACE), we have now identified ACE as having a physiological role in the processing of peptides for MHC class I. ACE edited the carboxyl terminus of proteasome-produced MHC class I peptides. The lack of ACE exposed new antigens but also abrogated some self antigens. ACE had substantial effects on the surface expression of MHC class I in a haplotype-dependent manner. We propose a revised model of peptide processing for MHC class I by introducing carboxypeptidase activity into the process.
- Subjects
CARBOXYPEPTIDASES; MAJOR histocompatibility complex; PEPTIDES; ANGIOTENSIN converting enzyme; T cells; IMMUNE response; AMINOPEPTIDASES
- Publication
Nature Immunology, 2011, Vol 12, Issue 11, p1078
- ISSN
1529-2908
- Publication type
Article
- DOI
10.1038/ni.2107