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Tissue Antigens. 2015 Jun;85(6):492-6. doi: 10.1111/tan.12565. Epub 2015 Apr 16.

A comprehensive analysis of peptides presented by HLA-A1.

Author information

1
Department of Biochemistry and Molecular Biology, Monash University, Clayton, Victoria 3800, Australia; The Department of Biochemistry and Molecular Biology, The Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Parkville, Victoria 3010, Australia.

Abstract

Human leukocyte antigen (HLA)-A1 is one of the most common Caucasian HLA-A alleles. Here, we describe the comprehensive analysis of the HLA-A*01:01 ligand repertoire with the identification of 4735 naturally processed and presented peptides derived from 2477 source proteins. We found HLA-A*01:01 bound an equivalent number of ligands of 9 or 10 amino acids in length as well as being remarkably tolerant of even longer peptides. Indeed close to half of the HLA-A1 bound peptides identified ranged between 11 and 13 amino acids in length. These longer peptides contained the strong canonical motif of and acidic E/D residue at position 3 (P3) and Y at the C-terminus (CΩ), a motif that was still apparent in peptides of up to 18 amino acids in length. The identification of this large database of natural ligands will facilitate the refinement of predictive algorithms particularly with respect to longer peptide ligands.

KEYWORDS:

antigen presentation; human leukocyte antigen-A1; immunopeptidome; mass spectrometry; peptides

PMID:
25880248
DOI:
10.1111/tan.12565
[Indexed for MEDLINE]

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