期刊
MOLECULAR IMMUNOLOGY
卷 53, 期 1-2, 页码 126-131出版社
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.molimm.2012.07.009
关键词
Non-classical HLA; Class Ib; HLA-E; HLA-A2; Antigen processing; MHC binding motif
资金
- Dutch Cancer Society [UL2007-3897]
- Landsteiner Foundation for Blood Transfusion Research [07-13]
- AICR [09-776]
The non-classical HLA-E is a conserved class I molecule that mainly presents monomorphic leader peptides derived from other HLA class I molecules. These leader peptides comprise an optimized sequence for tight and deep binding into the HLA-E groove. In a TAP-deficient environment, as it can be generated during viral infection or in tumor tissue, loading of the classical leader peptide sequences is hampered leading to an alternative HLA-E peptide repertoire. In this study, we characterized this alternative peptide repertoire using cells in which TAP activity is inhibited. We identified more than 500 unique peptide sequences carried by HLA-E and found that their binding motif is different from the dominant leader peptides. Hydrophobic amino acids were only found at positions 2 and 9, in close resemblance to the peptide binding motif of HLA-A*0201. HLA-E-eluted peptides were indeed able to bind this classical HLA class I molecule. Our findings suggest that the dominant leader peptides uniquely conform to HLA-E, but that in their absence a peptide pool is presented like that of HLA-A*0201. (C) 2012 Elsevier Ltd. All rights reserved.
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