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| Article Authors: | Christopher S Hourigan; Maria Harkiolaki; Neil A Peterson; John I Bell; E Yvonne Jones; Chris A O'Callaghan |
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| Article Title: | The structure of the human allo-ligand HLA-B*3501 in complex with a cytochrome p450 peptide: steric hindrance influences TCR allo-recognition. |
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| Reference ID: | 1004499 |
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| Abstract: | Virus-specific T cell populations have been implicated in allo-recognition. The subdominant T cell receptor JL12 recognizes both HLA-B*0801 presenting the Epstein-Barr virus-derived peptide FLRGRAYGL and also HLA-B*3501 presenting the cytochrome p450 self peptide KPIVVLHGY. This cross-reactivity could promote the rejection of HLA-B*3501-positive cells in Epstein-Barr virus-exposed HLA-B*0801 recipients. LC13, the dominant TCR against the HLA-B*0801:FLRGRAYGL complex, fails to recognize HLA-B*3501:KPIVVLHGY. We report the 1.75-Angstrom resolution crystal structure of the human allo-ligand HLA-B*3501:KPIVVLHGY. Similarities between this structure and that of HLA-B*0801:FLRGRAYGL may facilitate cross-recognition by JL12. Moreover, the elevated peptide position in HLA-B*3501:KPIVVLHGY would provide steric hindrance to LC13, preventing it from interacting in the manner in which it interacts with HLA-B*0801:FLRGRAYGL. These findings are relevant to understanding the basis of T cell cross-reactivity in allo-recognition, optimal transplant donor-recipient matching and developing specific molecular inhibitors of allo-recognition. |
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| Affiliations: | Nuffield Department of Medicine, John Radcliffe Hospital, Oxford, UK. |
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| Date: | 2006 |
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| Reference Type: | Literature |
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| PubMed ID: | 17109469 |
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| Journal: | Eur J Immunol |
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| Journal Volume: | 36 |
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| Article Pages: | 3288-93 |
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| Journal ISSN: | 0014-2980 |
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| Article Chemical List: | HLA-B Antigens;HLA-B*3501 antigen;Isoantigens;Ligands;Peptide Fragments;Receptors, Antigen, T-Cell, alpha-beta;Cytochrome P-450 Enzyme System |
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| Article MeSH List: | Amino Acid Sequence; Crystallography, X-Ray; Cytochrome P-450 Enzyme System(chemistry; metabolism ); HLA-B Antigens(chemistry; metabolism ); Humans; Isoantigens(chemistry; metabolism ); Ligands; Molecular Sequence Data; Peptide Fragments(chemistry; metabolism ); Protein Binding(immunology ); Protein Structure, Tertiary; Receptors, Antigen, T-Cell, alpha-beta(chemistry; metabolism ); Stereoisomerism |
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| Curation Last Updated: | 2011-03-28 22:11:25 |
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