Epitopes described in "The structure of the human allo-ligand HLA-B*3501 in complex with a cytochrome p450 peptide: steric hindrance influences TCR allo-recognition."

Reference
Article Authors:Christopher S Hourigan; Maria Harkiolaki; Neil A Peterson; John I Bell; E Yvonne Jones; Chris A O'Callaghan
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.
Reference Detail
Reference ID:1004499
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.
Date:2006
Reference Type:Literature
PubMed ID:17109469
Journal:Eur J Immunol
Journal Volume:36
Article Pages:3288-93
Journal ISSN:0014-2980
Article Chemical List:HLA-B Antigens;HLA-B*35:01 antigen;HLA-B35 Antigen;Isoantigens;Ligands;Peptide Fragments;Receptors, Antigen, T-Cell, alpha-beta;Cytochrome P-450 Enzyme System
Article MeSH List:Amino Acid Sequence; Crystallography, X-Ray; Cytochrome P-450 Enzyme System(chemistry; metabolism); HLA-B Antigens(chemistry; metabolism); HLA-B35 Antigen; 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
Curation Last Updated:2014-07-16 21:01:51