| First Author | Yin L | Year | 2012 |
| Journal | Proc Natl Acad Sci U S A | Volume | 109 |
| Issue | 45 | Pages | 18517-22 |
| PubMed ID | 23091041 | Mgi Jnum | J:191231 |
| Mgi Id | MGI:5461276 | Doi | 10.1073/pnas.1215928109 |
| Citation | Yin L, et al. (2012) T-cell receptor (TCR) interaction with peptides that mimic nickel offers insight into nickel contact allergy. Proc Natl Acad Sci U S A 109(45):18517-22 |
| abstractText | T cell-mediated allergy to Ni(++) is one of the most common forms of allergic contact dermatitis, but how the T-cell receptor (TCR) recognizes Ni(++) is unknown. We studied a TCR from an allergic patient that recognizes Ni(++) bound to the MHCII molecule DR52c containing an unknown self-peptide. We identified mimotope peptides that can replace both the self-peptide and Ni(++) in this ligand. They share a p7 lysine whose epsilonNH(2) group is surface-exposed when bound to DR52c. Whereas the TCR uses germ-line complementary-determining region (CDR)1/2 amino acids to dock in the conventional diagonal mode on the mimotope-DR52c complex, the interface is dominated by the TCR Vbeta CDR3 interaction with the p7 lysine. Mutations in the TCR CDR loops have similar effects on the T-cell response to either the mimotope or Ni(++) ligand. We suggest that the mimotope p7 lysine mimics Ni(++) in the natural TCR ligand and that MHCII beta-chain flexibility in the area around the peptide p7 position forms a common site for cation binding in metal allergies. |
