Figure 4 - full size

 

Figure 4.
Figure 4. SB27 TCR recognition of the HLA-B^*3508-LPEP complex is antibody like and is dominated by TCR-peptide interactions. (a,b) GRASP image of the SB27 TCR-peptide interaction (a) compared with that of a complex between an Fab and a peptide from human rhinovirus viral capsid protein VP2 (b; Protein Data Bank accession number, 1A3R)46. TCR V[ ]and Fab V[H], red; TCR V and Fab V[L], blue; Epstein-Barr virus LPEP and rhinovirus VP2 peptides, yellow. (c) Closer view of the SB27 TCR interactions with the solvent-exposed side chains of the LPEP peptide. Peptide, orange; CDR loop colors are as in Figure 1b. (d) Dose-response assays of analogs of the 13-residue peptide (LPEPLPQGQLTAY) that include single-amino acid substitutions, assessing recognition by SB27 CTLs (chromium-release assays, left) and binding to 'empty' HLA-B^*3508 with the transporter associated with antigen processing-deficient T2-B^*3508 (right). Peptides recognized well in the cytotoxicity assays are assumed to bind well to HLA-B^*3508 and are therefore excluded from the MHC-binding assays (NT). Data represent peptide concentrations for half-maximal lysis or binding calculated from dose-response curves for each peptide and are representative of two independent experiments with similar results.

The above figure is reprinted by permission from Macmillan Publishers Ltd: Nat Immunol (2005, 6, 1114-1122) copyright 2005.