An HLA‐B27 polymorphism (B* 2710) that is critical for T‐cell recognition has limited effects on peptide specificity

Abstract:

The B*2710 subtype differs from the HLA‐B27 prototype (B*2705) only by having Glu instead of Val at position 152, in the α2 helix of the peptide‐binding site. In spite of its structural similarity most allore‐active CTL raised against B*2705 fail to cross‐react with B*2710. Indeed, of the residues that are polymorphic among HLA‐B27 subtypes, the Val> Glu152 change has the greatest influence on HLA‐B27 T‐cell antigenicity. The molecular basis for this antigenic disparity was analyzed in this study. Sequence analysis indicated that B*2710‐bound peptides have very similar motifs to B*2705‐bound ones both at the main and auxiliary anchor positions. In addition, most of the individual ligands sequenced from B*2710 were previously found in B*2705. Together these results indicate that both subtypes have largely overlapping peptide repertoires. Molecular dynamics simulations of a common ligand in complex with …

Año de publicación:

1998

Keywords:

Fuente:

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