An HLA-B35-restricted epitope modified at an anchor residue results in an antagonist peptide.

Abstract:

:Peptides associated with HLA-B35 commonly have a proline or occasionally a serine residue in the P2 anchor position of the peptide, with a tyrosine at the C terminus. Based on this motif, we identified an octamer epitope from influenza A matrix protein which is presented by HLA-B35. The requirements for MHC binding and T cell receptor contact have been analyzed using analogs of this peptide with substitutions at positions 1, 2, 4, 7 and 8. The natural epitope contains a serine residue at P2 of the peptide. Substitution of this residue with proline (the favored amino acid in this position in B35-associated peptides) considerably enhances binding to HLA-B35 in the T2-B35 cell line, but the peptide is not recognized by the majority of CTL clones and can antagonize recognition of the index peptide. This suggests that a conservative substitution at the P2 anchor position results in a conformational change in the peptide-MHC surface exposed to the T cell receptor.

journal_name

Eur J Immunol

authors

Dong T,Boyd D,Rosenberg W,Alp N,Takiguchi M,McMichael A,Rowland-Jones S

doi

10.1002/eji.1830260210

subject

Has Abstract

pub_date

1996-02-01 00:00:00

pages

335-9

issue

2

eissn

0014-2980

issn

1521-4141

journal_volume

26

pub_type

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