Inhibition of HLA B8-restricted recognition by unrelated peptides: evidence for allosteric inhibition.
A panel of synthetic peptides representing human lymphocyte antigen (HLA) B8, other class I and class II restricted T cell epitopes and two B cell epitopes, were all able to compete with recognition of a HLA B8 restricted epitope by a cytotoxic T cell clone. Competition was obtained when the competitor peptides were added either before or after the target epitope. The target epitope also had a slow off rate, implicating allosteric inhibition. The presence of non-specific, allosteric binding sites may interfere with experiments attempting to define immunologically relevant MHC binding specificities.
Fernan
A
A
Queensland Institute of Medical Research, Bancroft Centre, Herston, Brisbane, Australia.
Burrows
S R
SR
Moss
D J
DJ
Saul
A
A
Suhrbier
A
A
D000495:Allosteric Site; D000595:Amino Acid Sequence; D000956:Antigens, Viral / Q000276:immunology*; D001402:B-Lymphocytes / Q000276:immunology; D001667:Binding, Competitive; D000939:Epitopes / Q000276:immunology; D006678:HIV / Q000276:immunology*; D015795:HLA-B8 Antigen / Q000276:immunology*; D004854:Herpesvirus 4, Human / Q000276:immunology*; D015395:Histocompatibility Antigens Class I / Q000276:immunology; D000949:Histocompatibility Antigens Class II / Q000276:immunology; D006801:Humans; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000138:chemical synthesis / Q000276:immunology / Q000494:pharmacology*; D013602:T-Lymphocytes, Cytotoxic / Q000276:immunology*
D000956:Antigens, Viral; D000939:Epitopes; D015795:HLA-B8 Antigen; D015395:Histocompatibility Antigens Class I; D000949:Histocompatibility Antigens Class II; D010446:Peptide Fragments