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Effect of anchor residue modifications on the stability of HLA-A11/peptide complexes

R Gavioli1, Q J Zhang, M Marastoni

  • 1Department of Biochemistry and Molecular Biology, University of Ferrara, Italy.

Biochemical and Biophysical Research Communications
|January 5, 1995
PubMed

MHC class I antigens bind peptides derived from endogenous proteins and present them to cytotoxic T lymphocytes. This binding is selective and shows high allele specificity. Peptides binding to HLA-A11 contain a hydrophobic or a small polar amino acid at position 2 and a lysine at the carboxy terminus. Peptide analogues, derived from previously identified high affinity peptides and carrying amino acid substitutions in position 2, were used to determine the requirements for formation of stable HLA-A11/peptide complexes. By kinetic analysis we were able to discriminate among apparent and true binders. Only analogues carrying in position 2 the amino acids valine, threonine and isoleucine formed stable complexes with HLA-A11 with a half life > or = 72 hours.

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