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An influenza B virus nucleoprotein (BNP) peptide, residues 82-94, defined by limited sequence homology with an HLA-A2-restricted peptide from influenza A matrix protein, was recognized by HLA-A2-restricted CTL. Reciprocal inhibition of T cell recognition by the two peptides suggest that the BNP peptide may have lower avidity for HLA-A2 molecules than the matrix peptide. The interaction between this peptide and HLA-A2 was explored by studying the CTL recognition of BNP 82-94 presented by mutant HLA-A2 molecules. Mutations at residues 9, 99, 70, 74, 152 and 156 were found to abolish T cell recognition of the BNP peptide. These results were compared with results previously obtained with the influenza A matrix peptide and suggest that the two peptides bind differently in the peptide binding site.


Journal article


Journal of immunology (Baltimore, Md. : 1950)

Publication Date





4098 - 4103


Institute of Molecular Medicine, John Radcliffe Hospital, Oxford, England.


T-Lymphocytes, Cytotoxic, Humans, Influenza B virus, Peptides, Nucleoproteins, Viral Matrix Proteins, HLA-A2 Antigen, Epitopes, Cross Reactions, Amino Acid Sequence, Mutation