Peptides shorter than a minimal CTL epitope may have a higher binding affinity than the epitope for the class I Kk molecule.
A previously published Kk-specific motif was used to predict that an optimal Kk-restricted epitope within the nucleoprotein (NP) of influenza A/PR/8/34 virus corresponds to sequence SDYEGRLI (residues 50-57). Although this is the minimal epitope recognized by murine cytotoxic T lymphocytes (CTL), its binding affinity for the Kk molecule is increased following removal of either the N-terminal amino acid residue (S) or the N-terminal dipeptide (SD). A possible explanation for this unexpected result is that interactions between the C-terminus of the epitope and the Kk molecule contribute to the binding energy to a much greater extent than interactions between the N-terminus of the epitope and the Kk molecule.
Cossins
J
J
Sir William Dunn School of Pathology, University of Oxford, United Kingdom.
Gould
K
K
Brownlee
G G
GG
D000595:Amino Acid Sequence; D000818:Animals; D002460:Cell Line; D000939:Epitopes; D006183:H-2 Antigens / Q000276:immunology*; D009980:Influenza A virus / Q000276:immunology*; D051379:Mice; D008969:Molecular Sequence Data; D010455:Peptides / Q000138:chemical synthesis / Q000276:immunology; D013602:T-Lymphocytes, Cytotoxic / Q000276:immunology*
D000939:Epitopes; D006183:H-2 Antigens; C024755:H-2K(K) antigen; D010455:Peptides