The binding affinity and dissociation rates of peptides for class I major histocompatibility complex molecules.
Peptides of various lengths derived from the influenza nucleoprotein (NP) bind to H-2Db class I molecules with affinities at 4 degrees C between approximately 3 x 10(5)- approximately 3 x 10(7) M-1. The peptide with the highest affinity corresponds to the sequence of nine amino acids (NP366-374) recently isolated from cells infected with influenza. This peptide forms stable complexes with half-lives greater than 110 h at 4 degrees C, 39 h at 22 degrees C and 3 h at 37 degrees C. Small increases in length of the peptide greatly reduce the stability of the complex (t1/2 approximately 1-10 h at 4 degrees C). These results may explain the homogeneous length of peptides isolated from class I molecules formed in vivo, and suggest that class I and II may differ in their dependence on the length of peptides for the formation of stable complexes.
Cerundolo
V
V
Institute of Molecular Medicine, John Radcliffe Hospital, Headington, Oxford, GB.
Elliott
T
T
Elvin
J
J
Bastin
J
J
Rammensee
H G
HG
Townsend
A
A
D000595:Amino Acid Sequence; D000818:Animals; D000937:Antigen-Antibody Reactions; D003602:Cytotoxicity, Immunologic; D006183:H-2 Antigens / Q000276:immunology; D015395:Histocompatibility Antigens Class I / Q000276:immunology*; D006801:Humans; D051379:Mice / Q000276:immunology; D008969:Molecular Sequence Data; D009698:Nucleoproteins / Q000378:metabolism*; D013602:T-Lymphocytes, Cytotoxic / Q000276:immunology; D013696:Temperature; D014162:Transfection
D006183:H-2 Antigens; D015395:Histocompatibility Antigens Class I; D009698:Nucleoproteins