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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.

Original publication

DOI

10.1002/eji.1830210915

Type

Journal article

Journal

Eur J Immunol

Publication Date

09/1991

Volume

21

Pages

2069 - 2075

Keywords

Amino Acid Sequence, Animals, Antigen-Antibody Reactions, Cytotoxicity, Immunologic, H-2 Antigens, Histocompatibility Antigens Class I, Humans, Mice, Molecular Sequence Data, Nucleoproteins, T-Lymphocytes, Cytotoxic, Temperature, Transfection