The binding affinity and dissociation rates of peptides for class I major histocompatibility complex molecules.

Journal article

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.

Authors: Cerundolo, V; Elliott, T; Elvin, J; Bastin, J; Rammensee, H

• Publication status: Published
• Journal: European journal of immunology
• Volume: 21
• Issue: 9
• Pages: 2069-2075
• Publication date: 1991-09-01
• DOI: 10.1002/eji.1830210915
• EISSN: 1521-4141
• ISSN: 0014-2980
• Language: English
• Keywords: Molecular Sequence Data; Transfection; Temperature; H-2 Antigens; Antigen-Antibody Reactions; Humans; Amino Acid Sequence; T-Lymphocytes, Cytotoxic; Animals; Cytotoxicity, Immunologic; Mice; Nucleoproteins; Histocompatibility Antigens Class I