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Determination of the Agretopic Residues of a Peptide Co‐Restricted to Different Class II Isotypes, I‐A u and I‐E u , and Its Application for Preparation of a Synthetic Peptide Vaccine against Influenza Virus A/Aichi/2/68
Author(s) -
Takami Kimitaka,
Ogasawara Kazumasa,
Itoh Yasushi,
Kajino Kiichi,
Naruse Hirohito,
Onoé Kazunori
Publication year - 1994
Publication title -
microbiology and immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.664
H-Index - 70
eISSN - 1348-0421
pISSN - 0385-5600
DOI - 10.1111/j.1348-0421.1994.tb01857.x
Subject(s) - peptide , immunogenicity , amino acid , biology , alanine , arginine , major histocompatibility complex , stereochemistry , peptide sequence , mhc class i , biochemistry , microbiology and biotechnology , antigen , chemistry , immunology , gene
We have defined that residues 46 and 54 on a synthetic peptide composed of residues 43–58 of pigeon cytochrome c (p43–58) work as agretopes (sites bound to an MHC molecule) in I‐A b mice. Substitution of amino acid residues on these positions altered the peptide to bind with the other MHC molecules. Furthermore, by substituting the agretopic residues with a variety of amino acids, we could determine the class II binding motif for each MHC molecule. In the present study, immunogenicity of a peptide, 46R50V54A, carrying valine (V) at epitopic (site bound to TCR) position 50, arginine (R) and alanine (A) at agretopic positions 46 and 54 of the p43–58, respectively has been analyzed in B10.PL (H‐2 u ) mice. We found that this peptide bound to two different class II isotypes, I‐A u and I‐E u . Arginine at position 46 or alanine at position 54 of the 46R50V54A was shown to be critical for binding to I‐A u or I‐E u , respectively. Further, on the basis of this class II binding motif we could prepare potent peptide vaccines against influenza A/Aichi/2/68 virus in B10. PL mice.