Characterization and quantitation of peptide-MHC complexes produced from hen egg lysozyme using a monoclonal antibody

Immunity. 1997 Jun;6(6):727-38. doi: 10.1016/s1074-7613(00)80448-3.


Here we describe generation of Aw3.18, a monoclonal antibody that recognizes peptide residues 48-62 of hen egg lysozyme (HEL) bound to the MHC class II molecule I-Ak. Epitope mapping revealed that Aw3.18 detects a change in the solvent-exposed surface of this peptide-MHC complex upon substitution of the peptide side chain at position P1. Furthermore, Aw3.18 blocked recognition by some, but not all, of the HEL 48-62-reactive T cell hybridomas tested, suggesting a heterogeneity in the T cell response toward this complex. Finally, using Aw3.18, it was possible to determine the fraction of I-Ak molecules loaded with 48-62 peptide after culture of an antigen-presenting cell in medium containing HEL.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Antibodies, Monoclonal / immunology*
  • Antibody Specificity
  • Antigen-Presenting Cells / immunology
  • B-Lymphocytes / immunology
  • Binding Sites, Antibody
  • Binding, Competitive
  • Histocompatibility Antigens Class II / immunology*
  • Macromolecular Substances
  • Mice
  • Molecular Sequence Data
  • Muramidase / immunology
  • Peptides / immunology*
  • Protein Conformation
  • Protein Structure, Tertiary
  • T-Lymphocytes / immunology*


  • Antibodies, Monoclonal
  • Histocompatibility Antigens Class II
  • Macromolecular Substances
  • Peptides
  • Muramidase