The human major histocompatibility complex class Ib molecule HLA-E binds signal sequence-derived peptides with primary anchor residues at positions 2 and 9

Eur J Immunol. 1997 May;27(5):1164-9. doi: 10.1002/eji.1830270517.

Abstract

Human histocompatibility leukocyte antigen E (HLA-E) and mouse major histocompatibility complex (MHC) class Ib antigen, Qa-1, share the same substitutions at two normally conserved positions 143 and 147, which are likely to affect binding of the C terminus of peptides. Qa-1 is able to bind a peptide derived from the leader sequence of H-2 D and H-2 L molecules. We developed a peptide binding assay in vitro to compare the binding specificity of HLA-E with the mouse MHC class Ib molecule Qa-1. We demonstrate that HLA-E binds, although poorly, the peptide which binds to Qa-1 and that it also binds nonamer signal sequence-derived peptides from human MHC class I molecules. Using alanine and glycine substitutions, we could define primary anchor residues at positions 2 and 9 and secondary anchor residues at position 7 and possibly 3.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Cell Line, Transformed
  • HLA Antigens / isolation & purification
  • HLA Antigens / metabolism*
  • Histocompatibility Antigens Class I / isolation & purification
  • Histocompatibility Antigens Class I / metabolism*
  • Humans
  • Isoelectric Focusing
  • L Cells
  • Mice
  • Oligopeptides / metabolism
  • Protein Binding / immunology
  • Protein Conformation*
  • Protein Sorting Signals / metabolism*

Substances

  • HLA Antigens
  • HLA-E antigen
  • Histocompatibility Antigens Class I
  • Oligopeptides
  • Protein Sorting Signals
  • Q surface antigens