Direct binding of peptide to empty MHC class I molecules on intact cells and in vitro

Cell. 1990 Aug 10;62(3):563-7. doi: 10.1016/0092-8674(90)90020-f.


MHC class I molecules devoid of peptide are expressed on the cell surface of the mouse mutant lymphoma cell line RMA-S upon culture at reduced temperature. Empty class I molecules are thermolabile at the cell surface and in detergent lysates, but can be stabilized by the addition of presentable peptide; peptide binding appears to be a rapid process. Furthermore, class I molecules on the surface of RMA-S (H-2b haplotype) cells cultured at 26 degrees C can efficiently and specifically bind iodinated peptide presented by H-2Kb. Binding of iodinated peptide is also observed at a lower level for nonmutant cells (RMA) cultured at 26 degrees C. These experiments underscore the role for peptide in maintenance of the structure of class I molecules and, more importantly, provide two assay systems to study the interactions of peptides with MHC class I molecules independent of the availability of T cells that recognize a particular peptide-MHC class I complex.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cell Line
  • Cell Membrane / immunology
  • Electrophoresis, Polyacrylamide Gel
  • H-2 Antigens / immunology
  • Histocompatibility Antigens Class I / immunology*
  • Histocompatibility Antigens Class I / isolation & purification
  • Immunoenzyme Techniques
  • Mice
  • Peptides / chemical synthesis
  • Protein Binding


  • H-2 Antigens
  • Histocompatibility Antigens Class I
  • Peptides