Empty MHC class I molecules come out in the cold

Nature. 1990 Aug 2;346(6283):476-80. doi: 10.1038/346476a0.


Major histocompatibility complex (MHC) class I molecules present antigen by transporting peptides from intracellularly degraded proteins to the cell surface for scrutiny by cytotoxic T cells. Recent work suggests that peptide binding may be required for efficient assembly and intracellular transport of MHC class I molecules, but it is not clear whether class I molecules can ever assemble in the absence of peptide. We report here that culture of the murine lymphoma mutant cell line RMA-S at reduced temperature (19-33 degrees C) promotes assembly, and results in a high level of cell surface expression of H-2/beta 2-microglobulin complexes that do not present endogenous antigens, and are labile at 37 degrees C. They can be stabilized at 37 degrees C by exposure to specific peptides known to interact with H-2Kb or Db. Our findings suggest that, in the absence of peptides, class I molecules can assemble but are unstable at body temperature. The induction of such molecules at reduced temperature opens new ways to analyse the nature of MHC class I peptide interactions at the cell surface.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Animals
  • Antigen-Presenting Cells / immunology
  • Biological Transport
  • Cell Membrane / immunology
  • Cold Temperature*
  • H-2 Antigens / immunology
  • H-2 Antigens / metabolism*
  • Lymphoma
  • Macromolecular Substances
  • Mice
  • Mutation
  • Protein Binding
  • Protein Conformation
  • Protein Processing, Post-Translational
  • T-Lymphocytes, Cytotoxic / immunology
  • Tumor Cells, Cultured
  • beta 2-Microglobulin / metabolism


  • H-2 Antigens
  • Macromolecular Substances
  • beta 2-Microglobulin