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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.

Original publication




Journal article



Publication Date





476 - 480


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