Empty MHC class I molecules come out in the cold
| Autor: | Hans-Gustaf Ljunggren, Nico J. Stam, Claes Öhlén, Jacques J. Neefjes, Petter Höglund, Marie-Thérèse Heemels, Judy Bastin, Ton N. M. Schumacher, Alain Townsend, Klas Kärre, Hidde L. Ploegh |
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| Rok vydání: | 1990 |
| Předmět: |
Lymphoma
Macromolecular Substances Protein Conformation Antigen presentation Antigen-Presenting Cells Peptide binding Major histocompatibility complex Mice Tapasin Antigen MHC class I Tumor Cells Cultured Cytotoxic T cell Animals Multidisciplinary biology Chemistry Cell Membrane H-2 Antigens Biological Transport Cell biology Cold Temperature ATP-Binding Cassette Sub-Family B Member 2 Immunology Mutation biology.protein beta 2-Microglobulin Protein Processing Post-Translational Protein Binding T-Lymphocytes Cytotoxic |
| Zdroj: | Nature. 346(6283) |
| ISSN: | 0028-0836 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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