Empty MHC class I molecules come out in the cold.

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...

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Main Authors: Ljunggren, H, Stam, N, Ohlén, C, Neefjes, J, Höglund, P, Heemels, M, Bastin, J, Schumacher, T, Townsend, A, Kärre, K
Format: Journal article
Language:English
Published: 1990
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author Ljunggren, H
Stam, N
Ohlén, C
Neefjes, J
Höglund, P
Heemels, M
Bastin, J
Schumacher, T
Townsend, A
Kärre, K
author_facet Ljunggren, H
Stam, N
Ohlén, C
Neefjes, J
Höglund, P
Heemels, M
Bastin, J
Schumacher, T
Townsend, A
Kärre, K
author_sort Ljunggren, H
collection OXFORD
description 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.
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spelling oxford-uuid:a54b2363-bd11-4272-b65f-9e8050958f552022-03-27T02:39:27ZEmpty MHC class I molecules come out in the cold.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:a54b2363-bd11-4272-b65f-9e8050958f55EnglishSymplectic Elements at Oxford1990Ljunggren, HStam, NOhlén, CNeefjes, JHöglund, PHeemels, MBastin, JSchumacher, TTownsend, AKärre, KMajor 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.
spellingShingle Ljunggren, H
Stam, N
Ohlén, C
Neefjes, J
Höglund, P
Heemels, M
Bastin, J
Schumacher, T
Townsend, A
Kärre, K
Empty MHC class I molecules come out in the cold.
title Empty MHC class I molecules come out in the cold.
title_full Empty MHC class I molecules come out in the cold.
title_fullStr Empty MHC class I molecules come out in the cold.
title_full_unstemmed Empty MHC class I molecules come out in the cold.
title_short Empty MHC class I molecules come out in the cold.
title_sort empty mhc class i molecules come out in the cold
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