Presentation of viral antigen by MHC class I molecules is dependent on a putative peptide transporter heterodimer.
Major histocompatibility complex (MHC) class I molecules present peptides derived from the endogenous protein pool to cytotoxic T lymphocytes, which can thus recognize intracellular antigen. This pathway may depend on a transporter (PSF1) to mediate entry of the cytosolic peptides into a pre-Golgi c...
Main Authors: | , , , , , |
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Format: | Journal article |
Language: | English |
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1992
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_version_ | 1797086342748831744 |
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author | Spies, T Cerundolo, V Colonna, M Cresswell, P Townsend, A DeMars, R |
author_facet | Spies, T Cerundolo, V Colonna, M Cresswell, P Townsend, A DeMars, R |
author_sort | Spies, T |
collection | OXFORD |
description | Major histocompatibility complex (MHC) class I molecules present peptides derived from the endogenous protein pool to cytotoxic T lymphocytes, which can thus recognize intracellular antigen. This pathway may depend on a transporter (PSF1) to mediate entry of the cytosolic peptides into a pre-Golgi compartment where they bind to class I heavy chains and promote their stable assembly with beta 2-microglobulin. There is, however, only indirect support for this function of PSF1. Here we show that PSF1 is necessary for the efficient assembly of class I molecules and enables them to present a peptide epitope derived from endogenously synthesized viral antigen. Immunochemical and genetic data demonstrate that the PSF1 polypeptide is associated with a complementary transporter chain, which is polymorphic and is encoded by the PSF2 gene, which is closely linked to PSF1. |
first_indexed | 2024-03-07T02:20:38Z |
format | Journal article |
id | oxford-uuid:a3c9fd12-d738-4918-8fdc-ef986edeb6c5 |
institution | University of Oxford |
language | English |
last_indexed | 2024-03-07T02:20:38Z |
publishDate | 1992 |
record_format | dspace |
spelling | oxford-uuid:a3c9fd12-d738-4918-8fdc-ef986edeb6c52022-03-27T02:29:31ZPresentation of viral antigen by MHC class I molecules is dependent on a putative peptide transporter heterodimer.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:a3c9fd12-d738-4918-8fdc-ef986edeb6c5EnglishSymplectic Elements at Oxford1992Spies, TCerundolo, VColonna, MCresswell, PTownsend, ADeMars, RMajor histocompatibility complex (MHC) class I molecules present peptides derived from the endogenous protein pool to cytotoxic T lymphocytes, which can thus recognize intracellular antigen. This pathway may depend on a transporter (PSF1) to mediate entry of the cytosolic peptides into a pre-Golgi compartment where they bind to class I heavy chains and promote their stable assembly with beta 2-microglobulin. There is, however, only indirect support for this function of PSF1. Here we show that PSF1 is necessary for the efficient assembly of class I molecules and enables them to present a peptide epitope derived from endogenously synthesized viral antigen. Immunochemical and genetic data demonstrate that the PSF1 polypeptide is associated with a complementary transporter chain, which is polymorphic and is encoded by the PSF2 gene, which is closely linked to PSF1. |
spellingShingle | Spies, T Cerundolo, V Colonna, M Cresswell, P Townsend, A DeMars, R Presentation of viral antigen by MHC class I molecules is dependent on a putative peptide transporter heterodimer. |
title | Presentation of viral antigen by MHC class I molecules is dependent on a putative peptide transporter heterodimer. |
title_full | Presentation of viral antigen by MHC class I molecules is dependent on a putative peptide transporter heterodimer. |
title_fullStr | Presentation of viral antigen by MHC class I molecules is dependent on a putative peptide transporter heterodimer. |
title_full_unstemmed | Presentation of viral antigen by MHC class I molecules is dependent on a putative peptide transporter heterodimer. |
title_short | Presentation of viral antigen by MHC class I molecules is dependent on a putative peptide transporter heterodimer. |
title_sort | presentation of viral antigen by mhc class i molecules is dependent on a putative peptide transporter heterodimer |
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