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...

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Main Authors: Spies, T, Cerundolo, V, Colonna, M, Cresswell, P, Townsend, A, DeMars, R
Format: Journal article
Language:English
Published: 1992
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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.
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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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