Processing of major histocompatibility class I-restricted antigens in the endoplasmic reticulum.

We have introduced long precursor peptides directly into the endoplasmic reticulum (ER) of a mutant cell line (T2-Db) that lacks the ability to transport peptides from the cytosol to the ER in a transporter associated with antigen processing (TAP) dependent way. This was done by expressing various i...

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Main Authors: Elliott, T, Willis, A, Cerundolo, V, Townsend, A
Format: Journal article
Language:English
Published: 1995
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author Elliott, T
Willis, A
Cerundolo, V
Townsend, A
author_facet Elliott, T
Willis, A
Cerundolo, V
Townsend, A
author_sort Elliott, T
collection OXFORD
description We have introduced long precursor peptides directly into the endoplasmic reticulum (ER) of a mutant cell line (T2-Db) that lacks the ability to transport peptides from the cytosol to the ER in a transporter associated with antigen processing (TAP) dependent way. This was done by expressing various influenza A-derived peptides containing the naturally processed epitope ASNENMDAM (366-374) preceded by the influenza hemagglutinin ER translocation sequence. Peptides derived from these minigenes that became associated with Db were isolated and identified by combined reversed phase liquid chromatography and detection by cytotoxic T lymphocytes. Our results establish that NH2-terminal extensions of at least 40 residues can be trimmed from peptides entering the ER, but that proteolysis of larger proteins may be limited.
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spelling oxford-uuid:f8b559f1-da2b-41fb-ae65-5369628fa1f52022-03-27T12:52:21ZProcessing of major histocompatibility class I-restricted antigens in the endoplasmic reticulum.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:f8b559f1-da2b-41fb-ae65-5369628fa1f5EnglishSymplectic Elements at Oxford1995Elliott, TWillis, ACerundolo, VTownsend, AWe have introduced long precursor peptides directly into the endoplasmic reticulum (ER) of a mutant cell line (T2-Db) that lacks the ability to transport peptides from the cytosol to the ER in a transporter associated with antigen processing (TAP) dependent way. This was done by expressing various influenza A-derived peptides containing the naturally processed epitope ASNENMDAM (366-374) preceded by the influenza hemagglutinin ER translocation sequence. Peptides derived from these minigenes that became associated with Db were isolated and identified by combined reversed phase liquid chromatography and detection by cytotoxic T lymphocytes. Our results establish that NH2-terminal extensions of at least 40 residues can be trimmed from peptides entering the ER, but that proteolysis of larger proteins may be limited.
spellingShingle Elliott, T
Willis, A
Cerundolo, V
Townsend, A
Processing of major histocompatibility class I-restricted antigens in the endoplasmic reticulum.
title Processing of major histocompatibility class I-restricted antigens in the endoplasmic reticulum.
title_full Processing of major histocompatibility class I-restricted antigens in the endoplasmic reticulum.
title_fullStr Processing of major histocompatibility class I-restricted antigens in the endoplasmic reticulum.
title_full_unstemmed Processing of major histocompatibility class I-restricted antigens in the endoplasmic reticulum.
title_short Processing of major histocompatibility class I-restricted antigens in the endoplasmic reticulum.
title_sort processing of major histocompatibility class i restricted antigens in the endoplasmic reticulum
work_keys_str_mv AT elliottt processingofmajorhistocompatibilityclassirestrictedantigensintheendoplasmicreticulum
AT willisa processingofmajorhistocompatibilityclassirestrictedantigensintheendoplasmicreticulum
AT cerundolov processingofmajorhistocompatibilityclassirestrictedantigensintheendoplasmicreticulum
AT townsenda processingofmajorhistocompatibilityclassirestrictedantigensintheendoplasmicreticulum