Optimization of the MHC class I peptide cargo is dependent on tapasin
Optimization of the MHC class I peptide cargo is dependent on tapasin
The loading of MHC class I molecules with their peptide cargo is undertaken by a multimolecular peptide loading complex within the endoplasmic reticulum. We show that MHC class I molecules can optimize their peptide repertoire over time and that this process is dependent on tapasin. Optimization of the peptide repertoire is both quantitatively and qualitatively improved by tapasin. The extent of optimization is maximal when MHC class I molecules are allowed to load within the fully assembled peptide loading complex. Finally, we identify a single natural polymorphism (116D>Y) in HLA-B*4402 that permits tapasin-independent loading of HLA-B*4405 (116Y). In the presence of tapasin, the tapasin-independent allele B*4405 (116Y) acquires a repertoire of peptides that is less optimal than the tapasin-dependent allele B*4402 (116D).
509-520
Williams, Anthony P.
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Peh, Chen Au
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Purcell, Anthony W.
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McCluskey, James
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Elliott, Tim
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April 2002
Williams, Anthony P.
973ff46f-46f1-4d7c-b27d-0f53221e4c44
Peh, Chen Au
b5832f49-ed3c-490b-98e0-1276f589e486
Purcell, Anthony W.
53398b33-0596-4288-9647-69cff610e97c
McCluskey, James
b1082fa3-75f2-4ab7-b574-ed1b7d0dac48
Elliott, Tim
16670fa8-c2f9-477a-91df-7c9e5b453e0e
Williams, Anthony P., Peh, Chen Au, Purcell, Anthony W., McCluskey, James and Elliott, Tim
(2002)
Optimization of the MHC class I peptide cargo is dependent on tapasin.
Immunity, 16 (4), .
(doi:10.1016/S1074-7613(02)00304-7).
Abstract
The loading of MHC class I molecules with their peptide cargo is undertaken by a multimolecular peptide loading complex within the endoplasmic reticulum. We show that MHC class I molecules can optimize their peptide repertoire over time and that this process is dependent on tapasin. Optimization of the peptide repertoire is both quantitatively and qualitatively improved by tapasin. The extent of optimization is maximal when MHC class I molecules are allowed to load within the fully assembled peptide loading complex. Finally, we identify a single natural polymorphism (116D>Y) in HLA-B*4402 that permits tapasin-independent loading of HLA-B*4405 (116Y). In the presence of tapasin, the tapasin-independent allele B*4405 (116Y) acquires a repertoire of peptides that is less optimal than the tapasin-dependent allele B*4402 (116D).
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Published date: April 2002
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Local EPrints ID: 26663
URI: http://eprints.soton.ac.uk/id/eprint/26663
ISSN: 1097-4180
PURE UUID: 3811981e-a224-4dcf-ab32-2c1f9d0fa8bd
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Date deposited: 21 Apr 2006
Last modified: 16 Mar 2024 03:19
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Author:
Chen Au Peh
Author:
Anthony W. Purcell
Author:
James McCluskey
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