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Optimization of the MHC class I peptide cargo is dependent on tapasin

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).
1097-4180
509-520
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.
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), pp. 509-520. (doi:10.1016/S1074-7613(02)00304-7).

Record type: Article

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

Identifiers

Local EPrints ID: 26663
URI: http://eprints.soton.ac.uk/id/eprint/26663
ISSN: 1097-4180
PURE UUID: 3811981e-a224-4dcf-ab32-2c1f9d0fa8bd
ORCID for Tim Elliott: ORCID iD orcid.org/0000-0003-1097-0222

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Date deposited: 21 Apr 2006
Last modified: 17 Jul 2017 16:06

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Contributors

Author: Chen Au Peh
Author: Anthony W. Purcell
Author: James McCluskey
Author: Tim Elliott ORCID iD

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