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TAPBPR alters MHC class I peptide presentation by functioning as a peptide exchange catalyst

Record type: Article

Our understanding of the antigen presentation pathway has recently been enhanced with the identification that the tapasin-related protein TAPBPR is a second MHC I-specific chaperone. We sought to determine whether, like tapasin, TAPBPR can also influence MHC I peptide selection by functioning as a peptide exchange catalyst. We show that TAPBPR can catalyse the dissociation of peptides from peptide-MHC I complexes, enhance the loading of peptide-receptive MHC I molecules, and discriminate between peptides based on affinity in vitro. In cells, the depletion of TAPBPR increased the diversity of peptides presented on MHC I molecules, suggesting that TAPBPR is involved in restricting peptide presentation. Our results suggest TAPBPR binds to MHC I in a peptide-receptive state and, like tapasin, works to enhance peptide optimisation. It is now clear there are two MHC class I specific peptide editors, tapasin and TAPBPR, intimately involved in controlling peptide presentation to the immune system.

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Hermann, Clemens, Van Hateren, Andy, Trautwein, Nico, Neerincx, Andreas, Duriez, Patrick J., Stevanović, Stefan, Trowsdale, John, Deane, Janet E., Elliott, Tim and Boyle, Louise H. (2015) TAPBPR alters MHC class I peptide presentation by functioning as a peptide exchange catalyst eLife, 4, (e09617), pp. 1-22. (doi:10.7554/eLife.09617.001). (PMID:26439010).

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Accepted/In Press date: 5 October 2015
Published date: 6 October 2015
Organisations: Southampton Cancer Research UK Centre, Cancer Sciences


Local EPrints ID: 384902
ISSN: 2050-084X
PURE UUID: 0fac4a58-9164-42e9-8efb-f5ffdb8e3a17
ORCID for Tim Elliott: ORCID iD

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Date deposited: 15 Dec 2015 14:44
Last modified: 17 Jul 2017 20:01

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Author: Clemens Hermann
Author: Andy Van Hateren
Author: Nico Trautwein
Author: Andreas Neerincx
Author: Patrick J. Duriez
Author: Stefan Stevanović
Author: John Trowsdale
Author: Janet E. Deane
Author: Tim Elliott ORCID iD
Author: Louise H. Boyle

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