The University of Southampton
University of Southampton Institutional Repository

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

TAPBPR alters MHC class I peptide presentation by functioning as a peptide exchange catalyst
TAPBPR alters MHC class I peptide presentation by functioning as a peptide exchange catalyst
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.
2050-084X
1-22
Hermann, Clemens
978cedee-4017-43e9-86a7-4665636ce553
Van Hateren, Andy
e345fa3c-d89c-4b91-947e-c1d818cc7f71
Trautwein, Nico
2387bf8d-9384-4edb-93e7-3cefe5021ae7
Neerincx, Andreas
e487d7b5-1d13-4847-83b2-67fc2754c238
Duriez, Patrick J.
4cf499bc-007a-43b3-b180-d6e5dc3d151b
Stevanović, Stefan
e09af639-b73f-459b-b111-55a6c722b03d
Trowsdale, John
5bbacc4a-45f4-4376-8357-a7c79fc4fe12
Deane, Janet E.
dd93a448-fe81-4c8b-884e-a396ada0cebd
Elliott, Tim
16670fa8-c2f9-477a-91df-7c9e5b453e0e
Boyle, Louise H.
e2afc84e-3524-417d-a54b-4f7f7d753866
Hermann, Clemens
978cedee-4017-43e9-86a7-4665636ce553
Van Hateren, Andy
e345fa3c-d89c-4b91-947e-c1d818cc7f71
Trautwein, Nico
2387bf8d-9384-4edb-93e7-3cefe5021ae7
Neerincx, Andreas
e487d7b5-1d13-4847-83b2-67fc2754c238
Duriez, Patrick J.
4cf499bc-007a-43b3-b180-d6e5dc3d151b
Stevanović, Stefan
e09af639-b73f-459b-b111-55a6c722b03d
Trowsdale, John
5bbacc4a-45f4-4376-8357-a7c79fc4fe12
Deane, Janet E.
dd93a448-fe81-4c8b-884e-a396ada0cebd
Elliott, Tim
16670fa8-c2f9-477a-91df-7c9e5b453e0e
Boyle, Louise H.
e2afc84e-3524-417d-a54b-4f7f7d753866

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).

Record type: Article

Abstract

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.

PDF 2015 TAPBPR alters MHC class I peptide presentation by functioning as a peptide exchange catalyst.pdf - Other
Download (21MB)
PDF elife-09617-v2.pdf - Version of Record
Available under License Creative Commons Attribution.
Download (2MB)

More information

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

Identifiers

Local EPrints ID: 384902
URI: http://eprints.soton.ac.uk/id/eprint/384902
ISSN: 2050-084X
PURE UUID: 0fac4a58-9164-42e9-8efb-f5ffdb8e3a17
ORCID for Tim Elliott: ORCID iD orcid.org/0000-0003-1097-0222

Catalogue record

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

Export record

Altmetrics

Contributors

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

University divisions

Download statistics

Downloads from ePrints over the past year. Other digital versions may also be available to download e.g. from the publisher's website.

View more statistics

Atom RSS 1.0 RSS 2.0

Contact ePrints Soton: eprints@soton.ac.uk

ePrints Soton supports OAI 2.0 with a base URL of http://eprints.soton.ac.uk/cgi/oai2

This repository has been built using EPrints software, developed at the University of Southampton, but available to everyone to use.

We use cookies to ensure that we give you the best experience on our website. If you continue without changing your settings, we will assume that you are happy to receive cookies on the University of Southampton website.

×