Evidence map›Paper›PMID 26439010›Full record

ArticleeLife2015

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

Clemens Hermann, Andy van Hateren, Nico Trautwein, Andreas Neerincx, Patrick J Duriez, Stefan Stevanović, John Trowsdale, Janet E Deane, Tim Elliott, Louise H Boyle

Open access · goldAbstract read
In one paragraph

Article in eLife, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.

0numbers the graph read from it
0cells of the map it votes in
59citing papers in PubMed
3.6field-weighted citation impact, top 6% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

59 citing papers in PubMed, 100 citations in OpenAlex.

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  14. Universal open MHC-I molecules for rapid peptide loading and enhanced complex stability across HLA allotypes.Proceedings of the National Academy of Sciences of the United States of America · 2023
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

10 authors at 4 institutions in 2 countries.

Clemens HermannDepartment of Pathology, University of Cambridge, Cambridge, United Kingdom.ORCID http://orcid.org/0000-0002-0009-9501
Andy van HaterenFaculty of Medicine and Institute for Life Science, University of Southampton, Southampton, United Kingdom.ORCID http://orcid.org/0000-0002-3915-0239
Nico TrautweinDepartment of Immunology, Eberhard Karls University Tübingen, Tübingen, Germany.ORCID http://orcid.org/0000-0003-3292-8850
Andreas NeerincxDepartment of Pathology, University of Cambridge, Cambridge, United Kingdom.ORCID http://orcid.org/0000-0002-6902-5383
Patrick J DuriezCancer Research UK Protein Core Facility, Faculty of Medicine, University of Southampton, Southampton, United Kingdom.ORCID http://orcid.org/0000-0003-1814-2552
Stefan StevanovićDepartment of Immunology, Eberhard Karls University Tübingen, Tübingen, Germany.ORCID http://orcid.org/0000-0003-1954-7762
John TrowsdaleDepartment of Pathology, University of Cambridge, Cambridge, United Kingdom.ORCID http://orcid.org/0000-0002-0150-5698
Janet E DeaneCambridge Institute for Medical Research, University of Cambridge, Cambridge, United Kingdom.ORCID http://orcid.org/0000-0002-4863-0330
Tim ElliottFaculty of Medicine and Institute for Life Science, University of Southampton, Southampton, United Kingdom.ORCID http://orcid.org/0000-0003-1097-0222
Louise H BoyleDepartment of Pathology, University of Cambridge, Cambridge, United Kingdom.ORCID http://orcid.org/0000-0002-3105-6555
University of Cambridge · GBUniversity of Southampton · GBUniversity of Tübingen · DECancer Research UK · GB

Funding

Cancer Research UK 16997Cancer Research UK C7056AMedical Research Council G0901682Wellcome Trust 085058Wellcome Trust 089563Wellcome Trust 089821Wellcome Trust 100140Wellcome Trust 104647
6 · The paper itself

Abstract

Our understanding of the antigen presentation pathway has recently been enhanced with the identification that the tapasin-related protein TAPBPR is a second major histocompatibility complex (MHC) class I-specific chaperone. We sought to determine whether, like tapasin, TAPBPR can also influence MHC class 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.

Indexed as

Antigen PresentationAntigensCell LineHistocompatibility Antigens Class IHumansImmunoglobulinsMembrane ProteinsPeptidesProtein BindingAntigensHistocompatibility Antigens Class IImmunoglobulinsMembrane ProteinsPeptidesTAPBPL protein, humanantigen processing and presentationcell biologyhumanimmunologyMHCpeptide repertoire

Identifiers

PMID26439010
PMCPMC4718805
OpenAlexW2204515846

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.