Evidence map›Paper›PMID 33298915›Full record

ArticleNature communications2020

Thermostability profiling of MHC-bound peptides: a new dimension in immunopeptidomics and aid for immunotherapy design.

Emma C Jappe, Christian Garde, Sri H Ramarathinam, Ethan Passantino, Patricia T Illing, Nicole A Mifsud, Thomas Trolle, Jens V Kringelum, Nathan P Croft, Anthony W Purcell

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.1field-weighted citation impact, top 23% 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

16 citing papers in PubMed, 26 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
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 3 countries.

Emma C JappeEvaxion Biotech, Bredgade 34E, 1260, Copenhagen, Denmark.
Christian GardeEvaxion Biotech, Bredgade 34E, 1260, Copenhagen, Denmark.
Sri H RamarathinamDepartment of Biochemistry and Molecular Biology, Infection and Immunity Program, Biomedicine Discovery Institute, Monash University, Clayton, VIC, Australia.ORCID 0000-0002-2787-1282
Ethan PassantinoDepartment of Biochemistry and Molecular Biology, Infection and Immunity Program, Biomedicine Discovery Institute, Monash University, Clayton, VIC, Australia.
Patricia T IllingDepartment of Biochemistry and Molecular Biology, Infection and Immunity Program, Biomedicine Discovery Institute, Monash University, Clayton, VIC, Australia.ORCID 0000-0002-3870-0796
Nicole A MifsudDepartment of Biochemistry and Molecular Biology, Infection and Immunity Program, Biomedicine Discovery Institute, Monash University, Clayton, VIC, Australia.ORCID 0000-0001-8647-2102
Thomas TrolleEvaxion Biotech, Bredgade 34E, 1260, Copenhagen, Denmark.
Jens V KringelumEvaxion Biotech, Bredgade 34E, 1260, Copenhagen, Denmark. jkgm@evaxion-biotech.com.ORCID 0000-0002-7415-3283
Nathan P CroftDepartment of Biochemistry and Molecular Biology, Infection and Immunity Program, Biomedicine Discovery Institute, Monash University, Clayton, VIC, Australia. nathan.croft@monash.edu.ORCID 0000-0002-2128-5127
Anthony W PurcellDepartment of Biochemistry and Molecular Biology, Infection and Immunity Program, Biomedicine Discovery Institute, Monash University, Clayton, VIC, Australia. anthony.purcell@monash.edu.ORCID 0000-0003-0532-8331
Australian Regenerative Medicine Institute · AUDiscovery Institute · USGalaxy Biotech (United States) · USTechnical University of Denmark · DK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The features of peptide antigens that contribute to their immunogenicity are not well understood. Although the stability of peptide-MHC (pMHC) is known to be important, current assays assess this interaction only for peptides in isolation and not in the context of natural antigen processing and presentation. Here, we present a method that provides a comprehensive and unbiased measure of pMHC stability for thousands of individual ligands detected simultaneously by mass spectrometry (MS). The method allows rapid assessment of intra-allelic and inter-allelic differences in pMHC stability and reveals profiles of stability that are broader than previously appreciated. The additional dimensionality of the data facilitated the training of a model which improves the prediction of peptide immunogenicity, specifically of cancer neoepitopes. This assay can be applied to any cells bearing MHC or MHC-like molecules, offering insight into not only the endogenous immunopeptidome, but also that of neoepitopes and pathogen-derived sequences.

Indexed as

AllelesAntigen PresentationAntigens, NeoplasmCell LineDatasets as TopicGenes, MHC Class IHigh-Throughput Screening AssaysHistocompatibility Antigens Class IHot TemperatureHumansImmunotherapyLigandsNeoplasmsNeural Networks, ComputerPeptide LibraryPeptidesAntigens, NeoplasmHistocompatibility Antigens Class ILigandsPeptide LibraryPeptides

Identifiers

PMID33298915
PMCPMC7726561
OpenAlexW3111171599

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.