Evidence map›Paper›PMID 32518267›Full record

ArticleNature communications2020

Structural basis for oligoclonal T cell recognition of a shared p53 cancer neoantigen.

Daichao Wu, D Travis Gallagher, Ragul Gowthaman, Brian G Pierce, Roy A Mariuzza

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 57 papers.

0numbers the graph read from it
0cells of the map it votes in
57citing papers in PubMed
3.5field-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

57 citing papers in PubMed, 74 citations in OpenAlex.

  1. Article
  2. A p53Molecular therapy. Oncology · 2026
    Article
  3. Structural basis for T-cell receptor recognition of p53Acta crystallographica. Section D, Structural biology · 2026
    Article
  4. Review
  5. Revisiting tumor immunogenicity through the lens of mutant p53: Implications for cancer immunotherapy.Apoptosis : an international journal on programmed cell death · 2026
    Review
  6. The AUTACE That Degrades KRAS and Engages CD8Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  7. Article
  8. Review
  9. Molecular origin, discovery, validation and application of neoantigens.Asian journal of pharmaceutical sciences · 2026
    Review
  10. Article
  11. Review
  12. Article
  13. Article
  14. Review
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. 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

5 authors at 2 institutions in 2 countries.

Daichao WuW.M. Keck Laboratory for Structural Biology, University of Maryland Institute for Bioscience and Biotechnology Research, Rockville, MD, 20850, USA.
D Travis GallagherW.M. Keck Laboratory for Structural Biology, University of Maryland Institute for Bioscience and Biotechnology Research, Rockville, MD, 20850, USA.
Ragul GowthamanW.M. Keck Laboratory for Structural Biology, University of Maryland Institute for Bioscience and Biotechnology Research, Rockville, MD, 20850, USA.ORCID http://orcid.org/0000-0002-0008-6401
Brian G PierceW.M. Keck Laboratory for Structural Biology, University of Maryland Institute for Bioscience and Biotechnology Research, Rockville, MD, 20850, USA.ORCID http://orcid.org/0000-0003-4821-0368
Roy A MariuzzaW.M. Keck Laboratory for Structural Biology, University of Maryland Institute for Bioscience and Biotechnology Research, Rockville, MD, 20850, USA. rmariuzz@umd.edu.
Advanced Bioscience Laboratories (United States) · USNational Institute of Standards and Technology · US

Funding

Structure and Activation of a Multiprotein Signaling ComplexR01AI129893 · NIAID · UNIV OF MARYLAND, COLLEGE PARK · PI MARIUZZA, ROY A, ORBAN, JOHN · 2017 to 2021
$3.5M
High Resolution Modeling and Design of T-Cell ReceptorsR01GM126299 · NIGMS · UNIV OF MARYLAND, COLLEGE PARK · PI PIERCE, BRIAN G. · 2018 to 2021
$1.3M
NIAID NIH HHS R01 AI129893NIGMS NIH HHS R01 GM126299
6 · The paper itself

Abstract

Adoptive cell therapy (ACT) with tumor-specific T cells can mediate cancer regression. The main target of tumor-specific T cells are neoantigens arising from mutations in self-proteins. Although the majority of cancer neoantigens are unique to each patient, and therefore not broadly useful for ACT, some are shared. We studied oligoclonal T-cell receptors (TCRs) that recognize a shared neoepitope arising from a driver mutation in the p53 oncogene (p53R175H) presented by HLA-A2. Here we report structures of wild-type and mutant p53-HLA-A2 ligands, as well as structures of three tumor-specific TCRs bound to p53R175H-HLA-A2. These structures reveal how a driver mutation in p53 rendered a self-peptide visible to T cells. The TCRs employ structurally distinct strategies that are highly focused on the mutation to discriminate between mutant and wild-type p53. The TCR-p53R175H-HLA-A2 complexes provide a framework for designing TCRs to improve potency for ACT without sacrificing specificity.

Indexed as

MutationAntigens, NeoplasmBinding SitesBiotinylationCodonCrystallography, X-RayEpitopesEscherichia coliHLA-A2 AntigenHumansImmunotherapy, AdoptiveLigandsLymphocytes, Tumor-InfiltratingNeoplasmsPeptidesProtein BindingAntigens, NeoplasmCodonEpitopesHLA-A2 AntigenLigandsPeptidesReceptors, Antigen, T-CellTP53 protein, humanTumor Suppressor Protein p53

Identifiers

PMID32518267
PMCPMC7283474
OpenAlexW3033239458

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.