Evidence map›Paper›PMID 34949827›Full record

ArticleNature microbiology2022

Molecular mimicry of NF-κB by vaccinia virus protein enables selective inhibition of antiviral responses.

Jonas D Albarnaz, Hongwei Ren, Alice A Torres, Evgeniya V Shmeleva, Carlos A Melo, Andrew J Bannister, Matthew P Brember, Betty Y-W Chung, Geoffrey L Smith

Open access · bronzeAbstract read
In one paragraph

Article in Nature microbiology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
7.4field-weighted citation impact, top 2% 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

32 citing papers in PubMed, 55 citations in OpenAlex.

  1. Oncolytic viruses: advanced strategies in cancer therapy.Signal transduction and targeted therapy · 2026
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  4. Cytokine Storm Induction Linked to Multi-Organ Failure in Fatal Jellyfish Stings.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Article
  5. Review
  6. Review
  7. Article
  8. Review
  9. Article
  10. Frontiers in immunology · 2025
    Article
  11. Article
  12. Article
  13. Review
  14. Review
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article
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

9 authors at 1 institution in 1 country.

Jonas D AlbarnazDepartment of Pathology, University of Cambridge, Cambridge, UK. jd732@cam.ac.uk.ORCID http://orcid.org/0000-0002-8792-813X
Hongwei RenDepartment of Pathology, University of Cambridge, Cambridge, UK.
Alice A TorresDepartment of Pathology, University of Cambridge, Cambridge, UK.ORCID http://orcid.org/0000-0003-2352-2584
Evgeniya V ShmelevaDepartment of Pathology, University of Cambridge, Cambridge, UK.ORCID http://orcid.org/0000-0002-7654-2960
Carlos A MeloThe Gurdon Institute, University of Cambridge, Cambridge, UK.
Andrew J BannisterThe Gurdon Institute, University of Cambridge, Cambridge, UK.ORCID http://orcid.org/0000-0002-6312-4436
Matthew P BremberDepartment of Pathology, University of Cambridge, Cambridge, UK.
Betty Y-W ChungDepartment of Pathology, University of Cambridge, Cambridge, UK.
Geoffrey L SmithDepartment of Pathology, University of Cambridge, Cambridge, UK. gls37@cam.ac.uk.ORCID http://orcid.org/0000-0002-3730-9955
University of Cambridge · GB

Funding

Biotechnology and Biological Sciences Research Council BB/V017780.1Cancer Research UK 17001Medical Research Council MR/M019810/1Medical Research Council MR/R021821/1Wellcome Trust 090315
6 · The paper itself

Abstract

Infection of mammalian cells with viruses activates NF-κB to induce the expression of cytokines and chemokines and initiate an antiviral response. Here, we show that a vaccinia virus protein mimics the transactivation domain of the p65 subunit of NF-κB to inhibit selectively the expression of NF-κB-regulated genes. Using co-immunoprecipitation assays, we found that the vaccinia virus protein F14 associates with NF-κB co-activator CREB-binding protein (CBP) and disrupts the interaction between p65 and CBP. This abrogates CBP-mediated acetylation of p65, after which it reduces promoter recruitment of the transcriptional regulator BRD4 and diminishes stimulation of NF-κB-regulated genes CXCL10 and CCL2. Recruitment of BRD4 to the promoters of NFKBIA and CXCL8 remains unaffected by either F14 or JQ1 (a competitive inhibitor of BRD4 bromodomains), indicating that BRD4 recruitment is acetylation-independent. Unlike other viral proteins that are general antagonists of NF-κB, F14 is a selective inhibitor of NF-κB-dependent gene expression. An in vivo model of infection demonstrated that F14 promotes virulence. Molecular mimicry of NF-κB may be conserved because other orthopoxviruses, including variola, monkeypox and cowpox viruses, encode orthologues of F14.

Indexed as

Molecular MimicryCREB-Binding ProteinHEK293 CellsHost-Pathogen InteractionsHumansNF-kappa BSignal TransductionTranscription, GeneticVacciniaVaccinia virusViral ProteinsCREB-Binding ProteinCREBBP protein, humanNF-kappa BViral Proteins

Identifiers

PMID34949827
PMCPMC7614822
OpenAlexW4200062256

What Socratic holds

Textmetadata
LicenceTDM
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 Socratic graph.