Evidence map›Paper›PMID 37818801›Full record

ArticleEMBO reports2023

Tetherin antagonism by SARS-CoV-2 ORF3a and spike protein enhances virus release.

Hazel Stewart, Roberta Palmulli, Kristoffer H Johansen, Naomi McGovern, Ola M Shehata, George W Carnell, Hannah K Jackson, Jin S Lee, Jonathan C Brown, Thomas Burgoyne and 5 more

Open access · hybridAbstract read
In one paragraph

Article in EMBO reports, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
5.6field-weighted citation impact, top 3% 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

21 citing papers in PubMed, 29 citations in OpenAlex.

  1. Trial
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  4. Host Responses to SARS-CoV-2 with an Emphasis on Cytokines.International journal of molecular sciences · 2026
    Review
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

15 authors at 5 institutions in 2 countries.

Hazel StewartDepartment of Pathology, University of Cambridge, Cambridge, UK.ORCID 0000-0003-1438-1089
Roberta PalmulliDepartment of Pathology, University of Cambridge, Cambridge, UK.ORCID 0000-0003-2271-3186
Kristoffer H JohansenDepartment of Pathology, University of Cambridge, Cambridge, UK.ORCID 0000-0002-7711-9451
Naomi McGovernDepartment of Pathology, University of Cambridge, Cambridge, UK.ORCID 0000-0001-5200-2698
Ola M ShehataDepartment of Biomedical Science, University of Sheffield, Firth Court, Sheffield, UK.
George W CarnellDepartment of Veterinary Medicine, University of Cambridge, Cambridge, UK.
Hannah K JacksonDepartment of Pathology, University of Cambridge, Cambridge, UK.ORCID 0000-0002-4090-0885
Jin S LeeDepartment of Pathology, University of Cambridge, Cambridge, UK.ORCID 0009-0004-4851-3806
Jonathan C BrownDepartment of Infectious Disease, Imperial College London, London, UK.ORCID 0000-0001-6849-3962
Thomas BurgoyneRoyal Brompton Hospital, Guy's and St Thomas' NHS Foundation Trust, London, UK.
Jonathan L HeeneyDepartment of Veterinary Medicine, University of Cambridge, Cambridge, UK.
Klaus OkkenhaugDepartment of Pathology, University of Cambridge, Cambridge, UK.ORCID 0000-0002-9432-4051
Andrew E FirthDepartment of Pathology, University of Cambridge, Cambridge, UK.
Andrew A PedenDepartment of Biomedical Science, University of Sheffield, Firth Court, Sheffield, UK.ORCID 0000-0003-0144-7712
James R EdgarDepartment of Pathology, University of Cambridge, Cambridge, UK.ORCID 0000-0001-7903-8199
University of Cambridge · GBUniversity of Sheffield · GBGuy's and St Thomas' NHS Foundation Trust · GBImperial College London · GBNational Institutes of Health · US

Funding

Wellcome TrustWellcome Trust 106207Wellcome Trust 200925/Z/16/ZWellcome Trust 204464/Z/16/ZWellcome Trust 216370/Z/19/ZWellcome Trust 220814
6 · The paper itself

Abstract

The antiviral restriction factor, tetherin, blocks the release of several different families of enveloped viruses, including the Coronaviridae. Tetherin is an interferon-induced protein that forms parallel homodimers between the host cell and viral particles, linking viruses to the surface of infected cells and inhibiting their release. We demonstrate that SARS-CoV-2 infection causes tetherin downregulation and that tetherin depletion from cells enhances SARS-CoV-2 viral titres. We investigate the potential viral proteins involved in abrogating tetherin function and find that SARS-CoV-2 ORF3a reduces tetherin localisation within biosynthetic organelles where Coronaviruses bud, and increases tetherin localisation to late endocytic organelles via reduced retrograde recycling. We also find that expression of Spike protein causes a reduction in cellular tetherin levels. Our results confirm that tetherin acts as a host restriction factor for SARS-CoV-2 and highlight the multiple distinct mechanisms by which SARS-CoV-2 subverts tetherin function.

Indexed as

Bone Marrow Stromal Antigen 2COVID-19SARS-CoV-2Spike Glycoprotein, CoronavirusVirus ReleaseGPI-Linked ProteinsHumansViroporin ProteinsBone Marrow Stromal Antigen 2GPI-Linked ProteinsORF3a protein, SARS-CoV-2Spike Glycoprotein, Coronavirusspike protein, SARS-CoV-2Viroporin ProteinsORF3arestriction factorSARS-CoV-2spiketetherin

Identifiers

PMID37818801
PMCPMC10702813
OpenAlexW4387564196

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.