Evidence map›Paper›PMID 23468491›Full record

ArticleJournal of virology2013

The spike protein of the emerging betacoronavirus EMC uses a novel coronavirus receptor for entry, can be activated by TMPRSS2, and is targeted by neutralizing antibodies.

Stefanie Gierer, Stephanie Bertram, Franziska Kaup, Florian Wrensch, Adeline Heurich, Annika Krämer-Kühl, Kathrin Welsch, Michael Winkler, Benjamin Meyer, Christian Drosten and 5 more

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 246 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
246citing papers in PubMed, 1 pooled it
16.3field-weighted citation impact, top 1% 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

246 citing papers in PubMed, 1 synthesis or guideline pooled it, 350 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Review
  5. Article
  6. In Silico Analysis of CMolecules (Basel, Switzerland) · 2025
    Article
  7. Review
  8. Article
  9. Journal of virology · 2025
    Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. TMPRSS2-mediated SARS-CoV-2 uptake boosts innate immune activation, enhances cytopathology, and drives convergent virus evolution.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  18. Article
  19. Article
  20. Review

186 more citing papers are in PubMed but not listed here.

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

15 authors at 4 institutions in 2 countries.

Stefanie GiererInfection Biology Unit, German Primate Center, Göttingen, Germany.
Stephanie Bertram
Franziska Kaup
Florian Wrensch
Adeline Heurich
Annika Krämer-Kühl
Kathrin Welsch
Michael Winkler
Benjamin Meyer
Christian Drosten
Ulf Dittmer
Thomas von Hahn
Graham Simmons
Heike Hofmann
Stefan Pöhlmann
German Primate Center · DEBlood Systems Research Institute · USMedizinische Hochschule Hannover · DEUniversity of Duisburg-Essen · DE

Funding

Modeling viral entry and its inhibition using SARS-CoVR01AI074986 · NIAID · VITALANT · PI SIMMONS, GRAHAM · 2008 to 2012
$2.0M
NIAID NIH HHS R01 AI074986NIAID NIH HHS R01AI074986
6 · The paper itself

Abstract

The novel human coronavirus EMC (hCoV-EMC), which recently emerged in Saudi Arabia, is highly pathogenic and could pose a significant threat to public health. The elucidation of hCoV-EMC interactions with host cells is critical to our understanding of the pathogenesis of this virus and to the identification of targets for antiviral intervention. Here we investigated the viral and cellular determinants governing hCoV-EMC entry into host cells. We found that the spike protein of hCoV-EMC (EMC-S) is incorporated into lentiviral particles and mediates transduction of human cell lines derived from different organs, including the lungs, kidneys, and colon, as well as primary human macrophages. Expression of the known coronavirus receptors ACE2, CD13, and CEACAM1 did not facilitate EMC-S-driven transduction, suggesting that hCoV-EMC uses a novel receptor for entry. Directed protease expression and inhibition analyses revealed that TMPRSS2 and endosomal cathepsins activate EMC-S for virus-cell fusion and constitute potential targets for antiviral intervention. Finally, EMC-S-driven transduction was abrogated by serum from an hCoV-EMC-infected patient, indicating that EMC-S-specific neutralizing antibodies can be generated in patients. Collectively, our results indicate that hCoV-EMC uses a novel receptor for protease-activated entry into human cells and might be capable of extrapulmonary spread. In addition, they define TMPRSS2 and cathepsins B and L as potential targets for intervention and suggest that neutralizing antibodies contribute to the control of hCoV-EMC infection.

Indexed as

Host-Pathogen InteractionsVirus InternalizationAntibodies, NeutralizingAntibodies, ViralCathepsinsCoronavirusCoronavirus InfectionsHumansMembrane GlycoproteinsReceptors, CoronavirusReceptors, VirusSaudi ArabiaSerine EndopeptidasesSpike Glycoprotein, CoronavirusTransduction, GeneticViral Envelope ProteinsAntibodies, NeutralizingAntibodies, ViralCathepsinsMembrane GlycoproteinsReceptors, CoronavirusReceptors, VirusSerine EndopeptidasesSpike Glycoprotein, CoronavirusTMPRSS2 protein, humanViral Envelope Proteins

Identifiers

PMID23468491
PMCPMC3648152
OpenAlexW2098086455

What OpenQuestion holds

Textmetadata
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.