Evidence map›Paper›PMID 24554652›Full record

ArticleJournal of virology2014

Identification and characterization of a proteolytically primed form of the murine coronavirus spike proteins after fusion with the target cell.

Oliver Wicht, Christine Burkard, Cornelis A M de Haan, Frank J M van Kuppeveld, Peter J M Rottier, Berend Jan Bosch

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
2.3field-weighted citation impact, top 11% 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

24 citing papers in PubMed, 28 citations in OpenAlex.

  1. TMPRSS2-mediated coronavirus spike activation and inhibition.Nature structural & molecular biology · 2026
    Article
  2. Review
  3. SARS-CoV-2 spike engagement of ACE2 primes S2' site cleavage and fusion initiation.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  4. Review
  5. The role of high cholesterol in age-related COVID19 lethality.bioRxiv : the preprint server for biology · 2021
    Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Proteolytic processing of Middle East respiratory syndrome coronavirus spikes expands virus tropism.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  17. Article
  18. Fusion of Enveloped Viruses in Endosomes.Traffic (Copenhagen, Denmark) · 2016
    Review
  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

6 authors at 1 institution in 1 country.

Oliver WichtVirology Division, Department of Infectious Diseases and Immunology, Faculty of Veterinary Medicine, Utrecht University, Utrecht, The Netherlands.
Christine Burkard
Cornelis A M de Haan
Frank J M van Kuppeveld
Peter J M Rottier
Berend Jan Bosch
Utrecht University · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

unlabelledEnveloped viruses carry highly specialized glycoproteins that catalyze membrane fusion under strict spatial and temporal control. To prevent premature activation after biosynthesis, viral class I fusion proteins adopt a locked conformation and require proteolytic cleavage to render them fusion-ready. This priming step may occur during virus exit from the infected cell, in the extracellular milieu or during entry at or in the next target cell. Proteolytic processing of coronavirus spike (S) fusion proteins during virus entry has been suggested but not yet formally demonstrated, while the nature and functionality of the resulting subunit is still unclear. We used a prototype coronavirus--mouse hepatitis virus (MHV)--to develop a conditional biotinylation assay that enables the specific identification and biochemical characterization of viral S proteins on virions that mediated membrane fusion with the target cell. We demonstrate that MHV S proteins are indeed cleaved upon virus endocytosis, and we identify a novel processing product S2* with characteristics of a fusion-active subunit. The precise cleavage site and the enzymes involved remain to be elucidated. IMPORTANCE: Virus entry determines the tropism and is a crucial step in the virus life cycle. We developed an approach to characterize structural components of virus particles after entering new target cells. A prototype coronavirus was used to illustrate how the virus fusion machinery can be controlled.

Indexed as

EndocytosisProtein Processing, Post-TranslationalVirus InternalizationAnimalsMiceMurine hepatitis virusProteolysisSpike Glycoprotein, CoronavirusSpike Glycoprotein, Coronavirus

Identifiers

PMID24554652
PMCPMC3993802
OpenAlexW2170024189

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.