Evidence map›Paper›PMID 17957264›Full record

ArticlePloS one2007

Conformational reorganization of the SARS coronavirus spike following receptor binding: implications for membrane fusion.

Daniel R Beniac, Shauna L deVarennes, Anton Andonov, Runtao He, Tim F Booth

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2007. 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
1.9field-weighted citation impact, top 15% 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, 59 citations in OpenAlex.

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  13. COVID-19: Risk groups, mechanistic insights and challenges.International journal of clinical practice · 2020
    Article
  14. Article
  15. Review
  16. Structural insights into coronavirus entry.Advances in virus research · 2019
    Article
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  18. Article
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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 1 country.

Daniel R BeniacViral Diseases Division, National Microbiology Laboratory, Public Health Agency of Canada, Winnipeg, Manitoba, Canada.
Shauna L deVarennes
Anton Andonov
Runtao He
Tim F Booth
University of Manitoba · CAPublic Health Agency of Canada · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The SARS coronavirus (SARS-CoV) spike is the largest known viral spike molecule, and shares a similar function with all class 1 viral fusion proteins. Previous structural studies of membrane fusion proteins have largely used crystallography of static molecular fragments, in isolation of their transmembrane domains. In this study we have produced purified, irradiated SARS-CoV virions that retain their morphology, and are fusogenic in cell culture. We used cryo-electron microscopy and image processing to investigate conformational changes that occur in the entire spike of intact virions when they bind to the viral receptor, angiotensin-converting enzyme 2 (ACE2). We have shown that ACE2 binding results in structural changes that appear to be the initial step in viral membrane fusion, and precisely localized the receptor-binding and fusion core domains within the entire spike. Furthermore, our results show that receptor binding and subsequent membrane fusion are distinct steps, and that each spike can bind up to three ACE2 molecules. The SARS-CoV spike provides an ideal model system to study receptor binding and membrane fusion in the native state, employing cryo-electron microscopy and single-particle image analysis.

Indexed as

Angiotensin-Converting Enzyme 2AnimalsChlorocebus aethiopsCryoelectron MicroscopyHumansImage Processing, Computer-AssistedMembrane FusionMembrane GlycoproteinsMicroscopy, ImmunoelectronModels, MolecularMolecular ConformationPeptidyl-Dipeptidase AProtein BindingProtein ConformationSevere acute respiratory syndrome-related coronavirusSpike Glycoprotein, CoronavirusACE2 protein, humanAngiotensin-Converting Enzyme 2Membrane GlycoproteinsPeptidyl-Dipeptidase ASpike Glycoprotein, Coronavirusspike glycoprotein, SARS-CoVViral Envelope Proteins

Identifiers

PMID17957264
PMCPMC2034598
OpenAlexW2081598467

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.