Evidence map›Paper›PMID 19717178›Full record

ArticleVirology2009

SARS-coronavirus spike S2 domain flanked by cysteine residues C822 and C833 is important for activation of membrane fusion.

Ikenna G Madu, Sandrine Belouzard, Gary R Whittaker

Abstract read
In one paragraph

Article in Virology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed, 1 pooled it
–field-weighted citation impact
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

31 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
  2. Trial
  3. Article
  4. Article
  5. Article
  6. Article
  7. Exploring antiviral and anti-inflammatory effects of thiol drugs in COVID-19.American journal of physiology. Lung cellular and molecular physiology · 2022
    Article
  8. Article
  9. Article
  10. Article
  11. Physico-Chemical Mechanisms of the Functioning of Membrane-Active Proteins of Enveloped Viruses.Biochemistry (Moscow) Supplement. Series A, Membrane and cell biology · 2022
    Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. CaBiophysical journal · 2021
    Article
  17. Review
  18. Article
  19. Ultra-large-scaleComputational and structural biotechnology journal · 2021
    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

3 authors.

Ikenna G MaduC4127 Veterinary Medical Center, Department of Microbiology and Immunology, Cornell University, Ithaca NY 14853, USA.
Sandrine Belouzard
Gary R Whittaker

Funding

Genome Scale Discovery of Mycobacterial Gene Function by Synthetic Genetic ArraysR21AI107258 · NIAID · WADSWORTH CENTER · PI DERBYSHIRE, KEITH M, GRAY, TODD · 2013 to 2014
$352k
Entry of Coronaviruses into Host CellsR03AI060946 · NIAID · CORNELL UNIVERSITY ITHACA · PI WHITTAKER, GARY R · 2004 to 2005
$158k
Characterizing Class 1 Fusion Proteins: Elucidation of Coronavirus fusion peptideF31GM082084 · NIGMS · CORNELL UNIVERSITY · PI MADU, IKENNA G · 2007 to 2009
$97k
NIAID NIH HHS R03 AI060946NIAID NIH HHS R21 AI107258NIAID NIH HHS R21 AI1076258NIGMS NIH HHS F31 GM082084
6 · The paper itself

Abstract

The S2 domain of the coronavirus spike (S) protein is known to be responsible for mediating membrane fusion. In addition to a well-recognized cleavage site at the S1-S2 boundary, a second proteolytic cleavage site has been identified in the severe acute respiratory syndrome coronavirus (SARS-CoV) S2 domain (R797). C-terminal to this S2 cleavage site is a conserved region flanked by cysteine residues C822 and C833. Here, we investigated the importance of this well conserved region for SARS-CoV S-mediated fusion activation. We show that the residues between C822-C833 are well conserved across all coronaviruses. Mutagenic analysis of SARS-CoV S, combined with cell-cell fusion and pseudotyped virion infectivity assays, showed a critical role for the core-conserved residues C822, D830, L831, and C833. Based on available predictive models, we propose that the conserved domain flanked by cysteines 822 and 833 forms a loop structure that interacts with components of the SARS-CoV S trimer to control the activation of membrane fusion.

Indexed as

Membrane FusionAmino Acid SequenceAnimalsCell FusionCell LineChlorocebus aethiopsConserved SequenceCricetinaeCysteineHumansMembrane GlycoproteinsMolecular Sequence DataMutagenesis, Site-DirectedSevere acute respiratory syndrome-related coronavirusSpike Glycoprotein, CoronavirusViral Envelope ProteinsCysteineMembrane GlycoproteinsSpike Glycoprotein, Coronavirusspike glycoprotein, SARS-CoVspike protein, mouse hepatitis virusViral Envelope Proteins

Identifiers

PMID19717178
PMCPMC3594805

What OpenQuestion holds

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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.