Evidence map›Paper›PMID 17134730›Full record

ArticleVirology2007

Palmitoylation of the cysteine-rich endodomain of the SARS-coronavirus spike glycoprotein is important for spike-mediated cell fusion.

Chad M Petit, Vladimir N Chouljenko, Arun Iyer, Robin Colgrove, Michael Farzan, David M Knipe, K G Kousoulas

Open access · greenAbstract read
In one paragraph

Article in Virology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 96 papers.

0numbers the graph read from it
0cells of the map it votes in
96citing papers in PubMed
1.4field-weighted citation impact, top 21% 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

96 citing papers in PubMed, 147 citations in OpenAlex.

  1. Review
  2. Review
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  6. Perturbation ofJournal of virology · 2025
    Article
  7. Article
  8. State-of-the-Art Molecular Biophysics in Russia.International journal of molecular sciences · 2024
    Article
  9. Virus-Induced Cell Fusion and Syncytia Formation.Results and problems in cell differentiation · 2024
    Article
  10. Article
  11. Inconspicuous Yet Indispensable: The Coronavirus Spike Transmembrane Domain.International journal of molecular sciences · 2023
    Review
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Review
  18. Review
  19. Lipid and Lipidation in Membrane Fusion.The Journal of membrane biology · 2022
    Review
  20. Article

36 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

7 authors at 3 institutions in 1 country.

Chad M PetitDivision of Biotechnology and Molecular Medicine (BIOMMED), USA.
Vladimir N Chouljenko
Arun Iyer
Robin Colgrove
Michael Farzan
David M Knipe
K G Kousoulas
Louisiana State University · USHarvard University · USBrigham and Women's Hospital · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The SARS-coronavirus (SARS-CoV) is the etiological agent of the severe acute respiratory syndrome (SARS). The SARS-CoV spike (S) glycoprotein mediates membrane fusion events during virus entry and virus-induced cell-to-cell fusion. The cytoplasmic portion of the S glycoprotein contains four cysteine-rich amino acid clusters. Individual cysteine clusters were altered via cysteine-to-alanine amino acid replacement and the modified S glycoproteins were tested for their transport to cell-surfaces and ability to cause cell fusion in transient transfection assays. Mutagenesis of the cysteine cluster I, located immediately proximal to the predicted transmembrane, domain did not appreciably reduce cell-surface expression, although S-mediated cell fusion was reduced by more than 50% in comparison to the wild-type S. Similarly, mutagenesis of the cysteine cluster II located adjacent to cluster I reduced S-mediated cell fusion by more than 60% compared to the wild-type S, while cell-surface expression was reduced by less than 20%. Mutagenesis of cysteine clusters III and IV did not appreciably affect S cell-surface expression or S-mediated cell fusion. The wild-type S was palmitoylated as evidenced by the efficient incorporation of (3)H-palmitic acid in wild-type S molecules. S glycoprotein palmitoylation was significantly reduced for mutant glycoproteins having cluster I and II cysteine changes, but was largely unaffected for cysteine cluster III and IV mutants. These results show that the S cytoplasmic domain is palmitoylated and that palmitoylation of the membrane proximal cysteine clusters I and II may be important for S-mediated cell fusion.

Indexed as

Cell FusionMembrane FusionProtein Processing, Post-TranslationalAmino Acid SequenceAnimalsCell MembraneChlorocebus aethiopsCysteineImmunohistochemistryIsotope LabelingMembrane GlycoproteinsMolecular Sequence DataMutagenesis, Site-DirectedPalmitic AcidSevere acute respiratory syndrome-related coronavirusSpike Glycoprotein, CoronavirusCysteineMembrane GlycoproteinsPalmitic AcidSpike Glycoprotein, Coronavirusspike glycoprotein, SARS-CoVTritiumViral Envelope Proteins

Identifiers

PMID17134730
PMCPMC7103323
OpenAlexW2025200316

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.