Evidence map›Paper›PMID 27431907›Full record

ArticleScientific reports2016

Influenza viral membrane fusion is sensitive to sterol concentration but surprisingly robust to sterol chemical identity.

Katarzyna E Zawada, Dominik Wrona, Robert J Rawle, Peter M Kasson

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.7field-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

17 citing papers in PubMed, 33 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. The Art of Viral Membrane Fusion and Penetration.Sub-cellular biochemistry · 2023
    Article
  6. Review
  7. Article
  8. Review
  9. Article
  10. Review
  11. Article
  12. Review
  13. Article
  14. Article
  15. Single-particle fusion of influenza viruses reveals complex interactions with target membranes.Journal of physics. Condensed matter : an Institute of Physics journal · 2018
    Article
  16. Phosphatidylcholine Membrane Fusion Is pH-Dependent.International journal of molecular sciences · 2018
    Article
  17. 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

4 authors at 1 institution in 1 country.

Katarzyna E ZawadaDepartments of Molecular Physiology and Biological Physics and of Biomedical Engineering, University of Virginia, Charlottesville, VA 22908, United States.
Dominik WronaDepartments of Molecular Physiology and Biological Physics and of Biomedical Engineering, University of Virginia, Charlottesville, VA 22908, United States.
Robert J RawleDepartments of Molecular Physiology and Biological Physics and of Biomedical Engineering, University of Virginia, Charlottesville, VA 22908, United States.
Peter M KassonDepartments of Molecular Physiology and Biological Physics and of Biomedical Engineering, University of Virginia, Charlottesville, VA 22908, United States.
University of Virginia · US

Funding

Molecular Electron Microscopy Core Facility ImprovementsG20RR031199 · NCRR · UNIVERSITY OF VIRGINIA · PI SHUPNIK, MARGARET A · 2010 to 2010
$2.0M
Understanding fusion peptide mutations in influenza hemagglutininR01GM098304 · NIGMS · UNIVERSITY OF VIRGINIA · PI KASSON, PETER M · 2012 to 2016
$1.7M
NCRR NIH HHS G20 RR031199NIGMS NIH HHS R01 GM098304
6 · The paper itself

Abstract

Influenza virions are enriched in cholesterol relative to the plasma membrane from which they bud. Previous work has shown that fusion between influenza virus and synthetic liposomes is sensitive to the amount of cholesterol in either the virus or the target membrane. Here, we test the chemical properties of cholesterol required to promote influenza fusion by replacing cholesterol with other sterols and assaying viral fusion kinetics. We find that influenza fusion with liposomes is surprisingly robust to sterol chemical identity, showing no significant dependence on sterol identity in target membranes for any of the sterols tested. In the viral membrane, lanosterol slowed fusion somewhat, while polar sterols produced a more pronounced slowing and inhibition of fusion. No other sterols tested showed a significant perturbation in fusion rates, including ones previously shown to alter membrane bending moduli or phase behavior. Although fusion rates depend on viral cholesterol, they thus do not require cholesterol's ability to support liquid-liquid phase coexistence. Using electron cryo-microscopy, we further find that sterol-dependent changes to hemagglutinin spatial patterning in the viral membrane do not require liquid-liquid phase coexistence. We therefore speculate that local sterol-hemagglutinin interactions in the viral envelope may control the rate-limiting step of fusion.

Indexed as

Membrane FusionAnimalsbeta-CyclodextrinsCell MembraneCholesterolCryoelectron MicroscopyDogsHemagglutinins, ViralInfluenza A Virus, H3N2 SubtypeKineticsLiposomesMadin Darby Canine Kidney CellsMembrane LipidsMolecular Dynamics SimulationMolecular StructureSterolsbeta-CyclodextrinsCholesterolHemagglutinins, ViralLiposomesMembrane Lipidsmethyl-beta-cyclodextrinSterols

Identifiers

PMID27431907
PMCPMC4949436
OpenAlexW2488366216

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.