Evidence map›Paper›PMID 25703376›Full record

ArticleStructure (London, England : 1993)2015

Nothing to sneeze at: a dynamic and integrative computational model of an influenza A virion.

Tyler Reddy, David Shorthouse, Daniel L Parton, Elizabeth Jefferys, Philip W Fowler, Matthieu Chavent, Marc Baaden, Mark S P Sansom

Open access · hybridAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
10.5field-weighted citation impact, top 1% 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

45 citing papers in PubMed, 102 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Review
  5. Article
  6. Understanding Virus Structure and Dynamics through Molecular Simulations.Journal of chemical theory and computation · 2023
    Review
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Assembly and Analysis of Cell-Scale Membrane Envelopes.Journal of chemical information and modeling · 2022
    Article
  14. Article
  15. Visualising Viruses.The Journal of general virology · 2022
    Review
  16. Review
  17. Article
  18. Article
  19. Article
  20. Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors at 2 institutions in 2 countries.

Tyler ReddyDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK.
David ShorthouseDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK.
Daniel L PartonDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK.
Elizabeth JefferysDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK.
Philip W FowlerDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK.
Matthieu ChaventDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK.
Marc BaadenInstitut de Biologie Physico-Chimique, Centre National de la Recherche Scientifique, UPR9080, Université Paris Diderot, Sorbonne Paris Cité, Paris, France.
Mark S P SansomDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK. Electronic address: mark.sansom@bioch.ox.ac.uk.
University of Oxford · GBSorbonne Paris Cité · FR

Funding

Biotechnology and Biological Sciences Research CouncilCIHRWellcome Trust
6 · The paper itself

Abstract

The influenza virus is surrounded by an envelope composed of a lipid bilayer and integral membrane proteins. Understanding the structural dynamics of the membrane envelope provides biophysical insights into aspects of viral function, such as the wide-ranging survival times of the virion in different environments. We have combined experimental data from X-ray crystallography, nuclear magnetic resonance spectroscopy, cryo-electron microscopy, and lipidomics to build a model of the intact influenza A virion. This is the basis of microsecond-scale coarse-grained molecular dynamics simulations of the virion, providing simulations at different temperatures and with varying lipid compositions. The presence of the Forssman glycolipid alters a number of biophysical properties of the virion, resulting in reduced mobility of bilayer lipid and protein species. Reduced mobility in the virion membrane may confer physical robustness to changes in environmental conditions. Our simulations indicate that viral spike proteins do not aggregate and thus are competent for multivalent immunoglobulin G interactions.

Indexed as

DiffusionHost-Pathogen InteractionsHumansInfluenza A virusLipidsMolecular Dynamics SimulationProtein BindingProtein Structure, QuaternaryReceptors, VirusVirionVirus AttachmentLipidsReceptors, Virus

Identifiers

PMID25703376
PMCPMC4353694
OpenAlexW2091148298

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.