Evidence map›Paper›PMID 28154158›Full record

ArticleJournal of cell science2017

Caveolae provide a specialized membrane environment for respiratory syncytial virus assembly.

Alexander Ludwig, Tra Huong Nguyen, Daniel Leong, Laxmi Iyer Ravi, Boon Huan Tan, Sara Sandin, Richard J Sugrue

Open access · hybridAbstract read
In one paragraph

Article in Journal of cell science, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.5field-weighted citation impact, top 20% 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

19 citing papers in PubMed, 30 citations in OpenAlex.

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  14. Caveolae as Potential Hijackable Gates in Cell Communication.Frontiers in cell and developmental biology · 2020
    Review
  15. Article
  16. Review
  17. Cholesterol modulates the cellular localization of Orai1 channels and its disposition among membrane domains.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2017
    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

7 authors at 2 institutions in 1 country.

Alexander LudwigSchool of Biological Sciences, Nanyang Technological University, 60 Nanyang Drive, Singapore 637551 aludwig@ntu.edu.sg rjsugrue@ntu.edu.sg.ORCID 0000-0002-0696-5298
Tra Huong NguyenSchool of Biological Sciences, Nanyang Technological University, 60 Nanyang Drive, Singapore 637551.
Daniel LeongDetection and Diagnostics Laboratory, DSO National Laboratories, 27 Medical Drive, Singapore 117510.
Laxmi Iyer RaviSchool of Biological Sciences, Nanyang Technological University, 60 Nanyang Drive, Singapore 637551.
Boon Huan TanDetection and Diagnostics Laboratory, DSO National Laboratories, 27 Medical Drive, Singapore 117510.
Sara SandinSchool of Biological Sciences, Nanyang Technological University, 60 Nanyang Drive, Singapore 637551.
Richard J SugrueSchool of Biological Sciences, Nanyang Technological University, 60 Nanyang Drive, Singapore 637551 aludwig@ntu.edu.sg rjsugrue@ntu.edu.sg.
Nanyang Technological University · SGDSO National Laboratories · SG

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Respiratory syncytial virus (RSV) is an enveloped virus that assembles into filamentous virus particles on the surface of infected cells. Morphogenesis of RSV is dependent upon cholesterol-rich (lipid raft) membrane microdomains, but the specific role of individual raft molecules in RSV assembly is not well defined. Here, we show that RSV morphogenesis occurs within caveolar membranes and that both caveolin-1 and cavin-1 (also known as PTRF), the two major structural and functional components of caveolae, are actively recruited to and incorporated into the RSV envelope. The recruitment of caveolae occurred just prior to the initiation of RSV filament assembly, and was dependent upon an intact actin network as well as a direct physical interaction between caveolin-1 and the viral G protein. Moreover, cavin-1 protein levels were significantly increased in RSV-infected cells, leading to a virus-induced change in the stoichiometry and biophysical properties of the caveolar coat complex. Our data indicate that RSV exploits caveolae for its assembly, and we propose that the incorporation of caveolae into the virus contributes to defining the biological properties of the RSV envelope.

Indexed as

ActinsCaveolaeCaveolin 1Cell MembraneHeLa CellsHumansModels, BiologicalMorphogenesisProtein BindingProtein StabilityRespiratory Syncytial Virus, HumanRNA-Binding ProteinsViral ProteinsVirus AssemblyActinsCaveolin 1CAVIN1 protein, humanRNA-Binding ProteinsViral ProteinsCaveolaeCaveolinCavinRespiratory syncytial virusVirus assemblyVirus envelope

Identifiers

PMID28154158
PMCPMC5358342
OpenAlexW2583992088

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.