Evidence map›Paper›PMID 20921141›Full record

ArticleThe Journal of cell biology2010

Distinct structural rearrangements of the VSV glycoprotein drive membrane fusion.

Sonia Libersou, Aurélie A V Albertini, Malika Ouldali, Virginie Maury, Christine Maheu, Hélène Raux, Felix de Haas, Stéphane Roche, Yves Gaudin, Jean Lepault

Abstract read
In one paragraph

Article in The Journal of cell biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
–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

39 citing papers in PubMed.

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  20. Mechanism of membrane fusion induced by vesicular stomatitis virus G protein.Proceedings of the National Academy of Sciences of the United States of America · 2017
    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

10 authors.

Sonia LibersouCentre de Recherche de Gif, Laboratoire de Virologie Moléculaire et Structurale, CNRS (UMR 2472), INRA (UMR 1153), IFR115, 91198 Gif-sur-Yvette, France.
Aurélie A V Albertini
Malika Ouldali
Virginie Maury
Christine Maheu
Hélène Raux
Felix de Haas
Stéphane Roche
Yves Gaudin
Jean Lepault

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The entry of enveloped viruses into cells requires the fusion of viral and cellular membranes, driven by conformational changes in viral glycoproteins. Many studies have shown that fusion involves the cooperative action of a large number of these glycoproteins, but the underlying mechanisms are unknown. We used electron microscopy and tomography to study the low pH-induced fusion reaction catalyzed by vesicular stomatitis virus glycoprotein (G). Pre- and post-fusion crystal structures were observed on virions at high and low pH, respectively. Individual fusion events with liposomes were also visualized. Fusion appears to be driven by two successive structural rearrangements of G at different sites on the virion. Fusion is initiated at the flat base of the particle. Glycoproteins located outside the contact zone between virions and liposomes then reorganize into regular arrays. We suggest that the formation of these arrays, which have been shown to be an intrinsic property of the G ectodomain, induces membrane constraints, achieving the fusion reaction.

Indexed as

Virus InternalizationCrystallography, X-RayHydrogen-Ion ConcentrationLiposomesMembrane FusionMembrane GlycoproteinsProtein Structure, TertiaryVesicular stomatitis Indiana virusViral Fusion ProteinsViral ProteinsVirionLiposomesMembrane GlycoproteinsViral Fusion ProteinsViral Proteins

Identifiers

PMID20921141
PMCPMC2953448

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Registered trials

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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.