Evidence map›Paper›PMID 18665235›Full record

ArticlePloS one2008

The Murid Herpesvirus-4 gL regulates an entry-associated conformation change in gH.

Laurent Gillet, Susanna Colaco, Philip G Stevenson

Erratum issuedAbstract read
In one paragraph

Article in PloS one, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing 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

19 citing papers in PubMed.

  1. Article
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  3. Review
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  17. Article
  18. Class III viral membrane fusion proteins.Current opinion in structural biology · 2009
    Review
  19. Article
4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

3 authors.

Laurent GilletDivision of Virology, Department of Pathology, University of Cambridge, Cambridge, United Kingdom.
Susanna Colaco
Philip G Stevenson

Funding

Cancer Research UK C19612/A6189Medical Research Council G0400427Medical Research Council G9800903Wellcome TrustWellcome Trust GR076956MA
6 · The paper itself

Abstract

The glycoprotein H (gH)/gL heterodimer is crucial for herpesvirus membrane fusion. Yet how it functions is not well understood. The Murid Herpesvirus-4 gH, like that of other herpesviruses, adopts its normal virion conformation by associating with gL. However, gH switched back to a gL-independent conformation after virion endocytosis. This switch coincided with a conformation switch in gB and with capsid release. Virions lacking gL constitutively expressed the down-stream form of gH, prematurely switched gB to its down-stream form, and showed premature capsid release with poor infectivity. These data argue that gL plays a key role in regulating a gH and gB functional switch from cell binding to membrane fusion.

Indexed as

AnimalsCricetinaeDimerizationEndocytosisEndosomesGlycoproteinsHydrogen-Ion ConcentrationMembrane FusionMembrane GlycoproteinsMiceMolecular ChaperonesNIH 3T3 CellsProtein ConformationRhadinovirusViral Envelope ProteinsViral Proteinsglycoprotein H, Herpesvirus 4glycoprotein L, Human herpesvirus 4GlycoproteinsMembrane GlycoproteinsMolecular ChaperonesViral Envelope ProteinsViral Proteins

Identifiers

PMID18665235
PMCPMC2481400

What OpenQuestion holds

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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.