Evidence map›Paper›PMID 20007281›Full record

ArticleJournal of virology2010

A rotavirus spike protein conformational intermediate binds lipid bilayers.

Shane D Trask, Irene S Kim, Stephen C Harrison, Philip R Dormitzer

Open access · bronzeAbstract read
In one paragraph

Article in Journal of virology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
1.9field-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

38 citing papers in PubMed, 53 citations in OpenAlex.

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  20. Comparative genomic analysis of genogroup 1 (Wa-like) rotaviruses circulating in the USA, 2006-2009.Infection, genetics and evolution : journal of molecular epidemiology and evolutionary genetics in infectious diseases · 2014
    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

4 authors at 2 institutions in 1 country.

Shane D TraskLaboratory of Molecular Medicine, Children's Hospital, Boston, Massachusetts 02115, USA.
Irene S Kim
Stephen C Harrison
Philip R Dormitzer
Boston Children's Hospital · USHoward Hughes Medical Institute · US

Funding

STRUCTURE AND ASSEMBLY OF VIRUSES AND OF COATED VESICLESR01CA013202 · NCI · HARVARD UNIVERSITY · PI HARRISON, STEPHEN COPLAN · 1985 to 2024
$4.9M
Structure and Assembly of VirusesR37CA013202 · NCI · CHILDREN'S HOSPITAL BOSTON · PI HARRISON, STEPHEN COPLAN · 2003 to 2012
$3.7M
Rotavirus VP4: Structure and functionR01AI053174 · NIAID · CHILDREN'S HOSPITAL BOSTON · PI HARRISON, STEPHEN COPLAN · 2003 to 2007
$1.5M
NCI NIH HHS CA-13202NCI NIH HHS R01 CA013202NCI NIH HHS R37 CA013202NIAID NIH HHS AI-053174NIAID NIH HHS R01 AI053174
6 · The paper itself

Abstract

During rotavirus entry, a virion penetrates a host cell membrane, sheds its outer capsid proteins, and releases a transcriptionally active subviral particle into the cytoplasm. VP5, the rotavirus protein believed to interact with the membrane bilayer, is a tryptic cleavage product of the outer capsid spike protein, VP4. When a rotavirus particle uncoats, VP5 folds back, in a rearrangement that resembles the fusogenic conformational changes in enveloped-virus fusion proteins. We present direct experimental evidence that this rearrangement leads to membrane binding. VP5 does not associate with liposomes when mounted as part of the trypsin-primed spikes on intact virions, nor does it do so after it has folded back into a stably trimeric, low-energy state. But it does bind liposomes when they are added to virions before uncoating, and VP5 rearrangement is then triggered by addition of EDTA. The presence of liposomes during the rearrangement enhances the otherwise inefficient VP5 conformational change. A VP5 fragment, VP5CT, produced from monomeric recombinant VP4 by successive treatments with chymotrypsin and trypsin, also binds liposomes only when the proteolysis proceeds in their presence. A monoclonal antibody that neutralizes infectivity by blocking a postattachment entry event also blocks VP5 liposome association. We propose that VP5 binds lipid bilayers in an intermediate conformational state, analogous to the extended intermediate conformation of enveloped-virus fusion proteins.

Indexed as

AnimalsAntibodies, NeutralizingCell LineChymotrypsinLipid BilayersLiposomesMacaca mulattaModels, BiologicalModels, MolecularPeptide FragmentsProtein BindingProtein ConformationRecombinant ProteinsRotavirusTrypsinViral Nonstructural ProteinsAntibodies, NeutralizingChymotrypsinLipid BilayersLiposomesnsp1 protein, RotavirusPeptide FragmentsRecombinant ProteinsTrypsinViral Nonstructural Proteins

Identifiers

PMID20007281
PMCPMC2812363
OpenAlexW2127073503

What OpenQuestion holds

Textmetadata
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.