Evidence map›Paper›PMID 20657818›Full record

ArticlePLoS pathogens2010

A spatio-temporal analysis of matrix protein and nucleocapsid trafficking during vesicular stomatitis virus uncoating.

Chad E Mire, Judith M White, Michael A Whitt

Open access · goldAbstract read
In one paragraph

Article in PLoS pathogens, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
3.0field-weighted citation impact, top 9% 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

29 citing papers in PubMed, 55 citations in OpenAlex.

  1. How endosomal PIKfyve inhibition prevents viral membrane fusion and entry.Proceedings of the National Academy of Sciences of the United States of America · 2026
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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

3 authors at 2 institutions in 1 country.

Chad E MireDepartment of Molecular Sciences, University of Tennessee Health Science Center, Memphis, Tennessee, United States of America.
Judith M White
Michael A Whitt
University of Tennessee Health Science Center · USUniversity of Virginia · US

Funding

MOLECULAR MECHANISMS OF VIRAL MEMBRANE FUSION PROTEINSR01AI022470 · NIAID · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI WHITE, JUDITH M. · 1985 to 2009
$3.4M
INTERDEPARTMENTAL CONFOCAL MICROSCOPE FACILITYS10RR013725 · NCRR · UNIVERSITY OF TENNESSEE HEALTH SCI CTR · PI WHITT, MICHAEL A · 1999 to 1999
–
NCRR NIH HHS S10 RR13725NIAID NIH HHS AI22470NIAID NIH HHS R01 AI022470
6 · The paper itself

Abstract

To study VSV entry and the fate of incoming matrix (M) protein during virus uncoating we used recombinant viruses encoding M proteins with a C-terminal tetracysteine tag that could be fluorescently labeled using biarsenical (Lumio) compounds. We found that uncoating occurs early in the endocytic pathway and is inhibited by expression of dominant-negative (DN) Rab5, but is not inhibited by DN-Rab7 or DN-Rab11. Uncoating, as defined by the separation of nucleocapsids from M protein, occurred between 15 and 20 minutes post-entry and did not require microtubules or an intact actin cytoskeleton. Unexpectedly, the bulk of M protein remained associated with endosomal membranes after uncoating and was eventually trafficked to recycling endosomes. Another small, but significant fraction of M distributed to nuclear pore complexes, which was also not dependent on microtubules or polymerized actin. Quantification of fluorescence from high-resolution confocal micrographs indicated that after membrane fusion, M protein diffuses across the endosomal membrane with a concomitant increase in fluorescence from the Lumio label which occurred soon after the release of RNPs into the cytoplasm. These data support a new model for VSV uncoating in which RNPs are released from M which remains bound to the endosomal membrane rather than the dissociation of M protein from RNPs after release of the complex into the cytoplasm following membrane fusion.

Indexed as

Virus InternalizationEndosomesGlycoproteinsMembrane FusionMolecular ProbesNucleocapsidProtein TransportRibonucleoproteinsVesiculovirusViral Matrix ProteinsVirus Physiological PhenomenaGlycoproteinsMolecular Probesprotein M (glycoprotein)RibonucleoproteinsViral Matrix Proteins

Identifiers

PMID20657818
PMCPMC2904772
OpenAlexW2068561321

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.