Evidence map›Paper›PMID 29669880›Full record

ArticlemSphere2018

Transmembrane Domains of Highly Pathogenic Viral Fusion Proteins Exhibit Trimeric Association

Stacy R Webb, Stacy E Smith, Michael G Fried, Rebecca Ellis Dutch

Open access · goldAbstract read
In one paragraph

Article in mSphere, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
2.0field-weighted citation impact, top 14% 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

12 citing papers in PubMed, 19 citations in OpenAlex.

  1. Article
  2. Article
  3. Inconspicuous Yet Indispensable: The Coronavirus Spike Transmembrane Domain.International journal of molecular sciences · 2023
    Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. 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 1 institution in 1 country.

Stacy R WebbDepartment of Molecular and Cellular Biochemistry, University of Kentucky, Lexington, Kentucky, USA.
Stacy E SmithDepartment of Molecular and Cellular Biochemistry, University of Kentucky, Lexington, Kentucky, USA.
Michael G FriedDepartment of Molecular and Cellular Biochemistry, University of Kentucky, Lexington, Kentucky, USA.
Rebecca Ellis DutchDepartment of Molecular and Cellular Biochemistry, University of Kentucky, Lexington, Kentucky, USA rdutc2@uky.edu.
University of Kentucky · US

Funding

Protein CoreP30GM110787 · NIGMS · UNIVERSITY OF KENTUCKY · PI WHITEHEART, SIDNEY WALDO · 2014 to 2018
$5.7M
SV5 and Hendra virus F protein promoted membrane fusionR01AI051517 · NIAID · UNIVERSITY OF KENTUCKY · PI DUTCH, REBECCA E. · 2002 to 2019
$4.4M
Fusion protein TM-TM interactions: Modulation of pre-fusion protein stabilityF31AI120653 · NIAID · UNIVERSITY OF KENTUCKY · PI WEBB, STACY RENEE · 2015 to 2016
$69k
NIAID NIH HHS F31 AI120653NIAID NIH HHS R01 AI051517NIGMS NIH HHS P30 GM110787
6 · The paper itself

Abstract

Enveloped viruses require viral fusion proteins to promote fusion of the viral envelope with a target cell membrane. To drive fusion, these proteins undergo large conformational changes that must occur at the right place and at the right time. Understanding the elements which control the stability of the prefusion state and the initiation of conformational changes is key to understanding the function of these important proteins. The construction of mutations in the fusion protein transmembrane domains (TMDs) or the replacement of these domains with lipid anchors has implicated the TMD in the fusion process. However, the structural and molecular details of the role of the TMD in these fusion events remain unclear. Previously, we demonstrated that isolated paramyxovirus fusion protein TMDs associate in a monomer-trimer equilibrium, using sedimentation equilibrium analytical ultracentrifugation. Using a similar approach, the work presented here indicates that trimeric interactions also occur between the fusion protein TMDs of Ebola virus, influenza virus, severe acute respiratory syndrome coronavirus (SARS CoV), and rabies virus. Our results suggest that TM-TM interactions are important in the fusion protein function of diverse viral families.

Indexed as

Protein MultimerizationEbolavirusGlycoproteinsMembrane FusionOrthomyxoviridaeProtein DomainsProtein StabilityRabies virusSevere acute respiratory syndrome-related coronavirusViral Envelope ProteinsViral Fusion ProteinsVirus InternalizationGlycoproteinsViral Envelope ProteinsViral Fusion ProteinsEbola virusfusion proteininfluenzarabiesSARStransmembrane domainvirus

Identifiers

PMID29669880
PMCPMC5907656
OpenAlexW2800257026

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.