Evidence map›Paper›PMID 30946995›Full record

ArticleVirology2019

Human metapneumovirus fusion protein triggering: Increasing complexities by analysis of new HMPV fusion proteins.

J Tyler Kinder, Edita M Klimyte, Andres Chang, John V Williams, Rebecca Ellis Dutch

Open access · greenAbstract read
In one paragraph

Article in Virology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.8field-weighted citation impact, top 27% 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

6 citing papers in PubMed, 13 citations in OpenAlex.

  1. Article
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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

5 authors at 2 institutions in 1 country.

J Tyler KinderDepartment of Molecular and Cellular Biochemistry, University of Kentucky, Lexington, KY, United States.
Edita M KlimyteDepartment of Molecular and Cellular Biochemistry, University of Kentucky, Lexington, KY, United States.
Andres ChangDepartment of Molecular and Cellular Biochemistry, University of Kentucky, Lexington, KY, United States.
John V WilliamsSchool of Medicine, University of Pittsburgh, Pittsburgh, PA, United States.
Rebecca Ellis DutchDepartment of Molecular and Cellular Biochemistry, University of Kentucky, Lexington, KY, United States. Electronic address: rdutc2@uky.edu.
University of Kentucky · USUniversity of Pittsburgh · US

Funding

Protein CoreP30GM110787 · NIGMS · UNIVERSITY OF KENTUCKY · PI WHITEHEART, SIDNEY WALDO · 2014 to 2018
$5.7M
Host Determinants of Human Metapneumovirus Immunity and PathogenesisR01AI085062 · NIAID · VANDERBILT UNIVERSITY · PI John V. Williams · 2010 to 2026
$5.6M
SV5 and Hendra virus F protein promoted membrane fusionR01AI051517 · NIAID · UNIVERSITY OF KENTUCKY · PI DUTCH, REBECCA E. · 2002 to 2019
$4.4M
Kentucky Center for Clinical and Translational ScienceTL1TR000115 · NCATS · UNIVERSITY OF KENTUCKY · PI KERN, PHILIP A · 2012 to 2015
$518k
Elucidating binding, fusion and entry of HMPV in cell culture and host tissueF30AI114194 · NIAID · UNIVERSITY OF KENTUCKY · PI KLIMYTE, EDITA MARIA · 2015 to 2018
$137k
NCATS NIH HHS TL1 TR000115NIAID NIH HHS F30 AI114194NIAID NIH HHS R01 AI051517NIAID NIH HHS R01 AI085062NIGMS NIH HHS P30 GM110787
6 · The paper itself

Abstract

The human metapneumovirus (HMPV) fusion protein (F) mediates fusion of the viral envelope and cellular membranes to establish infection. HMPV F from some, but not all, viral strains promotes fusion only after exposure to low pH. Previous studies have identified several key residues involved in low pH triggering, including H435 and a proposed requirement for glycine at position 294. We analyzed the different levels of fusion activity, protein expression and cleavage of three HMPV F proteins not previously examined. Interestingly, low pH-triggered fusion in the absence of G294 was identified in one F protein, while a novel histidine residue (H434) was identified that enhanced low pH promoted fusion in another. The third F protein failed to promote cell-to-cell fusion, suggesting other requirements for F protein triggering. Our results demonstrate HMPV F triggering is more complex than previously described and suggest a more intricate mechanism for fusion protein function and activation.

Indexed as

Amino Acid MotifsAmino Acid SequenceAnimalsChlorocebus aethiopsHumansMetapneumovirusParamyxoviridae InfectionsProtein StabilitySequence AlignmentVero CellsViral Fusion ProteinsViral Fusion ProteinsCladeFusionHMPVHuman metapneumovirusLow pHStrainsSyncytia

Identifiers

PMID30946995
PMCPMC6486425
OpenAlexW2921200901

What OpenQuestion holds

Textmetadata
LicenceTDM
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.