Evidence map›Paper›PMID 29997204›Full record

ArticleJournal of virology2018

Regulatory Role of the Morbillivirus Attachment Protein Head-to-Stalk Linker Module in Membrane Fusion Triggering.

Michael Herren, Neeta Shrestha, Marianne Wyss, Andreas Zurbriggen, Philippe Plattet

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.3field-weighted citation impact, top 20% 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

11 citing papers in PubMed, 17 citations in OpenAlex.

  1. Article
  2. Review
  3. Structure and supramolecular organization of the canine distemper virus attachment glycoprotein.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
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  5. Article
  6. Article
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  8. Review
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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 1 institution in 1 country.

Michael HerrenDivision of Experimental and Clinical Research, DCR-VPH, Vetsuisse Faculty, University of Bern, Bern, Switzerland.
Neeta ShresthaDivision of Experimental and Clinical Research, DCR-VPH, Vetsuisse Faculty, University of Bern, Bern, Switzerland.
Marianne WyssDivision of Experimental and Clinical Research, DCR-VPH, Vetsuisse Faculty, University of Bern, Bern, Switzerland.
Andreas ZurbriggenDivision of Experimental and Clinical Research, DCR-VPH, Vetsuisse Faculty, University of Bern, Bern, Switzerland.
Philippe PlattetDivision of Experimental and Clinical Research, DCR-VPH, Vetsuisse Faculty, University of Bern, Bern, Switzerland philippe.plattet@vetsuisse.unibe.ch.
University of Bern · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Morbillivirus (e.g., measles virus [MeV] and canine distemper virus [CDV]) host cell entry is coordinated by two interacting envelope glycoproteins, namely, an attachment (H) protein and a fusion (F) protein. The ectodomain of H proteins consists of stalk, connector, and head domains that assemble into functional noncovalent dimer-of-dimers. The role of the C-terminal module of the H-stalk domain (termed linker) and the connector, although putatively able to assume flexible structures and allow receptor-induced structural rearrangements, remains largely unexplored. Here, we carried out a nonconservative mutagenesis scan analysis of the MeV and CDV H-linker/connector domains. Our data demonstrated that replacing isoleucine 146 in H-linker (H-I146) with any charged amino acids prevented virus-mediated membrane fusion activity, despite proper trafficking of the mutants to the cell surface and preserved binding efficiency to the SLAM/CD150 receptor. Nondenaturing electrophoresis revealed that these charged amino acid changes led to the formation of irregular covalent H tetramers rather than functional dimer-of-dimers formed when isoleucine or other hydrophobic amino acids were present at residue position 146. Remarkably, we next demonstrated that covalent H tetramerization

Indexed as

Gene Expression Regulation, ViralViral Envelope ProteinsAnimalsChlorocebus aethiopsDistemper Virus, CanineGlycoproteinsHumansIsoleucineMembrane FusionMorbillivirusMutagenesisMutationProtein BindingProtein ConformationProtein FoldingProtein MultimerizationGlycoproteinsIsoleucineSignaling Lymphocytic Activation Molecule Family Member 1SLAMF1 protein, humanViral Envelope ProteinsViral Fusion Proteinsattachment proteinhost cell invasionlinker modulemembrane fusion activationMorbillivirusprotein foldingstalk domain

Identifiers

PMID29997204
PMCPMC6146710
OpenAlexW2823021133

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.