Evidence map›Paper›PMID 31619557›Full record

ArticleJournal of virology2020

Human Enterovirus Group B Viruses Rely on Vimentin Dynamics for Efficient Processing of Viral Nonstructural Proteins.

Paula Turkki, Mira Laajala, Malin Flodström-Tullberg, Varpu Marjomäki

Open access · hybridAbstract read
In one paragraph

Article in Journal of virology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
3.4field-weighted citation impact, top 6% 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

19 citing papers in PubMed, 33 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Antiviral Mechanisms ofPharmaceutics · 2023
    Article
  6. Review
  7. Article
  8. Extracellular Vimentin as a Target Against SARS-CoV-2 Host Cell Invasion.Small (Weinheim an der Bergstrasse, Germany) · 2022
    Article
  9. Article
  10. Review
  11. Pathophysiological Role of Vimentin Intermediate Filaments in Lung Diseases.Frontiers in cell and developmental biology · 2022
    Review
  12. Article
  13. Article
  14. Article
  15. Extracellular vimentin as a target against SARS-CoV-2 host cell invasion.bioRxiv : the preprint server for biology · 2021
    Article
  16. Article
  17. Review
  18. Mechanical and Non-Mechanical Functions of Filamentous and Non-Filamentous Vimentin.BioEssays : news and reviews in molecular, cellular and developmental biology · 2020
    Review
  19. Review
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 3 institutions in 2 countries.

Paula TurkkiDepartment of Biological and Environmental Science, Division of Cell and Molecular Biology/Nanoscience Center, University of Jyväskylä, Jyväskylä, Finland.
Mira LaajalaDepartment of Biological and Environmental Science, Division of Cell and Molecular Biology/Nanoscience Center, University of Jyväskylä, Jyväskylä, Finland.
Malin Flodström-TullbergCenter for Infectious Medicine, Department of Medicine Huddinge, Karolinska Institute, Karolinska University Hospital, Stockholm, Sweden.
Varpu MarjomäkiDepartment of Biological and Environmental Science, Division of Cell and Molecular Biology/Nanoscience Center, University of Jyväskylä, Jyväskylä, Finland varpu.s.marjomaki@jyu.fi.
University of Jyväskylä · FIKarolinska University Hospital · SETampere University · FI

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We report that several viruses from the human enterovirus group B cause massive vimentin rearrangements during lytic infection. Comprehensive studies suggested that viral protein synthesis was triggering the vimentin rearrangements. Blocking the host cell vimentin dynamics with β, β'-iminodipropionitrile (IDPN) did not significantly affect the production of progeny viruses and only moderately lowered the synthesis of structural proteins such as VP1. In contrast, the synthesis of the nonstructural proteins 2A, 3C, and 3D was drastically lowered. This led to attenuation of the cleavage of the host cell substrates PABP and G3BP1 and reduced caspase activation, leading to prolonged cell survival. Furthermore, the localization of the proteins differed in the infected cells. Capsid protein VP1 was found diffusely around the cytoplasm, whereas 2A and 3D followed vimentin distribution. Based on protein blotting, smaller amounts of nonstructural proteins did not result from proteasomal degradation but from lower synthesis without intact vimentin cage structure. In contrast, inhibition of Hsp90 chaperone activity, which regulates P1 maturation, lowered the amount of VP1 but had less effect on 2A. The results suggest that the vimentin dynamics regulate viral nonstructural protein synthesis while having less effect on structural protein synthesis or overall infection efficiency. The results presented here shed new light on differential fate of structural and nonstructural proteins of enteroviruses, having consequences on host cell survival.

Indexed as

Protein BiosynthesisA549 CellsDNA HelicasesEnterovirus B, HumanHeLa CellsHSP90 Heat-Shock ProteinsHumansPoly-ADP-Ribose Binding ProteinsRNA HelicasesRNA Recognition Motif ProteinsVimentinViral Nonstructural ProteinsDNA HelicasesG3BP1 protein, humanHSP90 Heat-Shock ProteinsPoly-ADP-Ribose Binding ProteinsRNA HelicasesRNA Recognition Motif ProteinsVimentinVIM protein, humanViral Nonstructural Proteinsapoptosisenteroviruspolyprotein processingproteasesvimentin

Identifiers

PMID31619557
PMCPMC6955253
OpenAlexW2980366253

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.