Evidence map›Paper›PMID 28368306›Full record

ArticleViruses2017

ICAM-1 Binding Rhinoviruses Enter HeLa Cells via Multiple Pathways and Travel to Distinct Intracellular Compartments for Uncoating.

Haleh Ganjian, Christin Zietz, Diana Mechtcheriakova, Dieter Blaas, Renate Fuchs

Open access · goldAbstract read
In one paragraph

Article in Viruses, 2017. 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
1.4field-weighted citation impact, top 17% 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, 21 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Myristoylated rhinovirus VP4 protein activates TLR2-dependent proinflammatory gene expression.American journal of physiology. Lung cellular and molecular physiology · 2019
    Article
  9. Virus Entry: Looking Back and Moving Forward.Journal of molecular biology · 2018
    Review
  10. Article
  11. 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

5 authors at 2 institutions in 1 country.

Haleh GanjianDepartment of Pathophysiology and Allergy Research, Medical University of Vienna, Währinger Gürtel 18-20, A-1090 Wien, Austria. halehganjian85@gmail.com.
Christin ZietzDepartment of Pathophysiology and Allergy Research, Medical University of Vienna, Währinger Gürtel 18-20, A-1090 Wien, Austria. a1368365@unet.univie.ac.at.
Diana MechtcheriakovaDepartment of Pathophysiology and Allergy Research, Medical University of Vienna, Währinger Gürtel 18-20, A-1090 Wien, Austria. diana.mechtcheriakova@meduniwien.ac.at.
Dieter BlaasMax F. Perutz Laboratories, Department of Medical Biochemistry, Medical University of Vienna, Dr. Bohr Gasse 9/3, A-1030 Vienna, Austria. dieter.blaas@meduniwien.ac.at.
Renate FuchsDepartment of Pathophysiology and Allergy Research, Medical University of Vienna, Währinger Gürtel 18-20, A-1090 Wien, Austria. renate.fuchs@meduniwien.ac.at.
Medical University of Vienna · ATMax Perutz Labs · AT

Funding

Austrian Science Fund FWF P 23308
6 · The paper itself

Abstract

Of the more than 150 human rhinovirus (RV) serotypes, 89 utilize intercellular adhesion molecule-1 (ICAM-1) for cell entry. These belong either to species A or B. We recently demonstrated that RV-B14 and RV-A89, despite binding this same receptor, are routed into distinct endosomal compartments for release of their RNA into the cytosol. To gain insight into the underlying mechanism we now comparatively investigate the port of entry, temperature-dependence of uncoating, and intracellular routing of RV-B3, RV-B14, RV-A16, and RV-A89 in HeLa cells. The effect of various drugs blocking distinct stages on the individual pathways was determined via comparing the number of infected cells in a TissueFaxs instrument. We found that RV-B14 and RV-A89 enter via clathrin-, dynamin-, and cholesterol-dependent pathways, as well as by macropinocytosis. Drugs interfering with actin function similarly blocked entry of all four viruses, indicating their dependence on a dynamic actin network. However, uniquely, RV-A89 was able to produce progeny when internalized at 20 °C followed by neutralizing the endosomal pH and further incubation at 37 °C. Blocking dynein-dependent endosomal transport prevented uncoating of RV-A16 and RV-A89, but not of RV-B3 and RV-B14, indicative for routing of RV-A16 and RV-A89 into the endocytic recycling compartment for uncoating. Our results call for caution when developing drugs aimed at targeting entry or intracellular trafficking of all rhinovirus serotypes.

Indexed as

Virus AttachmentVirus InternalizationVirus UncoatingBiological TransportHeLa CellsHumansHydrogen-Ion ConcentrationIntercellular Adhesion Molecule-1Receptors, VirusRhinovirusTemperatureIntercellular Adhesion Molecule-1Receptors, Virusactinclathrindynamindyneinendocytosishuman rhinovirusesICAM-1macropinocytosisproductive uncoating

Identifiers

PMID28368306
PMCPMC5408674
OpenAlexW2604699448

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.