Evidence map›Paper›PMID 32859902›Full record

ArticleNature communications2020

Dynamic remodelling of the human host cell proteome and phosphoproteome upon enterovirus infection.

Piero Giansanti, Jeroen R P M Strating, Kyra A Y Defourny, Ieva Cesonyte, Alexia M S Bottino, Harm Post, Ekaterina G Viktorova, Vien Quang Tri Ho, Martijn A Langereis, George A Belov and 3 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
2.1field-weighted citation impact, top 12% 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

24 citing papers in PubMed, 43 citations in OpenAlex.

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  10. The effect ofTranslational andrology and urology · 2024
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  15. Article
  16. The role of autophagy in viral infections.Journal of biomedical science · 2023
    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

13 authors at 2 institutions in 3 countries.

Piero Giansanti *Biomolecular Mass Spectrometry and Proteomics, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Padualaan 8, 3584 CH, Utrecht, The Netherlands.ORCID http://orcid.org/0000-0003-2857-0841
Jeroen R P M Strating *Virology Section, Division of Infectious Diseases and Immunology, Department of Biomolecular Health Sciences, Faculty of Veterinary Medicine, Utrecht University, Yalelaan 1, 3584 CL, Utrecht, The Netherlands.ORCID http://orcid.org/0000-0003-2509-5213
Kyra A Y Defourny *Division of Cell Biology, Metabolism & Cancer, Department of Biomolecular Health Sciences, Faculty of Veterinary Medicine, Utrecht University, Yalelaan 2, 3584 CM, Utrecht, The Netherlands.ORCID http://orcid.org/0000-0002-1812-7013
Ieva Cesonyte *Virology Section, Division of Infectious Diseases and Immunology, Department of Biomolecular Health Sciences, Faculty of Veterinary Medicine, Utrecht University, Yalelaan 1, 3584 CL, Utrecht, The Netherlands.ORCID http://orcid.org/0000-0002-8126-1960
Alexia M S BottinoVirology Section, Division of Infectious Diseases and Immunology, Department of Biomolecular Health Sciences, Faculty of Veterinary Medicine, Utrecht University, Yalelaan 1, 3584 CL, Utrecht, The Netherlands.ORCID http://orcid.org/0000-0001-7097-9697
Harm PostBiomolecular Mass Spectrometry and Proteomics, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Padualaan 8, 3584 CH, Utrecht, The Netherlands.
Ekaterina G ViktorovaDepartment of Veterinary Medicine, University of Maryland and VA-MD College of Veterinary Medicine, College Park, MD, 20742, USA.
Vien Quang Tri HoVirology Section, Division of Infectious Diseases and Immunology, Department of Biomolecular Health Sciences, Faculty of Veterinary Medicine, Utrecht University, Yalelaan 1, 3584 CL, Utrecht, The Netherlands.ORCID http://orcid.org/0000-0001-9405-7195
Martijn A LangereisVirology Section, Division of Infectious Diseases and Immunology, Department of Biomolecular Health Sciences, Faculty of Veterinary Medicine, Utrecht University, Yalelaan 1, 3584 CL, Utrecht, The Netherlands.
George A BelovDepartment of Veterinary Medicine, University of Maryland and VA-MD College of Veterinary Medicine, College Park, MD, 20742, USA.ORCID http://orcid.org/0000-0002-0892-1731
Esther N M Nolte-'t HoenDivision of Cell Biology, Metabolism & Cancer, Department of Biomolecular Health Sciences, Faculty of Veterinary Medicine, Utrecht University, Yalelaan 2, 3584 CM, Utrecht, The Netherlands.
Albert J R Heck *Biomolecular Mass Spectrometry and Proteomics, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Padualaan 8, 3584 CH, Utrecht, The Netherlands. a.j.r.heck@uu.nl.ORCID http://orcid.org/0000-0002-2405-4404
Frank J M van Kuppeveld *Virology Section, Division of Infectious Diseases and Immunology, Department of Biomolecular Health Sciences, Faculty of Veterinary Medicine, Utrecht University, Yalelaan 1, 3584 CL, Utrecht, The Netherlands. f.j.m.vankuppeveld@uu.nl.ORCID http://orcid.org/0000-0001-5800-749X
Utrecht University · NLVirginia–Maryland College of Veterinary Medicine · US

Funding

Role of host protein GBF1 in organizing enterovirus replication complexesR01AI125561 · NIAID · UNIV OF MARYLAND, COLLEGE PARK · PI BELOV, GEORGE A. · 2016 to 2020
$1.9M
NIAID NIH HHS R01 AI125561
6 · The paper itself

Abstract

The group of enteroviruses contains many important pathogens for humans, including poliovirus, coxsackievirus, rhinovirus, as well as newly emerging global health threats such as EV-A71 and EV-D68. Here, we describe an unbiased, system-wide and time-resolved analysis of the proteome and phosphoproteome of human cells infected with coxsackievirus B3. Of the ~3,200 proteins quantified throughout the time course, a large amount (~25%) shows a significant change, with the majority being downregulated. We find ~85% of the detected phosphosites to be significantly regulated, implying that most changes occur at the post-translational level. Kinase-motif analysis reveals temporal activation patterns of certain protein kinases, with several CDKs/MAPKs immediately active upon the infection, and basophilic kinases, ATM, and ATR engaging later. Through bioinformatics analysis and dedicated experiments, we identify mTORC1 signalling as a major regulation network during enterovirus infection. We demonstrate that inhibition of mTORC1 activates TFEB, which increases expression of lysosomal and autophagosomal genes, and that TFEB activation facilitates the release of virions in extracellular vesicles via secretory autophagy. Our study provides a rich framework for a system-level understanding of enterovirus-induced perturbations at the protein and signalling pathway levels, forming a base for the development of pharmacological inhibitors to treat enterovirus infections.

Indexed as

AnimalsAutophagyBasic Helix-Loop-Helix Leucine Zipper Transcription FactorsCell LineCell SurvivalCoxsackievirus InfectionsEnterovirusEnterovirus B, HumanGene Knockout TechniquesHeLa CellsHost-Pathogen InteractionsHumansMechanistic Target of Rapamycin Complex 1PhosphorylationProteomeSignal TransductionBasic Helix-Loop-Helix Leucine Zipper Transcription FactorsMechanistic Target of Rapamycin Complex 1ProteomeTFEB protein, humanViral Proteins

Identifiers

PMID32859902
PMCPMC7455705
OpenAlexW3081769550

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.