Evidence map›Paper›PMID 36306280›Full record

ArticlePLoS pathogens2022

A Proximity biotinylation assay with a host protein bait reveals multiple factors modulating enterovirus replication.

Seyedehmahsa Moghimi, Ekaterina G Viktorova, Samuel Gabaglio, Anna Zimina, Bogdan Budnik, Bridge G Wynn, Elizabeth Sztul, George A Belov

Open access · goldAbstract read
In one paragraph

Article in PLoS pathogens, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
1.0field-weighted citation impact, top 23% 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

7 citing papers in PubMed, 7 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. 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

8 authors at 3 institutions in 1 country.

Seyedehmahsa MoghimiDepartment of Veterinary Medicine and Virginia-Maryland College of Veterinary Medicine, University of Maryland, College Park, Maryland, United States of America.
Ekaterina G ViktorovaDepartment of Veterinary Medicine and Virginia-Maryland College of Veterinary Medicine, University of Maryland, College Park, Maryland, United States of America.
Samuel GabaglioDepartment of Veterinary Medicine and Virginia-Maryland College of Veterinary Medicine, University of Maryland, College Park, Maryland, United States of America.
Anna ZiminaDepartment of Veterinary Medicine and Virginia-Maryland College of Veterinary Medicine, University of Maryland, College Park, Maryland, United States of America.
Bogdan BudnikMass Spectrometry and Proteomics Resource Laboratory (MSPRL), FAS Division of Science, Harvard University, Cambridge, Massachusetts, United States of America.
Bridge G WynnDepartment of Cell, Developmental and Integrative Biology, University of Alabama at Birmingham; Birmingham, Alabama, United States of America.
Elizabeth SztulDepartment of Cell, Developmental and Integrative Biology, University of Alabama at Birmingham; Birmingham, Alabama, United States of America.
George A BelovDepartment of Veterinary Medicine and Virginia-Maryland College of Veterinary Medicine, University of Maryland, College Park, Maryland, United States of America.ORCID 0000-0002-0892-1731
Virginia–Maryland College of Veterinary Medicine · USUniversity of Alabama at Birmingham · USHarvard University · 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
Spatio-temporal regulation of ARF signaling in vesicle formationR01GM122802 · NIGMS · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI SZTUL, ELIZABETH S · 2017 to 2020
$1.5M
NIAID NIH HHS R01 AI125561NIGMS NIH HHS R01 GM122802
6 · The paper itself

Abstract

As ultimate parasites, viruses depend on host factors for every step of their life cycle. On the other hand, cells evolved multiple mechanisms of detecting and interfering with viral replication. Yet, our understanding of the complex ensembles of pro- and anti-viral factors is very limited in virtually every virus-cell system. Here we investigated the proteins recruited to the replication organelles of poliovirus, a representative of the genus Enterovirus of the Picornaviridae family. We took advantage of a strict dependence of enterovirus replication on a host protein GBF1, and established a stable cell line expressing a truncated GBF1 fused to APEX2 peroxidase that effectively supported viral replication upon inhibition of the endogenous GBF1. This construct biotinylated multiple host and viral proteins on the replication organelles. Among the viral proteins, the polyprotein cleavage intermediates were overrepresented, suggesting that the GBF1 environment is linked to viral polyprotein processing. The proteomics characterization of biotinylated host proteins identified multiple proteins previously associated with enterovirus replication, as well as more than 200 new factors recruited to the replication organelles. RNA metabolism proteins, many of which normally localize in the nucleus, constituted the largest group, underscoring the massive release of nuclear factors into the cytoplasm of infected cells and their involvement in viral replication. Functional analysis of several newly identified proteins revealed both pro- and anti-viral factors, including a novel component of infection-induced stress granules. Depletion of these proteins similarly affected the replication of diverse enteroviruses indicating broad conservation of the replication mechanisms. Thus, our data significantly expand the knowledge of the composition of enterovirus replication organelles, provide new insights into viral replication, and offer a novel resource for identifying targets for anti-viral interventions.

Indexed as

EnterovirusEnterovirus InfectionsPoliovirusAntiviral AgentsBiotinylationGuanine Nucleotide Exchange FactorsHumansPolyproteinsViral ProteinsVirus ReplicationAntiviral AgentsGBF1 protein, humanGuanine Nucleotide Exchange FactorsPolyproteinsViral Proteins

Identifiers

PMID36306280
PMCPMC9645661
OpenAlexW4307475390

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.