Evidence map›Paper›PMID 29244872›Full record

ArticlePloS one2017

The ubiquitin-proteasome system is required for African swine fever replication.

Lucía Barrado-Gil, Inmaculada Galindo, Diego Martínez-Alonso, Sergio Viedma, Covadonga Alonso

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
5.4field-weighted citation impact, top 4% 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

33 citing papers in PubMed, 49 citations in OpenAlex.

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  15. Insights into the function of ESCRT complex and LBPA in ASFV infection.Frontiers in cellular and infection microbiology · 2023
    Article
  16. African Swine Fever Virus: A Review.Life (Basel, Switzerland) · 2022
    Review
  17. Article
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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.

Lucía Barrado-GilDepartment of Biotechnology, Instituto Nacional de Investigación y Tecnología Agraria y Alimentaria, INIA, Madrid, Spain.
Inmaculada GalindoDepartment of Biotechnology, Instituto Nacional de Investigación y Tecnología Agraria y Alimentaria, INIA, Madrid, Spain.
Diego Martínez-AlonsoDepartment of Biotechnology, Instituto Nacional de Investigación y Tecnología Agraria y Alimentaria, INIA, Madrid, Spain.
Sergio ViedmaDepartment of Biotechnology, Instituto Nacional de Investigación y Tecnología Agraria y Alimentaria, INIA, Madrid, Spain.
Covadonga AlonsoDepartment of Biotechnology, Instituto Nacional de Investigación y Tecnología Agraria y Alimentaria, INIA, Madrid, Spain.ORCID http://orcid.org/0000-0002-0862-6177
Instituto Nacional de Investigación y Tecnología Agraria y Alimentaria · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Several viruses manipulate the ubiquitin-proteasome system (UPS) to initiate a productive infection. Determined viral proteins are able to change the host's ubiquitin machinery and some viruses even encode their own ubiquitinating or deubiquitinating enzymes. African swine fever virus (ASFV) encodes a gene homologous to the E2 ubiquitin conjugating (UBC) enzyme. The viral ubiquitin-conjugating enzyme (UBCv1) is expressed throughout ASFV infection and accumulates at late times post infection. UBCv is also present in the viral particle suggesting that the ubiquitin-proteasome pathway could play an important role at early ASFV infection. We determined that inhibition of the final stage of the ubiquitin-proteasome pathway blocked a post-internalization step in ASFV replication in Vero cells. Under proteasome inhibition, ASF viral genome replication, late gene expression and viral production were severely reduced. Also, ASFV enhanced proteasome activity at late times and the accumulation of polyubiquitinated proteins surrounding viral factories. Core-associated and/or viral proteins involved in DNA replication may be targets for the ubiquitin-proteasome pathway that could possibly assist virus uncoating at final core breakdown and viral DNA release. At later steps, polyubiquitinated proteins at viral factories could exert regulatory roles in cell signaling.

Indexed as

African Swine FeverAfrican Swine Fever VirusAnimalsChlorocebus aethiopsDNA ReplicationDNA, ViralGenome, ViralProteasome Endopeptidase ComplexSwineUbiquitinUbiquitin-Conjugating EnzymesVero CellsViral ProteinsVirionVirus ReplicationDNA, ViralProteasome Endopeptidase ComplexUbiquitinUbiquitin-Conjugating Enzymesubiquitin-conjugating enzyme UBCv1, African swine fever virusViral Proteins

Identifiers

PMID29244872
PMCPMC5731689
OpenAlexW2775249851

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.