Evidence map›Paper›PMID 37916833›Full record

ArticleJournal of virology2023

Adenovirus E1B-55K controls SUMO-dependent degradation of antiviral cellular restriction factors.

Wing-Hang Ip, Michael H Tatham, Steewen Krohne, Julia Gruhne, Michael Melling, Tina Meyer, Britta Gornott, Luca D Bertzbach, Ronald T Hay, Estefania Rodriguez and 1 more

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
2.5field-weighted citation impact, top 10% 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

12 citing papers in PubMed, 8 citations in OpenAlex.

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  10. The adenovirus DNA-binding protein DBP.Journal of virology · 2024
    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

11 authors at 2 institutions in 2 countries.

Wing-Hang Ip *Department of Viral Transformation, Leibniz Institute of Virology (LIV) , Hamburg, Germany.ORCID 0000-0002-5367-1401
Michael H Tatham *Molecular, Cell and Developmental Biology, School of Life Sciences, University of Dundee , Dundee, Scotland, United Kingdom.ORCID 0000-0001-6986-1691
Steewen KrohneDepartment of Viral Transformation, Leibniz Institute of Virology (LIV) , Hamburg, Germany.
Julia GruhneDepartment of Viral Transformation, Leibniz Institute of Virology (LIV) , Hamburg, Germany.
Michael MellingDepartment of Viral Transformation, Leibniz Institute of Virology (LIV) , Hamburg, Germany.
Tina MeyerDepartment of Viral Transformation, Leibniz Institute of Virology (LIV) , Hamburg, Germany.
Britta GornottDepartment of Viral Transformation, Leibniz Institute of Virology (LIV) , Hamburg, Germany.
Luca D BertzbachDepartment of Viral Transformation, Leibniz Institute of Virology (LIV) , Hamburg, Germany.ORCID 0000-0002-0698-5395
Ronald T HayMolecular, Cell and Developmental Biology, School of Life Sciences, University of Dundee , Dundee, Scotland, United Kingdom.ORCID 0000-0001-7113-9024
Estefania RodriguezDepartment of Viral Transformation, Leibniz Institute of Virology (LIV) , Hamburg, Germany.
Thomas DobnerDepartment of Viral Transformation, Leibniz Institute of Virology (LIV) , Hamburg, Germany.ORCID 0000-0001-7392-8588
Leibniz Institute of Virology (LIV) · DEUniversity of Dundee · GB

Funding

Cancer Research UKWellcome Trust
6 · The paper itself

Abstract

importanceHuman adenoviruses (HAdVs) generally cause mild and self-limiting diseases of the upper respiratory and gastrointestinal tracts but pose a serious risk to immunocompromised patients and children. Moreover, they are widely used as vectors for vaccines and vector-based gene therapy approaches. It is therefore vital to thoroughly characterize HAdV gene products and especially HAdV virulence factors. Early region 1B 55 kDa protein (E1B-55K) is a multifunctional HAdV-encoded oncoprotein involved in various viral and cellular pathways that promote viral replication and cell transformation. We analyzed the E1B-55K dependency of SUMOylation, a post-translational protein modification, in infected cells using quantitative proteomics. We found that HAdV increases overall cellular SUMOylation and that this increased SUMOylation can target antiviral cellular pathways that impact HAdV replication. Moreover, we showed that E1B-55K orchestrates the SUMO-dependent degradation of certain cellular antiviral factors. These results once more emphasize the key role of E1B-55K in the regulation of viral and cellular proteins in productive HAdV infections.

Indexed as

Adenoviridae InfectionsAdenoviruses, HumanAntiviral Restriction FactorsAdenoviridaeHumansSumoylationAntiviral Restriction Factorscell cycle regulationchromatin assemblyDNA damage responseE1B-55Kpost-translational modification (PTM)protein network analysissmall ubiquitin-like modifier (SUMO)SUMO E3-ligaseSUMO proteomicsviral transcription

Identifiers

PMID37916833
PMCPMC10688335
OpenAlexW4388222211

What OpenQuestion holds

Textmetadata
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.