Evidence map›Paper›PMID 38315728›Full record

ArticlePLoS pathogens2024

Guanylate-binding protein 1 acts as a pro-viral factor for the life cycle of hepatitis C virus.

Daniela Bender, Alexandra Koulouri, Xingjian Wen, Mirco Glitscher, Anja Schollmeier, Liliana Fernandes da Costa, Robin Oliver Murra, Gert Paul Carra, Vanessa Haberger, Gerrit J K Praefcke and 1 more

Open access · goldAbstract read
In one paragraph

Article in PLoS pathogens, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
1.8field-weighted citation impact, top 16% 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

3 citing papers in PubMed, 5 citations in OpenAlex.

  1. Review
  2. Article
  3. 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

11 authors at 1 institution in 1 country.

Daniela BenderPaul-Ehrlich-Institut, Department of Virology, Langen, Germany.
Alexandra KoulouriPaul-Ehrlich-Institut, Department of Virology, Langen, Germany.
Xingjian WenPaul-Ehrlich-Institut, Department of Virology, Langen, Germany.
Mirco GlitscherPaul-Ehrlich-Institut, Department of Virology, Langen, Germany.
Anja SchollmeierPaul-Ehrlich-Institut, Department of Virology, Langen, Germany.
Liliana Fernandes da CostaPaul-Ehrlich-Institut, Department of Virology, Langen, Germany.
Robin Oliver MurraPaul-Ehrlich-Institut, Department of Virology, Langen, Germany.
Gert Paul CarraPaul-Ehrlich-Institut, Department of Virology, Langen, Germany.
Vanessa HabergerPaul-Ehrlich-Institut, Department of Virology, Langen, Germany.
Gerrit J K PraefckePaul-Ehrlich-Institut, Department Haematology and Transfusion Medicine, Langen, Germany.
Eberhard HildtPaul-Ehrlich-Institut, Department of Virology, Langen, Germany.ORCID 0000-0002-3020-9564
Paul Ehrlich Institut · DE

Funding

European Union’s Horizon 2020 research and innovation programLOEWE center DRUID
6 · The paper itself

Abstract

Viral infections trigger the expression of interferons (IFNs) and interferon stimulated genes (ISGs), which are crucial to modulate an antiviral response. The human guanylate binding protein 1 (GBP1) is an ISG and exhibits antiviral activity against several viruses. In a previous study, GBP1 was described to impair replication of the hepatitis C virus (HCV). However, the impact of GBP1 on the HCV life cycle is still enigmatic. To monitor the expression and subcellular distribution of GBP1 and HCV we performed qPCR, Western blot, CLSM and STED microscopy, virus titration and reporter gene assays. In contrast to previous reports, we observed that HCV induces the expression of GBP1. Further, to induce GBP1 expression, the cells were stimulated with IFNγ. GBP1 modulation was achieved either by overexpression of GBP1-Wt or by siRNA-mediated knockdown. Silencing of GBP1 impaired the release of viral particles and resulted in intracellular HCV core accumulation, while overexpression of GBP1 favored viral replication and release. CLSM and STED analyses revealed a vesicular distribution of GBP1 in the perinuclear region. Here, it colocalizes with HCV core around lipid droplets, where it acts as assembly platform and thereby favors HCV morphogenesis and release. Collectively, our results identify an unprecedented function of GBP1 as a pro-viral factor. As such, it is essential for viral assembly and release acting through tethering factors involved in HCV morphogenesis onto the surface of lipid droplets.

Indexed as

GTP-Binding ProteinsHepacivirusHepatitis CHumansInterferonsVirus ReplicationGBP1 protein, humanGTP-Binding ProteinsInterferons

Identifiers

PMID38315728
PMCPMC10868826
OpenAlexW4391528510

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.