Evidence map›Paper›PMID 36722971›Full record

ArticleJournal of virology2023

CP204L Is a Multifunctional Protein of African Swine Fever Virus That Interacts with the VPS39 Subunit of the Homotypic Fusion and Vacuole Protein Sorting Complex and Promotes Lysosome Clustering.

Katarzyna Magdalena Dolata, Walter Fuchs, Grégory Caignard, Juliette Dupré, Katrin Pannhorst, Sandra Blome, Thomas C Mettenleiter, Axel Karger

Open access · hybridAbstract 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 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
5.9field-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

16 citing papers in PubMed, 17 citations in OpenAlex.

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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

8 authors at 2 institutions in 2 countries.

Katarzyna Magdalena DolataInstitute of Molecular Virology and Cell Biology, Friedrich-Loeffler-Institut, Greifswald-Insel Riems, Germany.ORCID 0000-0001-7009-1778
Walter FuchsInstitute of Molecular Virology and Cell Biology, Friedrich-Loeffler-Institut, Greifswald-Insel Riems, Germany.ORCID 0000-0002-7670-451X
Grégory CaignardUMR Virologie, INRAE, Ecole Nationale Vétérinaire d'Alfort, Laboratoire de Santé Animale d'Alfort, Anses, Université Paris-Est, Maisons-Alfort, France.
Juliette DupréUMR Virologie, INRAE, Ecole Nationale Vétérinaire d'Alfort, Laboratoire de Santé Animale d'Alfort, Anses, Université Paris-Est, Maisons-Alfort, France.
Katrin PannhorstInstitute of Molecular Virology and Cell Biology, Friedrich-Loeffler-Institut, Greifswald-Insel Riems, Germany.
Sandra BlomeInstitute of Diagnostic Virology, Friedrich-Loeffler-Institut, Greifswald-Insel Riems, Germany.ORCID 0000-0001-5465-5609
Thomas C MettenleiterInstitute of Molecular Virology and Cell Biology, Friedrich-Loeffler-Institut, Greifswald-Insel Riems, Germany.
Axel KargerInstitute of Molecular Virology and Cell Biology, Friedrich-Loeffler-Institut, Greifswald-Insel Riems, Germany.ORCID 0000-0002-0054-7394
Friedrich-Loeffler-Institut · DEÉcole Nationale Vétérinaire d'Alfort · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Virus replication depends on a complex interplay between viral and host proteins. In the case of African swine fever virus (ASFV), a large DNA virus, only a few virus-host protein-protein interactions have been identified to date. In this study, we demonstrate that the ASFV protein CP204L interacts with the cellular homotypic fusion and protein sorting (HOPS) protein VPS39, blocking its association with the lysosomal HOPS complex, which modulates endolysosomal trafficking and promotes lysosome clustering. Instead, CP204L and VPS39 are targeted to virus factories and localized at the periphery of the virus DNA replication sites. Furthermore, we show that loss of VPS39 reduces the levels of virus proteins synthesized in the early phase of infection and delays ASFV replication but does not completely inhibit it. Collectively, these results identify a novel virus-host protein interaction that modulates host membrane rearrangement during infection and provide evidence that CP204L is a multifunctional protein engaged in distinct steps of the ASFV life cycle.

Indexed as

African Swine FeverAfrican Swine Fever VirusViral ProteinsVirus ReplicationAnimalsLysosomesProtein TransportSwineVacuolesViral ProteinsAfrican swine fever virusASFVCP204LHOPS complexlysosomesvirus-host interactionVPS39

Identifiers

PMID36722971
PMCPMC9972913
OpenAlexW4318753837

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.