Evidence map›Paper›PMID 34578359›Full record

ArticleViruses2021

Evidence That the Adenovirus Single-Stranded DNA Binding Protein Mediates the Assembly of Biomolecular Condensates to Form Viral Replication Compartments.

Paloma Hidalgo, Arturo Pimentel, Diana Mojica-Santamaría, Konstantin von Stromberg, Helga Hofmann-Sieber, Christian Lona-Arrona, Thomas Dobner, Ramón A González

Open access · goldAbstract read
In one paragraph

Article in Viruses, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.9field-weighted citation impact, top 13% 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

19 citing papers in PubMed, 32 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

8 authors at 3 institutions in 2 countries.

Paloma HidalgoCentro de Investigación en Dinámica Celular, Instituto de Investigación en Ciencias Básicas y Aplicadas, Universidad Autónoma del Estado de Morelos, Cuernavaca 62209, Mexico.ORCID 0000-0001-5867-0128
Arturo PimentelLaboratorio Nacional de Microscopía Avanzada (LNMA), Instituto de Biotecnología, Universidad Nacional Autónoma de México (UNAM), Cuernavaca 62210, Mexico.ORCID 0000-0001-8569-0466
Diana Mojica-SantamaríaCentro de Investigación en Dinámica Celular, Instituto de Investigación en Ciencias Básicas y Aplicadas, Universidad Autónoma del Estado de Morelos, Cuernavaca 62209, Mexico.
Konstantin von StrombergLeibniz Institute for Experimental Virology (HPI), 20251 Hamburg, Germany.
Helga Hofmann-SieberLeibniz Institute for Experimental Virology (HPI), 20251 Hamburg, Germany.
Christian Lona-ArronaCentro de Investigación en Dinámica Celular, Instituto de Investigación en Ciencias Básicas y Aplicadas, Universidad Autónoma del Estado de Morelos, Cuernavaca 62209, Mexico.
Thomas DobnerLeibniz Institute for Experimental Virology (HPI), 20251 Hamburg, Germany.
Ramón A GonzálezCentro de Investigación en Dinámica Celular, Instituto de Investigación en Ciencias Básicas y Aplicadas, Universidad Autónoma del Estado de Morelos, Cuernavaca 62209, Mexico.ORCID 0000-0001-9689-8529
Leibniz Institute of Virology (LIV) · DEUniversidad Autónoma del Estado de Morelos · MXUniversidad Nacional Autónoma de México · MX

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A common viral replication strategy is characterized by the assembly of intracellular compartments that concentrate factors needed for viral replication and simultaneously conceal the viral genome from host-defense mechanisms. Recently, various membrane-less virus-induced compartments and cellular organelles have been shown to represent biomolecular condensates (BMCs) that assemble through liquid-liquid phase separation (LLPS). In the present work, we analyze biophysical properties of intranuclear replication compartments (RCs) induced during human adenovirus (HAdV) infection. The viral ssDNA-binding protein (DBP) is a major component of RCs that contains intrinsically disordered and low complexity proline-rich regions, features shared with proteins that drive phase transitions. Using fluorescence recovery after photobleaching (FRAP) and time-lapse studies in living HAdV-infected cells, we show that DBP-positive RCs display properties of liquid BMCs, which can fuse and divide, and eventually form an intranuclear mesh with less fluid-like features. Moreover, the transient expression of DBP recapitulates the assembly and liquid-like properties of RCs in HAdV-infected cells. These results are of relevance as they indicate that DBP may be a scaffold protein for the assembly of HAdV-RCs and should contribute to future studies on the role of BMCs in virus-host cell interactions.

Indexed as

Biomolecular CondensatesAdenoviridaeAdenoviridae InfectionsAdenoviruses, HumanCell LineDNA-Binding ProteinsHost Microbial InteractionsHumansOrganellesProtein DomainsViral ProteinsViral Replication CompartmentsVirus ReplicationDNA-Binding ProteinsViral Proteinsbiomolecular condensates (BMCs)human adenovirus type 5 (HAdV-5)liquid-liquid phase separation (LLPS)Replication Compartments (RCs)ssDNA-binding protein (DBP)virus-induced cellular compartmentalization

Identifiers

PMID34578359
PMCPMC8473285
OpenAlexW3197430400

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.