Evidence map›Paper›PMID 38295168›Full record

ArticleScience advances2024

G3BP1-dependent condensation of translationally inactive viral RNAs antagonizes infection.

James M Burke, Oshani C Ratnayake, J Monty Watkins, Rushika Perera, Roy Parker

Abstract read
In one paragraph

Article in Science advances, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
–field-weighted citation impact
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

32 citing papers in PubMed.

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  9. SARS-CoV-2 and MERS-CoV disrupt host protein synthesis via nsp1 with differential effects on the integrated stress response.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  10. Article
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  13. m6A epigenetic modification of viral RNA is critical for the transmission cycle of mosquito-borne flaviviruses.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  14. Article
  15. Article
  16. Exploration of Novel Markers in Tan Sheep Spermatogenesis.Animals : an open access journal from MDPI · 2026
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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.

James M BurkeDepartment of Molecular Medicine, The Herbert Wertheim UF Scripps Institute for Biomedical Innovation & Technology, Jupiter, FL 33458, USA.ORCID 0000-0002-5525-3641
Oshani C RatnayakeCenter for Vector-Borne and Infectious Diseases, Department of Microbiology, Immunology and Pathology, Colorado State University, Fort Collins, CO 80523, USA.ORCID 0000-0002-1036-4575
J Monty WatkinsDepartment of Molecular Medicine, The Herbert Wertheim UF Scripps Institute for Biomedical Innovation & Technology, Jupiter, FL 33458, USA.ORCID 0000-0002-3552-5734
Rushika PereraCenter for Vector-Borne and Infectious Diseases, Department of Microbiology, Immunology and Pathology, Colorado State University, Fort Collins, CO 80523, USA.ORCID 0000-0001-6798-2537
Roy ParkerHoward Hughes Medical Institute, University of Colorado Boulder, Boulder, CO 80303, USA.ORCID 0000-0002-8412-4152

Funding

Understanding the OAS/RNase L pathway during pathogenic viral infectionsR35GM151249 · NIGMS · UNIVERSITY OF FLORIDA · PI James M Burke · 2023 to 2026
$1.9M
Determining the specificity and biological functions of widespread host mRNA degradation by RNase LF32AI145112 · NIAID · UNIVERSITY OF COLORADO · PI BURKE, JAMES M · 2019 to 2021
$200k
NIAID NIH HHS F32 AI145112NIGMS NIH HHS R35 GM151249
6 · The paper itself

Abstract

G3BP1 is an RNA binding protein that condenses untranslating messenger RNAs into stress granules (SGs). G3BP1 is inactivated by multiple viruses and is thought to antagonize viral replication by SG-enhanced antiviral signaling. Here, we show that neither G3BP1 nor SGs generally alter the activation of innate immune pathways. Instead, we show that the RNAs encoded by West Nile virus, Zika virus, and severe acute respiratory syndrome coronavirus 2 are prone to G3BP1-dependent RNA condensation, which is enhanced by limiting translation initiation and correlates with the disruption of viral replication organelles and viral RNA replication. We show that these viruses counteract condensation of their RNA genomes by inhibiting the RNA condensing function of G3BP proteins, hijacking the RNA decondensing activity of eIF4A, and/or maintaining efficient translation. These findings argue that RNA condensation can function as an intrinsic antiviral mechanism, which explains why many viruses inactivate G3BP proteins and suggests that SGs may have arisen as a vestige of this antiviral mechanism.

Indexed as

Zika VirusZika Virus InfectionAntiviral AgentsDNA HelicasesHumansPoly-ADP-Ribose Binding ProteinsRNA HelicasesRNA Recognition Motif ProteinsRNA, ViralAntiviral AgentsDNA HelicasesG3BP1 protein, humanPoly-ADP-Ribose Binding ProteinsRNA HelicasesRNA Recognition Motif ProteinsRNA, Viral

Identifiers

PMID38295168
PMCPMC10830107

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LicenceCC BY
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Registered trials

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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.