Evidence map›Paper›PMID 39549315›Full record

ArticleVirology2025

Viral condensates formed by Pea enation mosaic virus 2 sequester ribosomal components and suppress translation.

Shelby L Brown, Jared P May

Abstract read
In one paragraph

Article in Virology, 2025. 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
–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

3 citing papers in PubMed.

  1. Article
  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

2 authors.

Shelby L BrownDivision of Biological and Biomedical Systems, School of Science and Engineering, University of Missouri-Kansas City, 5009 Rockhill Road, Kansas City, MO, 64110, USA.
Jared P MayDivision of Biological and Biomedical Systems, School of Science and Engineering, University of Missouri-Kansas City, 5009 Rockhill Road, Kansas City, MO, 64110, USA. Electronic address: jpmay@umkc.edu.

Funding

Dissecting the Impact of Viral Biomolecular Condensates on Cellular Translation and RNA Interference (RNAi)R35GM154909 · NIGMS · UNIVERSITY OF MISSOURI KANSAS CITY · PI Jared Paul May · 2024 to 2026
$1.2M
NIGMS NIH HHS R35 GM154909
6 · The paper itself

Abstract

Viral proteins with intrinsic disorder, such as the p26 movement protein from Pea enation mosaic virus 2 (PEMV2), can phase separate and form condensates that aid specific stages of virus replication. However, little is known about the impact of viral condensate formation on essential cellular processes, like translation. In this study, we performed mass spectrometry on affinity-purified p26 condensates and found an enrichment of RNA-binding proteins involved in translation and ribosome biogenesis. Puromycin assays and polysome profiling show that ectopic p26 expression suppresses ribosome assembly and translation in Nicotiana benthamiana, mirroring defects in late-stage PEMV2 infection. Despite interactions with the 2'-O-methyltransferase fibrillarin, p26 does not inhibit translation by altering rRNA methylation but instead binds directly to rRNAs and decreases their solubility. Disruption of ribosome assembly and translation by p26 during late PEMV2 infection may promote stages of the virus replication cycle that are incompatible with translation, including systemic movement.

Indexed as

NicotianaProtein BiosynthesisRibosomesVirus ReplicationBiomolecular CondensatesPlant DiseasesPlant Viral Movement ProteinsRNA-Binding ProteinsRNA, RibosomalPlant Viral Movement ProteinsRNA-Binding ProteinsRNA, RibosomalCondensateLLPSPhase separationPlant virusRNA virusTranslation

Identifiers

PMID39549315
PMCPMC11649027

What OpenQuestion holds

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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.