Evidence map›Paper›PMID 42066094›Full record

ArticleScience advances2026

In vitro liquid-liquid phase separation induced by respiratory syncytial virus proteins and RNA.

Vincent Basse, Tanushree Agarwal, Tomas Sneideris, Charles-Adrien Richard, Joris Troussier, Jean-Jacques Vasseur, Françoise Debart, Jean-François Eléouët, Ella de Csillery, Tuomas Knowles and 1 more

Abstract read
In one paragraph

Article in Science advances, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing 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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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.

Vincent BasseUnité de Virologie et Immunologie Moléculaires (VIM), Université Paris-Saclay, INRAE, Jouy-en-Josas, France.ORCID 0009-0005-5311-1120
Tanushree AgarwalDepartment of Chemistry, Centre for Misfolding Disease, University of Cambridge, Cambridge, CB2 1EW, UK.ORCID 0009-0001-5270-9420
Tomas SneiderisDepartment of Chemistry, Centre for Misfolding Disease, University of Cambridge, Cambridge, CB2 1EW, UK.ORCID 0000-0001-5285-871X
Charles-Adrien RichardUnité de Virologie et Immunologie Moléculaires (VIM), Université Paris-Saclay, INRAE, Jouy-en-Josas, France.ORCID 0000-0001-5306-2297
Joris TroussierIBMM, Université de Montpellier, ENSCM, CNRS, UMR, 5247, Montpellier, France.
Jean-Jacques VasseurIBMM, Université de Montpellier, ENSCM, CNRS, UMR, 5247, Montpellier, France.ORCID 0000-0002-4379-6139
Françoise DebartIBMM, Université de Montpellier, ENSCM, CNRS, UMR, 5247, Montpellier, France.ORCID 0000-0003-3422-3926
Jean-François EléouëtUnité de Virologie et Immunologie Moléculaires (VIM), Université Paris-Saclay, INRAE, Jouy-en-Josas, France.ORCID 0000-0002-7361-4885
Ella de CsilleryDepartment of Chemistry, Centre for Misfolding Disease, University of Cambridge, Cambridge, CB2 1EW, UK.ORCID 0000-0001-5917-9349
Tuomas KnowlesDepartment of Chemistry, Centre for Misfolding Disease, University of Cambridge, Cambridge, CB2 1EW, UK.ORCID 0000-0002-7879-0140
Marie GallouxUnité de Virologie et Immunologie Moléculaires (VIM), Université Paris-Saclay, INRAE, Jouy-en-Josas, France.ORCID 0000-0001-7477-8489

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Respiratory syncytial virus (RSV) causes severe respiratory infections, with viral replication occurring in cytoplasmic membraneless viral factories formed by liquid-liquid phase separation (LLPS). The interactions among the RSV nucleoprotein N, phosphoprotein P, transcription factor M2-1, and RNA drive these condensates. Here, we used a microfluidic PhaseScan platform, together with biochemical and cellular assays, to systematically characterize LLPS involving RSV proteins and RNA. We identified optimal concentrations of oligomeric N and P tetramers for condensate formation in vitro without crowding agents, demonstrated that monomeric N inhibits LLPS and revealed that M2-1 enhances condensate formation by increasing multivalency. Notably, we found that M2-1 preferentially binds 5' capped RNA, distinguishing it from N, which binds uncapped RNA. These findings elucidate molecular determinants of RSV viral factory assembly and subcompartmentalization, providing insights into viral replication mechanisms and informing potential antiviral strategies targeting LLPS processes.

Indexed as

Phase SeparationRespiratory Syncytial Virus, HumanRNA, ViralHumansMicrofluidicsPhosphoproteinsRespiratory Syncytial Virus InfectionsViral ProteinsVirus ReplicationPhosphoproteinsRNA, ViralViral Proteins

Identifiers

PMID42066094
PMCPMC13134614

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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.