ArticlePLoS pathogens2018
RSV hijacks cellular protein phosphatase 1 to regulate M2-1 phosphorylation and viral transcription.
Article in PLoS pathogens, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.
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Who cites it
52 citing papers in PubMed, 78 citations in OpenAlex.
- Functional minigenome system reveals polymerase features of swine orthopneumovirus.Journal of virology · 2026Article
- In vitro liquid-liquid phase separation induced by respiratory syncytial virus proteins and RNA.Science advances · 2026Article
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- ZNRD2 Mediated Nucleoprotein Aggregation Impairs Respiratory Syncytial Virus Replication.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Venenum bufonis and its active constituents alleviate RSV-induced pneumonia in mice by suppressing macrophage infiltration and NLRP3 inflammasome activation.Virus research · 2026Article
- Can plitidepsin be used as an antiviral against RSV?mSphere · 2025Article
- To be or not to be phosphorylated: understanding the role of Ebola virus nucleoprotein in the dynamic interplay with the transcriptional activator VP30 and the host phosphatase PP2A-B56.Emerging microbes & infections · 2025Article
- Participation of host cell proteins in inclusion bodies of non-segmented RNA virus infected cells: a molecular insight.Virology journal · 2025Review
- Estimating the prevalence of six common respiratory viral infections in Zhangzhou, China using nasopharyngeal swabs in adults and throat swabs in Children.Scientific reports · 2025Article
- Phosphorylation Modifications and Their Role in Viral Pneumonia: Mechanisms and Therapeutic Implications.Infection and drug resistance · 2025Review
- Expression and Purification of Recombinant Respiratory Syncytial Virus Proteins.Methods in molecular biology (Clifton, N.J.) · 2025Article
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- Pathogenicity and virulence of human respiratory syncytial virus: Multifunctional nonstructural proteins NS1 and NS2.Virulence · 2024Review
- Dimerization of Rabies Virus Phosphoprotein and Phosphorylation of Its Nucleoprotein Enhance Their Binding Affinity.Viruses · 2024Article
- CK1 and PP1 regulate Rift Valley fever virus genome replication through L protein phosphorylation.Antiviral research · 2024Article
- Viral PIC-pocketing: RSV sequestration of translational preinitiation complexes into bi-phasic biomolecular condensates.Journal of virology · 2024Article
- Prevention and Potential Treatment Strategies for Respiratory Syncytial Virus.Molecules (Basel, Switzerland) · 2024Review
- Liquid-liquid phase separation: a new perspective on respiratory diseases.Frontiers in immunology · 2024Review
- Hardening of Respiratory Syncytial Virus Inclusion Bodies by Cyclopamine Proceeds through Perturbation of the Interactions of the M2-1 Protein with RNA and the P Protein.International journal of molecular sciences · 2023Article
- Abnormal phase separation of biomacromolecules in human diseases.Acta biochimica et biophysica Sinica · 2023Review
Corrections and comments
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Authors and funding
11 authors at 4 institutions in 2 countries.
Funding
Abstract
Respiratory syncytial virus (RSV) RNA synthesis occurs in cytoplasmic inclusion bodies (IBs) in which all the components of the viral RNA polymerase are concentrated. In this work, we show that RSV P protein recruits the essential RSV transcription factor M2-1 to IBs independently of the phosphorylation state of M2-1. We also show that M2-1 dephosphorylation is achieved by a complex formed between P and the cellular phosphatase PP1. We identified the PP1 binding site of P, which is an RVxF-like motif located nearby and upstream of the M2-1 binding region. NMR confirmed both P-M2-1 and P-PP1 interaction regions in P. When the P-PP1 interaction was disrupted, M2-1 remained phosphorylated and viral transcription was impaired, showing that M2-1 dephosphorylation is required, in a cyclic manner, for efficient viral transcription. IBs contain substructures called inclusion bodies associated granules (IBAGs), where M2-1 and neo-synthesized viral mRNAs concentrate. Disruption of the P-PP1 interaction was correlated with M2-1 exclusion from IBAGs, indicating that only dephosphorylated M2-1 is competent for viral mRNA binding and hence for a previously proposed post-transcriptional function.
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Registered trials
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.