ArticleJournal of virology2012
The interactome of the human respiratory syncytial virus NS1 protein highlights multiple effects on host cell biology.
Article in Journal of virology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.
What it found
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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.
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.
Who cites it
47 citing papers in PubMed, 76 citations in OpenAlex.
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- A dual interaction between RSV NS1 and MED25 ACID domain reshapes antiviral responses.PLoS pathogens · 2025Article
- Host Immune Response to Respiratory Syncytial Virus Infection in Children.Influenza and other respiratory viruses · 2025Review
- Molecular basis for human respiratory syncytial virus transcriptional regulator NS1 interactions with MED25.Nature communications · 2025Article
- Multiomics as instrument to promote 3P medical approaches for the overall management of respiratory syncytial viral infections.The EPMA journal · 2025Review
- Introduction to Respiratory Syncytial Virus.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Pathogenicity and virulence of human respiratory syncytial virus: Multifunctional nonstructural proteins NS1 and NS2.Virulence · 2024Review
- Reshaping Our Knowledge: Advancements in Understanding the Immune Response to Human Respiratory Syncytial Virus.Pathogens (Basel, Switzerland) · 2023Review
- Article
- An Unexpected Encounter: Respiratory Syncytial Virus Nonstructural Protein 1 Interacts with Mediator Subunit MED25.Journal of virology · 2022Review
- Review
- Baicalin Induces a Potent Innate Immune Response to Inhibit Respiratory Syncytial Virus ReplicationFrontiers in immunology · 2022Article
- Nuclear-localized human respiratory syncytial virus NS1 protein modulates host gene transcription.Cell reports · 2021Article
- Structural basis for IFN antagonism by human respiratory syncytial virus nonstructural protein 2.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Mass spectrometry-based protein-protein interaction networks for the study of human diseases.Molecular systems biology · 2021Review
- Review
- Addressing Non-linear System Dynamics of Single-Strand RNA Virus-Host Interaction.Frontiers in microbiology · 2020Article
- Respiratory Syncytial Virus's Non-structural Proteins: Masters of Interference.Frontiers in cellular and infection microbiology · 2020Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
Abstract
Viral proteins can have multiple effects on host cell biology. Human respiratory syncytial virus (HRSV) nonstructural protein 1 (NS1) is a good example of this. During the virus life cycle, NS1 can act as an antagonist of host type I and III interferon production and signaling, inhibit apoptosis, suppress dendritic cell maturation, control protein stability, and regulate transcription of host cell mRNAs, among other functions. It is likely that NS1 performs these different roles through interactions with multiple host cell proteins. To investigate this and identify cellular proteins that could interact with NS1, we used quantitative proteomics in combination with green fluorescent protein (GFP)-trap immunoprecipitation and bioinformatic analysis. This analysis identified 221 proteins that were potentially part of complexes that could interact with NS1, with many of these associated with transcriptional regulation as part of the mediator complex, cell cycle regulation, and other functions previously assigned to NS1. Specific immunoprecipitation using the GFP trap was used to confirm the ability of selected cellular proteins to interact individually with NS1. Infection of A549 cells with recombinant viruses deficient in the expression of NS1 and overexpression analysis both demonstrated that NS1 was necessary and sufficient for the enrichment of cells in the G(1) phase of the cell cycle.
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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.