ArticleScientific reports2016
Nucleolin interacts with influenza A nucleoprotein and contributes to viral ribonucleoprotein complexes nuclear trafficking and efficient influenza viral replication.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 44 citations in OpenAlex.
- Host nucleolin-targeting unique peptide drugs as potent broad-spectrum anti-influenza therapies.PNAS nexus · 2026Article
- How Oncovirus Affects Drug Resistance in Cancer Cells.Recent patents on anti-cancer drug discovery · 2026Review
- Nucleolin a Central Player in Host Virus Interactions and its Role in Viral Progeny Production.Molecular biotechnology · 2026Review
- TfR1 facilitates influenza virus endocytosis and uncoating by interacting with NA and M1 via extracellular and intracellular domains.PLoS pathogens · 2025Article
- Exploring Therapeutic Targets From Spreading Patterns Against Respiratory Syncytial Virus.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2025Review
- Nucleophosmin 1 inhibits the replication of influenza A virus by competitively binding viral RNA with viral proteins.Virologica Sinica · 2025Article
- Cell binding, uptake, and infection of influenza A virus using recombinant antibody-based receptors.Journal of virology · 2025Article
- Influenza A virus RNA localisation and the interceding trafficking pathways of the host cell.PLoS pathogens · 2025Review
- Analysis of the interaction of influenza a virus nucleoprotein with host cell nucleolin.Archives of virology · 2024Article
- Reduced Non-Specific Binding of Super-Resolution DNA-PAINT Markers by Shielded DNA-PAINT Labeling Protocols.Small (Weinheim an der Bergstrasse, Germany) · 2024Article
- Unravelling the interaction between Influenza virus and the nuclear pore complex: insights into viral replication and host immune response.Virusdisease · 2024Review
- Article
- The RGG motif proteins: Interactions, functions, and regulations.Wiley interdisciplinary reviews. RNA · 2023Review
- Nucleolin: a cell portal for viruses, bacteria, and toxins.Cellular and molecular life sciences : CMLS · 2022Review
- Altered gene expression in human brain microvascular endothelial cells in response to the infection of influenza H1N1 virus.Animal diseases · 2022Article
- Acetylation, Methylation and Allysine Modification Profile of Viral and Host Proteins during Influenza A Virus Infection.Viruses · 2021Article
- Manipulation of Cellular Processes via Nucleolus Hijaking in the Course of Viral Infection in Mammals.Cells · 2021Review
- Nucleolin Promotes IRES-Driven Translation of Foot-and-Mouth Disease Virus by Supporting the Assembly of Translation Initiation Complexes.Journal of virology · 2021Article
- Anti-Influenza Activity of the Ribonuclease Binase: Cellular Targets Detected by Quantitative Proteomics.International journal of molecular sciences · 2020Article
- Catechin inhibiting the H1N1 influenza virus associated with the regulation of autophagy.Journal of the Chinese Medical Association : JCMA · 2020Article
Corrections and comments
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Authors and funding
15 authors at 8 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Influenza viruses replicate their single-stranded RNA genomes in the nucleus of infected cells and these replicated genomes (vRNPs) are then exported from the nucleus to the cytoplasm and plasma membrane before budding. To achieve this export, influenza viruses hijack the host cell export machinery. However, the complete mechanisms underlying this hijacking remain not fully understood. We have previously shown that influenza viruses induce a marked alteration of the nucleus during the time-course of infection and notably in the nucleolar compartment. In this study, we discovered that a major nucleolar component, called nucleolin, is required for an efficient export of vRNPs and viral replication. We have notably shown that nucleolin interacts with the viral nucleoprotein (NP) that mainly constitutes vRNPs. Our results suggest that this interaction could allow vRNPs to "catch" the host cell export machinery, a necessary step for viral replication.
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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.