ArticlePLoS pathogens2018
Phospholipid scramblase 1 interacts with influenza A virus NP, impairing its nuclear import and thereby suppressing virus replication.
Article in PLoS pathogens, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 77 papers.
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Who cites it
77 citing papers in PubMed, 106 citations in OpenAlex.
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- Enolase 1 suppresses influenza A virus replication by blocking the nuclear import of the viral ribonucleoprotein complex.Cellular and molecular life sciences : CMLS · 2026Article
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- Broad-spectrum inhibition of influenza A virus replication by blocking the nuclear export of viral ribonucleoprotein complexes.Journal of virology · 2025Article
- Targeted NanoBiT Screening Identifies a Novel Interaction Between SNAPIN and Influenza A Virus M1 Protein.Biology · 2025Article
- CSAD inhibits excessive inflammation during viral infections through the NF-κB signaling pathway.Journal of virology · 2025Article
- TRIM45 restricts influenza virus infection through modulating the chaperone-mediated autophagic degradation of viral PB2 protein.PLoS pathogens · 2025Article
- IFN-inducible human phospholipid scramblase 1 (PLSCR1) protein restricts HIV-1 infection by inhibiting membrane fusion.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Phospholipid Scramblase 1 (PLSCR1) Regulates Interferon-Lambda Receptor 1 (IFN-λR1) and IFN-λ Signaling in Influenza A Virus (IAV) Infection.bioRxiv : the preprint server for biology · 2025Article
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- IFN-inducible Human Phospholipid Scramblase 1 (PLSCR1) Protein Restricts HIV-1 Infection by Inhibiting Membrane Fusion.bioRxiv : the preprint server for biology · 2025Article
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- Antecedent Flu-Like Illness and Onset of Idiopathic Dilated Cardiomyopathy: The DCM Precision Medicine Study.Circulation. Heart failure · 2025Article
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- PLSCR1 suppresses SARS-CoV-2 infection by downregulating cell surface ACE2.Journal of virology · 2025Article
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- LDC000067, a CDK9 inhibitor, unveils promising results in suppressing influenza virus infectionsAntimicrobial agents and chemotherapy · 2025Article
17 more citing papers are in PubMed but not listed here.
Corrections and comments
- Erratum issued
Authors and funding
21 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Transcription and replication of the influenza A virus (IAV) genome occur in the nucleus of infected cells and are carried out by the viral ribonucleoprotein complex (vRNP). As a major component of the vRNP complex, the viral nucleoprotein (NP) mediates the nuclear import of the vRNP complex via its nuclear localization signals (NLSs). Clearly, an effective way for the host to antagonize IAV infection would be by targeting vRNP nuclear import. Here, we identified phospholipid scramblase 1 (PLSCR1) as a binding partner of NP by using a yeast two-hybrid (Y2H) screen. The interaction between NP and PLSCR1 in mammalian cells was demonstrated by using co-immunoprecipitation and pull-down assays. We found that the stable overexpression of PLSCR1 suppressed the nuclear import of NP, hindered the virus life cycle, and significantly inhibited the replication of various influenza subtypes. In contrast, siRNA knockdown or CRISPR/Cas9 knockout of PLSCR1 increased virus propagation. Further analysis indicated that the inhibitory effect of PLSCR1 on the nuclear import of NP was not caused by affecting the phosphorylation status of NP or by stimulating the interferon (IFN) pathways. Instead, PLSCR1 was found to form a trimeric complex with NP and members of the importin α family, which inhibited the incorporation of importin β, a key mediator of the classical nuclear import pathway, into the complex, thus impairing the nuclear import of NP and suppressing virus replication. Our results demonstrate that PLSCR1 negatively regulates virus replication by interacting with NP in the cytoplasm and preventing its nuclear import.
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