ArticleJournal of virology2002
Functional replacement of the carboxy-terminal two-thirds of the influenza A virus NS1 protein with short heterologous dimerization domains.
Article in Journal of virology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.
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Who cites it
56 citing papers in PubMed, 108 citations in OpenAlex.
- Efficacy of intranasal administration of a truncated NS1 modified live influenza virus vaccine in swine.Vaccine · 2007Trial
- A naturally occurring NS1 variant with effector domain deletion gains growth advantages in influenza virus infection.Emerging microbes & infections · 2025Article
- The C-terminal amino acid motifs of NS1 protein affect the replication and virulence of naturally NS-truncated H1N1 canine influenza virus.Emerging microbes & infections · 2024Article
- Antiviral responses versus virus-induced cellular shutoff: a game of thrones between influenza A virus NS1 and SARS-CoV-2 Nsp1.Frontiers in cellular and infection microbiology · 2024Review
- Pathobiology of an NS1-Truncated H3N2 Swine Influenza Virus Strain in Pigs.Journal of virology · 2022Article
- A Review and Meta-Analysis of Influenza Interactome Studies.Frontiers in microbiology · 2022Review
- A Game of Infection - Song of Respiratory Viruses and Interferons.Frontiers in cellular and infection microbiology · 2022Review
- Article
- 139D in NS1 Contributes to the Virulence of H5N6 Influenza Virus in Mice.Frontiers in veterinary science · 2021Article
- Structural Basis of Human Helicase DDX21 in RNA Binding, Unwinding, and Antiviral Signal Activation.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2020Article
- Review
- Influenza viral vectors expressing two kinds of HA proteins for bivalent vaccines against clade 2.3.4.4 and clade 2.3.2.1 H5 HPAIVs.Scientific reports · 2018Article
- A Naturally Occurring Deletion in the Effector Domain of H5N1 Swine Influenza Virus Nonstructural Protein 1 Regulates Viral Fitness and Host Innate Immunity.Journal of virology · 2018Article
- Mammalian Adaptation of an Avian Influenza A Virus Involves Stepwise Changes in NS1.Journal of virology · 2018Article
- Influenza Virus: A Master Tactician in Innate Immune Evasion and Novel Therapeutic Interventions.Frontiers in immunology · 2018Review
- A comparison of RSV and influenza in vitro kinetic parameters reveals differences in infecting time.PloS one · 2018Article
- Influenza A Virus Virulence Depends on Two Amino Acids in the N-Terminal Domain of Its NS1 Protein To Facilitate Inhibition of the RNA-Dependent Protein Kinase PKR.Journal of virology · 2017Article
- The Influenza NS1 Protein: What Do We Know in Equine Influenza Virus Pathogenesis?Pathogens (Basel, Switzerland) · 2016Review
- Review
- Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
The NS1 protein of influenza A/WSN/33 virus is a 230-amino-acid-long protein which functions as an interferon alpha/beta (IFN-alpha/beta) antagonist by preventing the synthesis of IFN during viral infection. In tissue culture, the IFN inhibitory function of the NS1 protein has been mapped to the RNA binding domain, the first 73 amino acids. Nevertheless, influenza viruses expressing carboxy-terminally truncated NS1 proteins are attenuated in mice. Dimerization of the NS1 protein has previously been shown to be essential for its RNA binding activity. We have explored the ability of heterologous dimerization domains to functionally substitute in vivo for the carboxy-terminal domains of the NS1 protein. Recombinant influenza viruses were generated that expressed truncated NS1 proteins of 126 amino acids, fused to 28 or 24 amino acids derived from the dimerization domains of either the Saccharomyces cerevisiae PUT3 or the Drosophila melanogaster Ncd (DmNcd) proteins. These viruses regained virulence and lethality in mice. Moreover, a recombinant influenza virus expressing only the first 73 amino acids of the NS1 protein was able to replicate in mice lacking three IFN-regulated antiviral enzymes, PKR, RNaseL, and Mx, but not in wild-type (Mx-deficient) mice, suggesting that the attenuation was mainly due to an inability to inhibit the IFN system. Remarkably, a virus with an NS1 truncated at amino acid 73 but fused to the dimerization domain of DmNcd replicated and was also highly pathogenic in wild-type mice. These results suggest that the main biological function of the carboxy-terminal region of the NS1 protein of influenza A virus is the enhancement of its IFN antagonist properties by stabilizing the NS1 dimeric structure.
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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.