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• W2023626183 abstract "The influenza A virus NS1 protein is a virulence factor and an antagonist of host cell innate immune responses. During virus infection NS1 protein has several functions both in the nucleus and in the cytoplasm and its intracellular localization is regulated by one or two nuclear localization signals (NLS) and a nuclear export signal (NES). In order to investigate the role of NS1 NES in intracellular localization, virus life cycle and host interferon responses, we generated recombinant A/Udorn/72 viruses harboring point mutations in the NES sequence. NS1 NES was found to be inactivated by several of the mutations resulting in nuclear retention of NS1 at late stages of infection confirming that this sequence is a bona fide functional NES. Some of the mutant viruses showed reduced growth properties in cell culture, inability to antagonize host cell interferon production and increased p-IRF3 levels, but no clear correlation between these phenotypes and NS1 localization could be made. Impaired activation of Akt phosphorylation by the replication-deficient viruses indicates possible disruption of NS1-p85β interaction by mutations in the NES region. We conclude that mutations within the NS1 NES result in impairment of several NS1 functions which extends further from the NES site being only involved in regulating the nuclear-cytoplasmic trafficking of NS1." @default.
• W2023626183 created "2016-06-24" @default.
• W2023626183 creator A5007995979 @default.
• W2023626183 creator A5011996258 @default.
• W2023626183 creator A5043246091 @default.
• W2023626183 date "2014-07-14" @default.
• W2023626183 modified "2023-10-16" @default.
• W2023626183 title "Mutations within the conserved NS1 nuclear export signal lead to inhibition of influenza A virus replication" @default.
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• W2023626183 doi "https://doi.org/10.1186/1743-422x-11-128" @default.
• W2023626183 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4112715" @default.
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• W2023626183 hasPublicationYear "2014" @default.
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