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- W2897318629 abstract "ABSTRACT Influenza A viruses are able to adapt to restrictive conditions due to their high mutation rates. Here, we addressed the question by which mechanisms influenza A viruses may escape restriction by the cellular importin-α7 protein, a component of the nuclear import machinery required for avian-mammalian adaptation and replicative fitness in human cells. Therefore, we assessed viral evolution in mice lacking the importin-α7 gene. Here, we show that particularly three mutations occur with high frequency in the viral NP protein (G102R, M105K and D375N) in a specific structural area upon in vivo adaptation. Moreover, our findings suggest that the adaptive NP mutations mediate viral escape from importin-α7 requirement likely due to the utilization of alternative interaction sites in NP beyond the classical nuclear localization signal and importin-α isoforms. However, viral escape from importin-α7 is, at least in part, associated with reduced replicative fitness in human cells." @default.
- W2897318629 created "2018-10-26" @default.
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- W2897318629 date "2018-10-19" @default.
- W2897318629 modified "2023-10-02" @default.
- W2897318629 title "Alternative interaction sites in the influenza A virus nucleoprotein mediate viral escape from the importin-α7 mediated nuclear import pathway" @default.
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- W2897318629 doi "https://doi.org/10.1101/447979" @default.
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