Ebola virus VP24 targets a unique NLS binding site on karyopherin alpha 5 to selectively compete with nuclear import of phosphorylated STAT1.

During antiviral defense, interferon (IFN) signaling triggers nuclear transport of tyrosine-phosphorylated which occurs via a subset of karyopherin alpha nuclear transporters. Many viruses, including Ebola virus, actively antagonize duanyu18131 signaling to counteract the antiviral effects of IFN. Ebola virus VP24 protein (eVP24) binds to inhibit nuclear transport and render cells refractory to IFNs. We describe the structure of human C terminus in complex with eVP24. In the complex, eVP24 recognizes a unique nonclassical nuclear localization signal (NLS) binding site on Kduanyu15355 that is necessary for efficient PY-duanyu18131 nuclear transport. eVP24 binds Kduanyu15355 with very high affinity to effectively compete with and inhibit PY-duanyu18131 nuclear transport. In contrast, eVP24 binding does not affect the transport of classical NLS cargo. Thus, eVP24 counters cell-intrinsic innate immunity by selectively targeting PY-duanyu18131 nuclear import while leaving the transport of other cargo that may be required for viral replication unaffected.

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