Structural highlights
Function
NS6_SARS Disrupts bidirectional nucleocytoplasmic transport by interacting with host RAE1-NUP98 complex (PubMed:33849972). Disrupts cell nuclear import complex formation also by tethering karyopherin alpha 2 and karyopherin beta 1 to the membrane (PubMed:17596301). Retention of import factors at the ER/Golgi membrane leads to a loss of transport into the nucleus (PubMed:17596301). Thereby prevents STAT1 nuclear translocation in response to interferon signaling, thus blocking the expression of interferon stimulated genes (ISGs) that display multiple antiviral activities (PubMed:17596301).[1] [2]
References
- ↑ Frieman M, Yount B, Heise M, Kopecky-Bromberg SA, Palese P, Baric RS. Severe acute respiratory syndrome coronavirus ORF6 antagonizes STAT1 function by sequestering nuclear import factors on the rough endoplasmic reticulum/Golgi membrane. J Virol. 2007 Sep;81(18):9812-24. doi: 10.1128/JVI.01012-07. Epub 2007 Jun 27. PMID:17596301 doi:http://dx.doi.org/10.1128/JVI.01012-07
- ↑ Addetia A, Lieberman NAP, Phung Q, Hsiang TY, Xie H, Roychoudhury P, Shrestha L, Loprieno MA, Huang ML, Gale M Jr, Jerome KR, Greninger AL. SARS-CoV-2 ORF6 Disrupts Bidirectional Nucleocytoplasmic Transport through Interactions with Rae1 and Nup98. mBio. 2021 Apr 13;12(2). pii: mBio.00065-21. doi: 10.1128/mBio.00065-21. PMID:33849972 doi:http://dx.doi.org/10.1128/mBio.00065-21
