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10.1073/pnas.2016650117 http://scihub22266oqcxt.onion/10.1073/pnas.2016650117 33097660!7668094!33097660     free     free     free Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Proc+Natl+Acad+Sci+U+S+A 2020 ; 117 (45): 28344-28354 Nephropedia Template TP {{tp|p=33097660|t=2020. SARS-CoV-2 Orf6 hijacks Nup98 to block STAT nuclear import and antagonize interferon signaling |pdf=|usr=}}{{33097660}} gab.com Text SARS-CoV-2 Orf6 hijacks Nup98 to block STAT nuclear import and antagonize interferon signaling JO: Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=33097660 #FOAvip Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is the causative agent of the ongoing coronavirus disease 2019 (COVID-19) pandemic that is a serious global health problem. Evasion of IFN-mediated antiviral signaling is a common defense strategy that pathogenic viruses use to replicate and propagate in their host. In this study, we show that SARS-CoV-2 is able to efficiently block STAT1 and STAT2 nuclear translocation in order to impair transcriptional induction of IFN-stimulated genes (ISGs). Our results demonstrate that the viral accessory protein Orf6 exerts this anti-IFN activity. We found that SARS-CoV-2 Orf6 localizes at the nuclear pore complex (NPC) and directly interacts with Nup98-Rae1 via its C-terminal domain to impair docking of cargo-receptor (karyopherin/importin) complex and disrupt nuclear import. In addition, we show that a methionine-to-arginine substitution at residue 58 impairs Orf6 binding to the Nup98-Rae1 complex and abolishes its IFN antagonistic function. All together our data unravel a mechanism of viral antagonism in which a virus hijacks the Nup98-Rae1 complex to overcome the antiviral action of IFN. Twit Text FOAVip SARS-CoV-2 Orf6 hijacks Nup98 to block STAT nuclear import and antagonize interferon signaling ????Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=33097660 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=33097660 #FOAvip English Wikipedia <ref>{{Cite pmid|33097660}}</ref> SARS-CoV-2 Orf6 hijacks Nup98 to block STAT nuclear import and antagonize interferon signaling #MMPMID33097660 Miorin L; Kehrer T; Sanchez-Aparicio MT; Zhang K; Cohen P; Patel RS; Cupic A; Makio T; Mei M; Moreno E; Danziger O; White KM; Rathnasinghe R; Uccellini M; Gao S; Aydillo T; Mena I; Yin X; Martin-Sancho L; Krogan NJ; Chanda SK; Schotsaert M; Wozniak RW; Ren Y; Rosenberg BR; Fontoura BMA; Garcia-Sastre A Proc Natl Acad Sci U S A 2020[Nov]; 117 (45): 28344-28354 PMID33097660show ga Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is the causative agent of the ongoing coronavirus disease 2019 (COVID-19) pandemic that is a serious global health problem. Evasion of IFN-mediated antiviral signaling is a common defense strategy that pathogenic viruses use to replicate and propagate in their host. In this study, we show that SARS-CoV-2 is able to efficiently block STAT1 and STAT2 nuclear translocation in order to impair transcriptional induction of IFN-stimulated genes (ISGs). Our results demonstrate that the viral accessory protein Orf6 exerts this anti-IFN activity. We found that SARS-CoV-2 Orf6 localizes at the nuclear pore complex (NPC) and directly interacts with Nup98-Rae1 via its C-terminal domain to impair docking of cargo-receptor (karyopherin/importin) complex and disrupt nuclear import. In addition, we show that a methionine-to-arginine substitution at residue 58 impairs Orf6 binding to the Nup98-Rae1 complex and abolishes its IFN antagonistic function. All together our data unravel a mechanism of viral antagonism in which a virus hijacks the Nup98-Rae1 complex to overcome the antiviral action of IFN. |Active Transport, Cell Nucleus[MESH] |Animals[MESH] |Binding Sites[MESH] |COVID-19/*metabolism[MESH] |Chlorocebus aethiops[MESH] |HEK293 Cells[MESH] |Humans[MESH] |Interferons/*metabolism[MESH] |Nuclear Matrix-Associated Proteins/chemistry/metabolism[MESH] |Nuclear Pore Complex Proteins/*metabolism[MESH] |Nuclear Pore/*metabolism[MESH] |Nucleocytoplasmic Transport Proteins/chemistry/metabolism[MESH] |Protein Binding[MESH] |STAT1 Transcription Factor/*metabolism[MESH] |STAT2 Transcription Factor/*metabolism[MESH] |Signal Transduction[MESH] |Vero Cells[MESH]SARS-CoV-2 Orf6 hijacks Nup98 to block STAT nuclear import and antagon(epmc).pdf DeepDyve Pubget Overpricing