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10.1002/mco2.92 http://scihub22266oqcxt.onion/10.1002/mco2.92 34909756!8661858!34909756     free     free     free Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       MedComm+(2020) 2021 ; 2 (4): 798-809 Nephropedia Template TP {{tp|p=34909756|t=2021. SARS-CoV-2 spike protein harnesses SNX27-mediated endocytic recycling pathway |pdf=|usr=}}{{34909756}} gab.com Text SARS-CoV-2 spike protein harnesses SNX27-mediated endocytic recycling pathway JO: MedComm (2020) http://www.kidney.de/pget.php?&tw=1&pmid=34909756 #FOAvip SARS-CoV-2 is an enveloped positive-sense RNA virus that depends on host factors for all stages of its life. Membrane receptor ACE2 is a well-established factor for SARS-CoV-2 docking. In addition to ACE2, whole-genome genetic screens have identified additional proteins, such as endosomal trafficking regulators SNX27 and retromer, as key host factors required for SARS-CoV-2 infection. However, it is poorly understood how SARS-CoV-2 utilize host endocytic transport pathways to produce productive infection. Here, we report that SNX27 interacts with the SARS-CoV-2 spike (S) protein to facilitate S protein surface expression. Interestingly, S protein binds to the PDZ domain of SNX27, although it does not contain a PDZ-binding motif (PDZbm). Either abrogation of the SNX27 PDZ domain or S protein "MTSC" motif, which is critical for SNX27 binding, decreases surface expression of S protein and viral production. Collectively, our study highlights a novel approach utilized by SARS-CoV-2 to facilitate virion trafficking to establish virus infection. Twit Text FOAVip SARS-CoV-2 spike protein harnesses SNX27-mediated endocytic recycling pathway ????MedComm (2020) http://www.kidney.de/pget.php?&tw=1&pmid=34909756 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=34909756 #FOAvip English Wikipedia <ref>{{Cite pmid|34909756}}</ref> SARS-CoV-2 spike protein harnesses SNX27-mediated endocytic recycling pathway #MMPMID34909756 Zhao L; Zhong K; Zhao J; Yong X; Tong A; Jia D MedComm (2020) 2021[Dec]; 2 (4): 798-809 PMID34909756show ga SARS-CoV-2 is an enveloped positive-sense RNA virus that depends on host factors for all stages of its life. Membrane receptor ACE2 is a well-established factor for SARS-CoV-2 docking. In addition to ACE2, whole-genome genetic screens have identified additional proteins, such as endosomal trafficking regulators SNX27 and retromer, as key host factors required for SARS-CoV-2 infection. However, it is poorly understood how SARS-CoV-2 utilize host endocytic transport pathways to produce productive infection. Here, we report that SNX27 interacts with the SARS-CoV-2 spike (S) protein to facilitate S protein surface expression. Interestingly, S protein binds to the PDZ domain of SNX27, although it does not contain a PDZ-binding motif (PDZbm). Either abrogation of the SNX27 PDZ domain or S protein "MTSC" motif, which is critical for SNX27 binding, decreases surface expression of S protein and viral production. Collectively, our study highlights a novel approach utilized by SARS-CoV-2 to facilitate virion trafficking to establish virus infection. äSARS-CoV-2 spike protein harnesses SNX27-mediated endocytic recycling (epmc).pdf DeepDyve Pubget Overpricing