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10.1038/s41421-021-00268-z http://scihub22266oqcxt.onion/10.1038/s41421-021-00268-z 33947832!8096138!33947832     free     free     free Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Cell+Discov 2021 ; 7 (1): 31 Nephropedia Template TP {{tp|p=33947832|t=2021. The SARS-CoV-2 protein ORF3a inhibits fusion of autophagosomes with lysosomes |pdf=|usr=}}{{33947832}} gab.com Text The SARS-CoV-2 protein ORF3a inhibits fusion of autophagosomes with lysosomes JO: Cell Discov http://www.kidney.de/pget.php?&tw=1&pmid=33947832 #FOAvip Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has caused the ongoing coronavirus disease 2019 pandemic. How SARS-CoV-2 regulates cellular responses to escape clearance by host cells is unknown. Autophagy is an intracellular lysosomal degradation pathway for the clearance of various cargoes, including viruses. Here, we systematically screened 28 viral proteins of SARS-CoV-2 and identified that ORF3a strongly inhibited autophagic flux by blocking the fusion of autophagosomes with lysosomes. ORF3a colocalized with lysosomes and interacted with VPS39, a component of the homotypic fusion and protein sorting (HOPS) complex. The ORF3a-VPS39 interaction prohibited the binding of HOPS with RAB7, which prevented the assembly of fusion machinery, leading to the accumulation of unfused autophagosomes. These results indicated the potential mechanism by which SARS-CoV-2 escapes degradation; that is, the virus interferes with autophagosome-lysosome fusion. Furthermore, our findings will facilitate strategies targeting autophagy for conferring potential protection against the spread of SARS-CoV-2. Twit Text FOAVip The SARS-CoV-2 protein ORF3a inhibits fusion of autophagosomes with lysosomes ????Cell Discov http://www.kidney.de/pget.php?&tw=1&pmid=33947832 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=33947832 #FOAvip English Wikipedia <ref>{{Cite pmid|33947832}}</ref> The SARS-CoV-2 protein ORF3a inhibits fusion of autophagosomes with lysosomes #MMPMID33947832 Zhang Y; Sun H; Pei R; Mao B; Zhao Z; Li H; Lin Y; Lu K Cell Discov 2021[May]; 7 (1): 31 PMID33947832show ga Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has caused the ongoing coronavirus disease 2019 pandemic. How SARS-CoV-2 regulates cellular responses to escape clearance by host cells is unknown. Autophagy is an intracellular lysosomal degradation pathway for the clearance of various cargoes, including viruses. Here, we systematically screened 28 viral proteins of SARS-CoV-2 and identified that ORF3a strongly inhibited autophagic flux by blocking the fusion of autophagosomes with lysosomes. ORF3a colocalized with lysosomes and interacted with VPS39, a component of the homotypic fusion and protein sorting (HOPS) complex. The ORF3a-VPS39 interaction prohibited the binding of HOPS with RAB7, which prevented the assembly of fusion machinery, leading to the accumulation of unfused autophagosomes. These results indicated the potential mechanism by which SARS-CoV-2 escapes degradation; that is, the virus interferes with autophagosome-lysosome fusion. Furthermore, our findings will facilitate strategies targeting autophagy for conferring potential protection against the spread of SARS-CoV-2. äThe SARS-CoV-2 protein ORF3a inhibits fusion of autophagosomes with ly(epmc).pdf DeepDyve Pubget Overpricing