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10.1038/s41421-021-00279-w

http://scihub22266oqcxt.onion/10.1038/s41421-021-00279-w
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34031383!8143069!34031383
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suck abstract from ncbi


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pmid34031383      Cell+Discov 2021 ; 7 (1): 37
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  • Targeting novel LSD1-dependent ACE2 demethylation domains inhibits SARS-CoV-2 replication #MMPMID34031383
  • Tu WJ; McCuaig RD; Melino M; Rawle DJ; Le TT; Yan K; Suhrbier A; Johnston RL; Koufariotis LT; Waddell N; Cross EM; Tsimbalyuk S; Bain A; Ahern E; Collinson N; Phipps S; Forwood JK; Seddiki N; Rao S
  • Cell Discov 2021[May]; 7 (1): 37 PMID34031383show ga
  • Treatment options for COVID-19 remain limited, especially during the early or asymptomatic phase. Here, we report a novel SARS-CoV-2 viral replication mechanism mediated by interactions between ACE2 and the epigenetic eraser enzyme LSD1, and its interplay with the nuclear shuttling importin pathway. Recent studies have shown a critical role for the importin pathway in SARS-CoV-2 infection, and many RNA viruses hijack this axis to re-direct host cell transcription. LSD1 colocalized with ACE2 at the cell surface to maintain demethylated SARS-CoV-2 spike receptor-binding domain lysine 31 to promote virus-ACE2 interactions. Two newly developed peptide inhibitors competitively inhibited virus-ACE2 interactions, and demethylase access to significantly inhibit viral replication. Similar to some other predominantly plasma membrane proteins, ACE2 had a novel nuclear function: its cytoplasmic domain harbors a nuclear shuttling domain, which when demethylated by LSD1 promoted importin-alpha-dependent nuclear ACE2 entry following infection to regulate active transcription. A novel, cell permeable ACE2 peptide inhibitor prevented ACE2 nuclear entry, significantly inhibiting viral replication in SARS-CoV-2-infected cell lines, outperforming other LSD1 inhibitors. These data raise the prospect of post-exposure prophylaxis for SARS-CoV-2, either through repurposed LSD1 inhibitors or new, nuclear-specific ACE2 inhibitors.
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