Author: Dorothea Bestle; Miriam Ruth Heindl; Hannah Limburg; Thuy Van Lam van; Oliver Pilgram; Hong Moulton; David A. Stein; Kornelia Hardes; Markus Eickmann; Olga Dolnik; Cornelius Rohde; Stephan Becker; Hans-Dieter Klenk; Wolfgang Garten; Torsten Steinmetzer; Eva Böttcher-Friebertshäuser
Title: TMPRSS2 and furin are both essential for proteolytic activation and spread of SARS-CoV-2 in human airway epithelial cells and provide promising drug targets Document date: 2020_4_15
ID: anedg12x_19
Snippet: CoV-2 activation. In conclusion, our data demonstrate that both TMPRSS2 and furin cleave the SARS-CoV-2 S 364 protein and are essential for virus multicycle replication in Calu-3 human airway cells. The 365 results indicate that TMPRSS2 and furin cleave S at different sites -furin at the S1/S2 site 366 and TMPRSS2 at the S2' site -and that TMPRSS2 and furin cannot compensate for each 367 other in SARS-CoV-2 S activation. Hence, inhibition of eith.....
Document: CoV-2 activation. In conclusion, our data demonstrate that both TMPRSS2 and furin cleave the SARS-CoV-2 S 364 protein and are essential for virus multicycle replication in Calu-3 human airway cells. The 365 results indicate that TMPRSS2 and furin cleave S at different sites -furin at the S1/S2 site 366 and TMPRSS2 at the S2' site -and that TMPRSS2 and furin cannot compensate for each 367 other in SARS-CoV-2 S activation. Hence, inhibition of either one of these critical proteases 368
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