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_16
Snippet: However, the amount of S2' protein present in transient TMPRSS2 expressing cells was 191 similar in MI-1851 treated and untreated cells, suggesting that S cleavage at the S2' site is 192 only caused by TMPRSS2 activity. The small amount of S2 protein detected in expressing cells in the presence of MI-1851 was likely due to residual furin activity rather 194 than cleavage of S at the S1/S2 site by TMPRSS2. Together, the data show that SARS-CoV-195.....
Document: However, the amount of S2' protein present in transient TMPRSS2 expressing cells was 191 similar in MI-1851 treated and untreated cells, suggesting that S cleavage at the S2' site is 192 only caused by TMPRSS2 activity. The small amount of S2 protein detected in expressing cells in the presence of MI-1851 was likely due to residual furin activity rather 194 than cleavage of S at the S1/S2 site by TMPRSS2. Together, the data show that SARS-CoV-195 2 can be cleaved by furin and by TMPRSS2. The data further suggest that the proteases 196 cleave S at different sites with furin processing the S1/S2 site and TMPRSS2 cleaving at the 197 S2' site. The copyright holder for this preprint (which was not peer-reviewed) is the . https://doi.org/10.1101/2020.04.15.042085 doi: bioRxiv preprint
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