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_7
Snippet: However, sequence analysis of the SARS-CoV-2 S protein suggests that furin may also be 129 involved in S processing ( Fig. 1B ; Coutard et al., 2020; Walls et al., 2020). The S1/S2 site of 130 SARS-CoV-2 S protein contains an insertion of four amino acids providing a minimal furin 131 cleavage site (R-R-A-R 685 ↓) in contrast to the S protein of SARS-CoV. Instead, similar to 132 SARS-CoV the S2' cleavage site of SARS-CoV-2 S possesses a paired .....
Document: However, sequence analysis of the SARS-CoV-2 S protein suggests that furin may also be 129 involved in S processing ( Fig. 1B ; Coutard et al., 2020; Walls et al., 2020). The S1/S2 site of 130 SARS-CoV-2 S protein contains an insertion of four amino acids providing a minimal furin 131 cleavage site (R-R-A-R 685 ↓) in contrast to the S protein of SARS-CoV. Instead, similar to 132 SARS-CoV the S2' cleavage site of SARS-CoV-2 S possesses a paired dibasic motif with a 133 single KR segment (KR 815 ↓) that is recognized by trypsin-like serine proteases. 134
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