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. 2021 Apr 6;7:21. doi: 10.1038/s41421-021-00256-3

Fig. 2. Effects of protease cleavage on viral infectivity.

Fig. 2

a Amino acid alignment of the protease cleavage site for SARS-CoV-2, PCoV-GD, PCoV-GX, and RaTG13. The recognition sequences were embraced in boxes and cleavage sites indicated with triangles. b Pseudoviruses produced in cells overexpressing different proteases. Most of SARS-CoV-2 S were cleaved into S1 and S2. The ratio of the cleaved form increased slightly in Furin and TMPRSS2. The other three pseudoviruses present the S on their surface mostly in intact forms. c Relative infectivity of the pseudoviruses in hACE2 cells and hACE2 cells with various overexpressed proteases. d The entry of SARS-CoV-2, PCoV-GD, and PCoV-GX into cell lines expressing different proteases was blocked with three protease inhibitors, Decanoyl-RvKR-CMK for Furin, Camostat for TMPRSS2, and E64D for Cathepsin L inhibitor. All results were obtained from three independent experiments (mean ± SEM). In each experiment, the infection assay was performed in duplicate wells.