PMC:7100515 / 17312-20113 JSONTXT

{"target":"https://pubannotation.org/docs/sourcedb/PMC/sourceid/7100515","sourcedb":"PMC","sourceid":"7100515","source_url":"https://www.ncbi.nlm.nih.gov/pmc/7100515","text":"Effect of cathepsin inhibitors on SARS-CoV-2 entry\nProtease activation on S protein is an important step for coronavirus entry, and cathepsins in lysosome have been shown to be critical for SARS-CoV and MERS-CoV entry through endocytosis. To investigate whether cathepsins are required for SARS-CoV-2 entry, HEK 293/hACE2 cells were treated with either a broad inhibitor for cathepsin B, H, L, and calpain (E64D), cathepsin L inhibitor (SID 26681509), or cathepsin B inhibitor (CA-074). VSV-G pseudovirions were used as a negative control, since virus entry mediated by VSV-G does not require protease activation. E64D treatment of 293/hACE2 cells reduced entry of SARS-CoV-2 S pseudovirions by 92.5%, indicating that at least one of cathepsins or calpain might be required for SARS-CoV-2 entry (Fig. 4a). While cathepsin B inhibitor treatment did not show any marked effect on virus entry, cathepsin L inhibition treatment decreased entry of SARS-CoV-2 S pseudovirions into 293/hACE2 by over 76% (Fig. 4a), suggesting that cathepsin L should be essential for priming of SARS-CoV-2 S protein in lysosome for entry into 293/hACE2 cells.\nFig. 4 Activation of SARS-CoV-2 S protein by cathepsin and trypsin.\na Effects of cathepsin inhibitors on entry of SARS-CoV-2 S pseudovirions on 293/hACE2 cells. HEK 293/hACE2 cells were pretreated with broad-spectrum cathepsin inhibitor E64D, cathepsin L-specific inhibitor (SID 26681509), or cathepsin B-specific inhibitor (CA-074) and then transduced with SARS-CoV-2 S and VSV-G pseudovirions. Pseudoviral transduction was measured at 40 h post inoculation. Experiments were done in triplicates and repeated at least three times. One representative is shown. Error bars indicate SEM of technical triplicates. b Cell–cell fusion mediated by SARS-CoV-2 S protein. HEK 293T cells were transiently expressing eGFP and either SARS-CoV-2 or SARS-CoV S protein were detached with either trypsin or EDTA, and co-cultured with 293/hACE2 or 293 cells for 4 h at 37 °C. The scale bar indicates 250 µm. c Quantitative analysis of syncytia in panel b. d, e Thermostability analysis of SARS-CoV-2 S protein. d SARS-CoV and SARS-CoV-2 S pseudovirons were incubated at 37 °C for the specified times (0 to 4 h) in the absence of serum, and then assayed on 293/hACE2 cells. The results from infection at 0 h were set as 100%, and the experiments were repeated four times, and means with standard deviations are shown. e SARS-CoV and SARS-CoV-2 S pseudovirions without serum were incubated at the indicated temperature (37 to 51 °C) for 2 h and then assayed on 293/hACE2 cells. The results are reported as the percentage of transduction at 37 °C. The experiments were repeated four times, and means with standard deviations are shown. 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