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10.26508/lsa.202000786 http://scihub22266oqcxt.onion/10.26508/lsa.202000786 32703818!7383062!32703818     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=32703818&cmd=llinks): Failed to open stream: HTTP request failed! 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TMPRSS2 and furin are both essential for proteolytic activation of SARS-CoV-2 in human airway cells |pdf=|usr=}}{{32703818}} gab.com Text TMPRSS2 and furin are both essential for proteolytic activation of SARS-CoV-2 in human airway cells JO: Life Sci Alliance http://www.kidney.de/pget.php?&tw=1&pmid=32703818 #FOAvip The novel emerged SARS-CoV-2 has rapidly spread around the world causing acute infection of the respiratory tract (COVID-19) that can result in severe disease and lethality. For SARS-CoV-2 to enter cells, its surface glycoprotein spike (S) must be cleaved at two different sites by host cell proteases, which therefore represent potential drug targets. In the present study, we show that S can be cleaved by the proprotein convertase furin at the S1/S2 site and the transmembrane serine protease 2 (TMPRSS2) at the S2' site. We demonstrate that TMPRSS2 is essential for activation of SARS-CoV-2 S in Calu-3 human airway epithelial cells through antisense-mediated knockdown of TMPRSS2 expression. Furthermore, SARS-CoV-2 replication was also strongly inhibited by the synthetic furin inhibitor MI-1851 in human airway cells. In contrast, inhibition of endosomal cathepsins by E64d did not affect virus replication. Combining various TMPRSS2 inhibitors with furin inhibitor MI-1851 produced more potent antiviral activity against SARS-CoV-2 than an equimolar amount of any single serine protease inhibitor. Therefore, this approach has considerable therapeutic potential for treatment of COVID-19. Twit Text FOAVip TMPRSS2 and furin are both essential for proteolytic activation of SARS-CoV-2 in human airway cells ????Life Sci Alliance http://www.kidney.de/pget.php?&tw=1&pmid=32703818 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=32703818 #FOAvip English Wikipedia <ref>{{Cite pmid|32703818}}</ref> TMPRSS2 and furin are both essential for proteolytic activation of SARS-CoV-2 in human airway cells #MMPMID32703818 Bestle D; Heindl MR; Limburg H; Van Lam van T; Pilgram O; Moulton H; Stein DA; Hardes K; Eickmann M; Dolnik O; Rohde C; Klenk HD; Garten W; Steinmetzer T; Bottcher-Friebertshauser E Life Sci Alliance 2020[Sep]; 3 (9): ä PMID32703818show ga The novel emerged SARS-CoV-2 has rapidly spread around the world causing acute infection of the respiratory tract (COVID-19) that can result in severe disease and lethality. For SARS-CoV-2 to enter cells, its surface glycoprotein spike (S) must be cleaved at two different sites by host cell proteases, which therefore represent potential drug targets. In the present study, we show that S can be cleaved by the proprotein convertase furin at the S1/S2 site and the transmembrane serine protease 2 (TMPRSS2) at the S2' site. We demonstrate that TMPRSS2 is essential for activation of SARS-CoV-2 S in Calu-3 human airway epithelial cells through antisense-mediated knockdown of TMPRSS2 expression. Furthermore, SARS-CoV-2 replication was also strongly inhibited by the synthetic furin inhibitor MI-1851 in human airway cells. In contrast, inhibition of endosomal cathepsins by E64d did not affect virus replication. Combining various TMPRSS2 inhibitors with furin inhibitor MI-1851 produced more potent antiviral activity against SARS-CoV-2 than an equimolar amount of any single serine protease inhibitor. Therefore, this approach has considerable therapeutic potential for treatment of COVID-19. |Alveolar Epithelial Cells/cytology/*virology[MESH] |Animals[MESH] |Betacoronavirus/*physiology[MESH] |Binding Sites[MESH] |Cell Line[MESH] |Chlorocebus aethiops[MESH] |Furin/*genetics[MESH] |HEK293 Cells[MESH] |Humans[MESH] |Proteolysis[MESH] |SARS-CoV-2[MESH] |Serine Endopeptidases/*genetics[MESH] |Spike Glycoprotein, Coronavirus/chemistry/*metabolism[MESH] |Vero Cells[MESH] |Virus Internalization[MESH]TMPRSS2 and furin are both essential for proteolytic activation of SAR(epmc).pdf DeepDyve Pubget Overpricing