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10.3390/v13030384 http://scihub22266oqcxt.onion/10.3390/v13030384 33671076!8001073!33671076     free     free     free Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Viruses 2021 ; 13 (3): ä Nephropedia Template TP {{tp|p=33671076|t=2021. TMPRSS11D and TMPRSS13 Activate the SARS-CoV-2 Spike Protein |pdf=|usr=}}{{33671076}} gab.com Text TMPRSS11D and TMPRSS13 Activate the SARS-CoV-2 Spike Protein JO: Viruses http://www.kidney.de/pget.php?&tw=1&pmid=33671076 #FOAvip Severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2) utilizes host proteases, including a plasma membrane-associated transmembrane protease, serine 2 (TMPRSS2) to cleave and activate the virus spike protein to facilitate cellular entry. Although TMPRSS2 is a well-characterized type II transmembrane serine protease (TTSP), the role of other TTSPs on the replication of SARS-CoV-2 remains to be elucidated. Here, we have screened 12 TTSPs using human angiotensin-converting enzyme 2-expressing HEK293T (293T-ACE2) cells and Vero E6 cells and demonstrated that exogenous expression of TMPRSS11D and TMPRSS13 enhanced cellular uptake and subsequent replication of SARS-CoV-2. In addition, SARS-CoV-1 and SARS-CoV-2 share the same TTSPs in the viral entry process. Our study demonstrates the impact of host TTSPs on infection of SARS-CoV-2, which may have implications for cell and tissue tropism, for pathogenicity, and potentially for vaccine development. Twit Text FOAVip TMPRSS11D and TMPRSS13 Activate the SARS-CoV-2 Spike Protein ????Viruses http://www.kidney.de/pget.php?&tw=1&pmid=33671076 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=33671076 #FOAvip English Wikipedia <ref>{{Cite pmid|33671076}}</ref> TMPRSS11D and TMPRSS13 Activate the SARS-CoV-2 Spike Protein #MMPMID33671076 Kishimoto M; Uemura K; Sanaki T; Sato A; Hall WW; Kariwa H; Orba Y; Sawa H; Sasaki M Viruses 2021[Feb]; 13 (3): ä PMID33671076show ga Severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2) utilizes host proteases, including a plasma membrane-associated transmembrane protease, serine 2 (TMPRSS2) to cleave and activate the virus spike protein to facilitate cellular entry. Although TMPRSS2 is a well-characterized type II transmembrane serine protease (TTSP), the role of other TTSPs on the replication of SARS-CoV-2 remains to be elucidated. Here, we have screened 12 TTSPs using human angiotensin-converting enzyme 2-expressing HEK293T (293T-ACE2) cells and Vero E6 cells and demonstrated that exogenous expression of TMPRSS11D and TMPRSS13 enhanced cellular uptake and subsequent replication of SARS-CoV-2. In addition, SARS-CoV-1 and SARS-CoV-2 share the same TTSPs in the viral entry process. Our study demonstrates the impact of host TTSPs on infection of SARS-CoV-2, which may have implications for cell and tissue tropism, for pathogenicity, and potentially for vaccine development. |Angiotensin-Converting Enzyme 2/metabolism[MESH] |Animals[MESH] |COVID-19/*metabolism/*virology[MESH] |Chlorocebus aethiops[MESH] |HEK293 Cells[MESH] |Humans[MESH] |Membrane Proteins/*metabolism[MESH] |SARS-CoV-2/*metabolism[MESH] |Serine Endopeptidases/*metabolism[MESH] |Serine Proteases/*metabolism[MESH] |Spike Glycoprotein, Coronavirus/*metabolism[MESH] |Vero Cells[MESH]TMPRSS11D and TMPRSS13 Activate the SARS-CoV-2 Spike Protein (epmc).pdf DeepDyve Pubget Overpricing