PMC:7352545 / 48098-53918 JSONTXT

{"target":"https://pubannotation.org/docs/sourcedb/PMC/sourceid/7352545","sourcedb":"PMC","sourceid":"7352545","source_url":"https://www.ncbi.nlm.nih.gov/pmc/7352545","text":"Host Cell ADAM17 and TMPRSS2 Competitively Cleave ACE2\nA disintegrin and metallopeptidase domain (ADAM) family of Zn-metalloproteinases belongs to membrane proteins. The well-known ADAM17 is a TNF-α-converting enzyme (TACE), called the sheddase for TNF-α. Other ADAM sheddase family members include ADAM9, ADAM10 and ADAM12. ADAM17 mediates ACE2 shedding. SARS-CoV S glycoprotein activates cellular TACE and consequently facilitates virus entry. Soluble ACE2 as the N-terminal carboxypeptidase domain form is derived from the original ACE2 form by an ADAM17 metalloprotease in the membrane [89]. ADAM17 is indeed an enzyme that can convert membrane type pro-TNF-α to soluble TNF-α, a functional proinflammatory cytokine. Therefore, ADAM17 inhibition indicates an anti-inflammatory response and ADAM17 inhibitors are promising candidates for TNF-α-induced inflammatory diseases. The short C-terminal domain of ACE2 is removed by ADAM17 and TMPRSS2. However, TMPRSS2 cleaves ACE2 competitively with the ADAM17 metalloprotease. SARS-S protein-ACE2 binding leads to ADAM17/TNF-α-converting enzyme (TACE)-cleavage of ACE2, facilitating extracellular ACE2 shedding and consequent SARS-CoV entry into host cells [90,91]. Only TMPRSS2 cleavage allows SARS-CoV entry into host cells through endocytosis and fusion. Soluble ACE2 also recognizes the virus and prevents SARS-CoV-2 infection. SARS-CoV-2 infection requires membrane ACE2 and TMPRSS2. The ACE2–B0AT1 complex binds to the S glycoprotein of SARS-CoV-2. Intestinal membrane ACE2 and lung TMPRSS2-shedded ACE2 can act as alternative entry sites for SARS-CoV-2. SARS-CoV-2 infects the lungs and intestine via TMPRSS2-cleaved ACE2. If TMPRSS2 is engaged in SARS-CoV-2 entry and ACE2 downregulation, TMPRSS2 inhibition would lead to COVID-19 prevention. Although ACE2 is expressed both in type I and type II lung alveolar epithelial cells, SARS-CoV and SARS-CoV-2 target only type II epithelial cells due to the ACE2–TMPRSS2 interaction. Therefore, supplementation of ACE2 (soluble ACE2) or Ang-1 to Ang-7 should be a way to reduce SARS-CoV-2-related symptoms.\nTMPRSS2-cleaved ACE2 is involved in SARS-CoV and MERS-CoV infections. SARS-CoV-2 uses ACE2 for cell entry through TMPRSS2 priming of the S glycoprotein (Figure 7). Infection of the H7N9 influenza and H1N1 influenza A subtype viruses are also mediated by TMPRSS2-cleaved ACE2. This implies that TMPRSS2 can be targeted as a strategic antiviral therapy [92]. Transmembrane protease serine 2, termed TMPRSS2, a type II TM Ser protease (TTSP), also cleaves ACE2. The human TMPRSS2 gene, located on chromosome 21, comprises androgen receptor elements (AREs) in the upstream 5′-flanking region [93]. TMPRSS2 expression is regulated in an androgen-dependent manner. The TMPRSS2 gene encodes 492 amino acids. The original form is cleaved into the major membrane form and the minor soluble form. TMPRSS2 activates protease activated receptor 2 (PAR-2) and activated PAR-2 upregulates matrix metalloproteinase-2 (MMP-2) and MMP-9. TMPRSS2-activated hepatocyte growth factor (HGF) induces c-Met receptor signaling. TMPRSS2 activates SARS-CoV and MERS-CoV. The SARS-CoV S glycoprotein is cleaved by host-borne TMPRSS2, human airway trypsin-like protease (HAT), TM protease, serine 13 (MSPL), serine protease DESC1 (DESC1), furin, factor Xa and endosomal cathepsin L/B. SARS-CoV can enter cells upon cleavage by protease TMPRSS2 or endosomal cathepsin L/B [90]. Virus S protein precursor is cleaved by host proteases. The spikes are cleaved by endosomal cathepsin and by Golgi or plasma membrane TMPRSS2 in the step of assembly or attachment and release. The serine protease inhibitor camostat effectively blocks lethal SARS-CoV infection to mice. However, serine protease and cathepsin inhibitors are not effective. Thus, TMPRSS2 is suggested to be an acting protease for SARS-CoV entry into host cells, but not by cathepsin. Cis-cleavage liberates SARS-CoV S glycoprotein fragments into the extracellular supernatant. Trans-cleavage activates the SARS-CoV S glycoprotein on the target cells, potentiating efficient SARS-CoV S glycoprotein-driven viral fusion. TMPRSS2-activated SARS-CoV facilitates enveloped virus entry into cells. TMPRSS2 is important for SARS-CoV entry and infection [81,94,95,96].\nThe fact that SARS- and MERS-CoV infections are potentiated by TMPRSS2 indicates that TMPRSS2 is a promising target for therapeutic agents. For example, several Ser protease inhibitors such as camostat mesylate inhibit TMPRSS2–ACE2-involved SARS-CoV-2 entry. camostat, a serine protease inhibitor, reduces influenza virus titers in cell culture. camostat-treated TMPRSS2 inhibition in Calu-3 cells greatly reduces SARS-CoV viral titers and improves survival rate in SARS-CoV infected mice. A treatment of 10-μM camostat blocks MERS-CoV entry to African green monkey kidney (Vero)-TMPRSS2 cells and blocks viral RNA synthesis in Calu-3 cells upon MERS-CoV infection. Aprotinin is a polypeptide with 58 amino acid residues that was isolated from bovine lungs. Another serine protease inhibitor, nafamostat, inhibits MERS-CoV entry and infection by TMPRSS2 inhibition [93]. nafamostat mesylate blocks the TMPRSS2–ACE2-involved SARS-CoV-2 envelope–PM fusion and prevents SARS-CoV-2 entry [95]. nafamostat mesylate inhibits viral entry and thrombosis in COVID-19 patients. Similarly, an FDA-approved mucolytic cough suppressant, Bromhexine hydrochloride (BHH), inhibits TMPRSS2 (IC50 0.75 μM) and hence blocks infection of CoV and influenza virus. MPRSS2 as a host factor plays a pivotal role in SARS-CoV and MERS-CoV infections. FDA-approved TMPRSS2 inhibitors are yet under development. Because TMPRSS2 mediates efficient viral entry and replication, it should be a promising target for new therapeutics against CoV 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