PMC:7161517 / 25809-30611 JSONTXT

{"target":"http://pubannotation.org/docs/sourcedb/PMC/sourceid/7161517","sourcedb":"PMC","sourceid":"7161517","source_url":"https://www.ncbi.nlm.nih.gov/pmc/7161517","text":"ACE2 and SARS-CoV-2\nSARS-CoV, which emerged in the Guangdong province, China, and SARS-CoV-2, which emerged in Wuhan, China are closely related beta-coronaviruses whose affected receptor is ACE2 (1,3,4). At this time, it is unknown if the approximate 76% sequence similarity between these strains of viruses translates into similar biological properties (14). Recent studies have confirmed COVID-19 exploits ACE2 for entry and thus may target a similar spectrum of cells as SARS-CoV (14). SARS-CoV-2 binds to ACE2 via its spike (S) protein (13,14). The surface unit S1, of the S protein binds to ACE2, which facilitates viral attachment to target cells. Following receptor binding, the virus must gain access to host cytosol, which is accomplished by acid-dependent proteolytic cleavage of the S protein by cellular serine protease TMPRSS2, which is similar to S protein priming in SARS-CoV (14) (Figure 2 ).\nFigure 2 Proposed Mechanism of Entry for SARS-CoV-2 Via ACE2\nSevere acute respiratory syndrome coronavirus 2 (SARS-CoV-2) binds to the catalytic site of ACE2 via its S protein. To gain access to the host cytosol, the S protein undergoes acid dependent proteolytic cleavage by ACE2, tumor necrosis factor (TNF)-α, transmembrane protease serine 2 (TMPRRS2), which results in the formation of an S1 and S2 subunit. S2 fusion peptide inserts into the membrane, which allows for clatherin-dependent endocytosis of ACE2-SARS-CoV-2. Viral binding stimulates TNF-α and calmodulin inhibitors to promote ectodomain cleavage of ACE2. ADAM 17 = disintegrin and metalloprotease 17; other abbreviations as in Figure 1.\nBecause of the sequence similarity between SARS-CoV and SARS-CoV-2, their affected receptor, and recently confirmed TMPRSS2-mediated viral entry, it is reasonable to hypothesize that SARS-CoV-2 may act similarly with respect to using host endocytosis machinery, subsequent virus propagation, and further infection. Upon binding to ACE2, cleavage of the S protein at the S1/S2 sites and S2 allows for fusion of viral and cellular membranes. SARS-CoV is then internalized and penetrates early endosomes in a clathrin-dependent manner (62). Viral binding to ACE2 appears to affect TNF-α activity, which in the presence of calmodulin inhibitors promotes ectodomain cleavage (63). In the case of SARS-CoV-2, it is possible this shedding is also mediated by TNF-α because 1 of the clinical features noted in patients with COVID-19 has been the presence of a cytokine storm with increased plasma concentrations of IL-2, IL-7, IL-10, granulocyte-colony stimulating factor (GCSF), interferon gamma-induced protein 10 (IP10), monocyte chemoattractant protein 1, macrophage inflammatory protein 1 alpha (MIP1A), and TNF-α (2). It is also possible that ACE2 shedding may be mediated by other cytokines dysregulated in COVID-19. This shedding contributes to the down-regulation of membrane-bound ACE2 observed in severe acute lung injury (64). Ectodomain shedding increases the concentration of plasma ACE2, which remains catalytically active, although the function of soluble ACE2 remains unclear. In patients with advanced heart failure, plasma ACE2 activity is increased in direct proportion with worsening clinical status and reduction in ejection fraction and correlates with adverse clinical outcomes (65). Because down-regulation of bound ACE2 is observed in severe acute lung injury (65) and after myocardial infarction (46), and concentrations of soluble ACE2 appear to correlate with clinical outcomes of patients with heart failure (30), it is possible to suggest that concentrations of soluble ACE2 may correlate to the extent of tissue damage sustained and may correlate to the degree by which systemic inflammatory pathways are upregulated. There is some evidence to suggest soluble ACE2 is able to regulate systemic Ang II. Clinical trials have shown rhACE2 could convert systemic Ang II to Ang 1-7 (57,58) and play some pathological, compensatory, or counter regulatory roles.\nIf SARS-CoV-2 does induce ACE2 ectodomain shedding, which results in the reduction of ACE2 entry sites on the infected cell, it is possible that following transcription S proteins fuse directly at the host cell membrane and directly promote infection of neighboring cells, which results in the formation of multinucleated syncytia (66). Formation of multinucleated cells would allow the virus to spread without being detected or neutralized by virus-specific antibodies (66). Otherwise, following replication and transcription, complete virion assembly in the Golgi would result in transportation of the virus in vesicles and release by exocytosis (66). In the setting of full virion assembly and exocytosis, it is unclear if ACE2 ectodomain shedding would be favorable for further propagation and 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