PMC:7386875 / 5844-7287 JSONTXT

{"target":"https://pubannotation.org/docs/sourcedb/PMC/sourceid/7386875","sourcedb":"PMC","sourceid":"7386875","source_url":"https://www.ncbi.nlm.nih.gov/pmc/7386875","text":"In humans, these coronaviruses gain entry into host cells by way of their transmembrane spike (S) GP (glycoprotein), which comprises an S1 and S2 subunit (Figure 1). The S1 subunit is responsible for binding to the host cell receptor, and the S2 subunit assists with viral and host cell fusion.1 While the MERS-CoV S GP binds to DPP-4 (dipeptidyl peptidase 4) expressed on epithelial tissue, both SARS-CoV-2 and SARS-CoV bind to human cells via the ACE-2 (angiotensin-converting enzyme 2) receptor.5 In addition to having different amino acid residues within the RBD (receptor-binding domain) of the S protein compared to SARS-CoV, another novel structural feature of SARS-CoV-2, is the presence of a polybasic furin cleavage site, at the junction of S1 and S2. Cleavage of the S protein by cellular proteases, including furin and TMPRSS-2 (transmembrane protease serine 2), is speculated to play an important role in the infectivity and host range of SARS-CoV-2, although its functional significance regarding how this feature may mediate SAR-CoV-2 transmissibility and pathogenicity is yet be fully elucidated.1 In the context of COVID-19-associated thrombosis, understanding how these structural differences of SARS-CoV-2 may relate to the prothrombotic phenotype of COVID-19 is likely to be of fundamental importance given the significantly higher rates of thrombosis observed in SARS-CoV-2, compared with SARS-CoV and MERS-CoV 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