| Id |
Subject |
Object |
Predicate |
Lexical cue |
| T29 |
0-165 |
Sentence |
denotes |
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). |
| T30 |
166-761 |
Sentence |
denotes |
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. |
| T31 |
762-1443 |
Sentence |
denotes |
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 infections. |
