| Id |
Subject |
Object |
Predicate |
Lexical cue |
| T34 |
0-316 |
Sentence |
denotes |
2019-nCoV possessed the typical coronavirus structure with the “spike protein” in the membrane envelope30, and also expressed other polyproteins, nucleoproteins, and membrane proteins, such as RNA polymerase, 3-chymotrypsin-like protease, papain-like protease, helicase, glycoprotein, and accessory proteins10,11,30. |
| T35 |
317-435 |
Sentence |
denotes |
The S protein from coronavirus can bind to the receptors of the host to facilitate viral entry into target cells31,32. |
| T36 |
436-789 |
Sentence |
denotes |
Although there are four amino acid variations of S protein between 2019-nCoV and SARS-CoV, 2019-nCoV can also bind to the human angiotensin-converting enzyme 2 (ACE2), the same host receptor for SARS-CoV, as 2019-nCoV can bind to the ACE2 receptor from the cells from human, bat, civet cat, and pig, but it cannot bind to the cells without ACE211,33–35. |
| T37 |
790-1017 |
Sentence |
denotes |
A recombinant ACE2-Ig antibody, a SARS-CoV-specific human monoclonal antibody, and the serum from a convalescent SARS-CoV-infected patient, which can neutralize 2019-nCoV, confirmed ACE2 as the host receptor for 2019-nCoV36–39. |
| T38 |
1018-1183 |
Sentence |
denotes |
The high affinity between ACE2 and 2019-nCoV S protein also suggested that the population with higher expression of ACE2 might be more susceptible to 2019-nCoV40,41. |
| T39 |
1184-1353 |
Sentence |
denotes |
The cellular serine protease TMPRSS2 also contributed to the S-protein priming of 2019-nCoV, indicating that the TMPRSS2 inhibitor might constitute a treatment option36. |
