Id |
Subject |
Object |
Predicate |
Lexical cue |
T148 |
0-49 |
Sentence |
denotes |
Cell–cell fusion mediated by SARS-CoV-2 S protein |
T149 |
50-241 |
Sentence |
denotes |
Type II membrane serine proteases (TMPRSS)-mediated cleavage can activate the fusion potential of SARS-CoV and MERS-CoV S protein and induce receptor-dependent syncytium formation28,29,38,39. |
T150 |
242-476 |
Sentence |
denotes |
To test whether SARS-CoV-2 S protein cleaved by these cellular proteases could trigger syncytium formation, we overlaid HEK 293T cells expressing SARS-CoV-2 S or control proteins on 293/hACE2 cells in presence or absence of proteases. |
T151 |
477-645 |
Sentence |
denotes |
Expression of TMPRSS 2, 4, 11 A, 11D, and 11E on 293/hACE2 cells enhanced SARS-CoV-2 S protein-mediated cell–cell fusion similarly to SASR-CoV S (Supplementary Fig. 2). |
T152 |
646-684 |
Sentence |
denotes |
Next we evaluated the role of trypsin. |
T153 |
685-847 |
Sentence |
denotes |
Consistent to our previous report23, addition of trypsin triggered syncytium formation on 293/hACE2 cells by SARS-CoV S protein after 4 h incubation (Fig. 4b, c). |
T154 |
848-1010 |
Sentence |
denotes |
Large syncytia were formed at a level similar to SARS-CoV S proteins when SARS-CoV-2 S protein expressing 293T cells were added onto 293/hACE2 cells with trypsin. |
T155 |
1011-1281 |
Sentence |
denotes |
Of note, SARS-CoV-2, but not SARS-CoV, S proteins induced syncytia formation on 293/hACE2 cells even in the absence of trypsin (Fig. 4c), suggesting that SARS-CoV-2 S proteins could be triggered upon the receptor binding without exogenous protease priming or activation. |
T156 |
1282-1437 |
Sentence |
denotes |
During 2013–2016 Ebola virus outbreak, A82V and T544I mutations in glycoprotein (gp) of Ebola virus were linked to increase of virus transmissibility40–42. |
T157 |
1438-1581 |
Sentence |
denotes |
Further study showed that A82V and T544I mutation decreases the thermostability of gp while they increases virus infectivity in cell culture42. |
T158 |
1582-1647 |
Sentence |
denotes |
We then investigated the thermostability of SARS-CoV-2 S protein. |
T159 |
1648-1806 |
Sentence |
denotes |
Compared to SARS-CoV S protein, SARS-CoV-2 S protein was less stable, requiring significant shorter time and lower temperature to be inactivated (Fig. 4d, e). |
T160 |
1807-2035 |
Sentence |
denotes |
The native S protein is metastable, and there is an energy barrier that prevents it from undergoing conformational change before triggering, SARS-CoV-2 S protein might decrease its energy barrier by reducing its thermostability. |
T161 |
2036-2104 |
Sentence |
denotes |
This might contribute to high-transmission efficiency of SARS-CoV-2. |