| Id |
Subject |
Object |
Predicate |
Lexical cue |
| T217 |
0-215 |
Sentence |
denotes |
The cryo-electron microscopy structure of an HCoV-OC43 S trimer in complex with a 9-O-Ac-Me-Sia revealed that a sialoside-binding site was located at the surface-exposed groove of each S1A monomer (Figure 5a) [193]. |
| T218 |
216-557 |
Sentence |
denotes |
The sialoside-binding groove (Figure 5b,c) is formed by two loops, L1 consisting of 27-NDKDTG-32 and L2 consisting of 80-LKGSVLL-86 at the RBS edges, two hydrophobic pockets separated by the indole side chain of W90, P1 consisting of L85, L86 and W90 and P2 consisting of L80, W90 and F95 [193], and a residue, S87, interacting with L1 [92]. |
| T219 |
558-946 |
Sentence |
denotes |
Substitutions of N27 having an H-bond with OA9 of the 9-O-acetyl carbonyl group, K81 forming H-bonds with O1 and N5 of Sia, or S83 containing an H-bond with O3 of Sia C1, with alanine and mutations of L80, L86 or W90 in hydrophobic pockets accommodating the 5-N-acyl moiety and the 9-O-acetyl-methyl moiety provided a mutant HCoV-OC43 S1A that had lost the ability to bind to 9-O-Ac-6SLN. |
| T220 |
947-1111 |
Sentence |
denotes |
Substitutions at N27, T31, L80, K81, S83, L86 and W90 completely blocked the entry of pseudotyped VSVΔG particles harboring HCoV-OC43 S proteins into HEK293T cells. |
| T221 |
1112-1312 |
Sentence |
denotes |
These results confirmed that residues in the surface-exposed groove are critical for interaction with the 9-O-Ac-Sia receptor and that their interactions are essential for mediating viral entry [193]. |
| T222 |
1313-1394 |
Sentence |
denotes |
Interestingly, HCoV-OC43 S1A recognized 9-O-Ac-Sia bound to Gal via α2,6 linkage. |
| T223 |
1395-1840 |
Sentence |
denotes |
More research on binding specificity of both animal and human 9-O-Ac-Sia-binding β1CoVs to the internal part of the receptor in combination with analysis of 9-O-Ac-Sia-containing glycan structures expressed on host tissues and analysis of changes in the viral S1A proteins could reveal which part of 9-O-Ac-Sia-containing glycans determines host/tissue tropism of β1CoVs and changes in the viral S1A proteins associated with host/tissue tropism. |
