| Id |
Subject |
Object |
Predicate |
Lexical cue |
| T264 |
0-320 |
Sentence |
denotes |
Viral binding sites on hAPN, based on interface residues of hAPN (red letter codes in Figure 4b) to 4 classes of HCoV-229E RBD [194] were aligned with bat H. armiger APN, due to the unavailability of APN of H. cf. ruber and H. abae, which are known to be bat hosts of HCoV-229E-related CoVs, and Camelus dromedarius APN. |
| T265 |
321-607 |
Sentence |
denotes |
E291N, K292E, Q293T triple mutations generating a glycosylation site at position 291 in the hAPN abolished binding to all 6 HCoV-229E RBD classes [83], being in agreement with the finding that E291 plays a critical role in the formation of hydrogen bonds with N319 of the HCoV-229E RBD. |
| T266 |
608-696 |
Sentence |
denotes |
Both E291 of hAPN and N319 of HCoV-229E RBDs are highly conserved among different hosts. |
| T267 |
697-1090 |
Sentence |
denotes |
In addition to E291, several amino acids on the viral binding site including A208, L243, T244, S285 E286, F287, V290, W303, P360, A308, G312, G314, L318 and N319 (based on hAPN numbering) are highly conserved among different hosts, and these amino acids on APN may therefore play a role in interspecies transmission of HCoV-229E-related CoVs, a possibility that should be further investigated. |
| T268 |
1091-1248 |
Sentence |
denotes |
The specific binding of HCoV-229E-related CoVs to their host APN should be governed by other amino acids that are not conserved among different host species. |
| T269 |
1249-1654 |
Sentence |
denotes |
These amino acids might be (i) K241, D242, and A310 in human and camel APNs, which are different from those in bat APN that carries S241, N242 and K310, (ii) D288, I309, A311, and D315, which are different from those in bat and camel APNs that carry T288, T309, E311, and I315, and (iii) Y289 and K292, which are different from those in bat APN carrying A289 and E292 and camel APN carrying C289 and G292. |
| T270 |
1655-1922 |
Sentence |
denotes |
Mutations in hAPN, D288A, Y289A, V290G, I309A and L318A, resulted in hAPN binding affinity to HCoV-229E RBD, and the V290G mutant showed the greatest reduction (30-fold reduction) of binding affinity, indicating receptor binding specificity of the HCoV-229E RBD [83]. |
| T271 |
1923-2057 |
Sentence |
denotes |
An understanding of the alteration in 229E receptor binding specificity should lead to prevention of virus infection and transmission. |
