| Id |
Subject |
Object |
Predicate |
Lexical cue |
| T403 |
0-127 |
Sentence |
denotes |
MERS-CoV S glycoprotein can hemagglutinate human erythrocytes and mediates virus entry into human respiratory epithelial cells. |
| T404 |
128-277 |
Sentence |
denotes |
MERS-CoV S glycoprotein attachment is not observed for 9-O-acetylated or 5-N-glycolyl SAs, but is observed for α2,3-SA linkage over α2,6-SA linkages. |
| T405 |
278-441 |
Sentence |
denotes |
SA-binding sites of MERS-CoV S glycoprotein and HCoV-OC43 S glycoprotein are not conserved [78], although they engage α2,3-SAs on the avian host cell surface [79]. |
| T406 |
442-547 |
Sentence |
denotes |
MERS-CoV recognizes α2,3-SA and to a lesser extent the α2,6-SAs and sulfated SLeX for binding preference. |
| T407 |
548-616 |
Sentence |
denotes |
Thus, S glycoproteins may have independently evolved SA recognition. |
| T408 |
617-900 |
Sentence |
denotes |
The acquisition of SA-binding ability of MERS-CoV S seems to be an evolutionarily recent event, because HKU4 S1 and HKU5 S1 cannot hemagglutinate human erythrocytes [75], indicating flexible evolutionary exchange allowing cross-species transmission towards host cell tropism of CoVs. |
| T409 |
901-1076 |
Sentence |
denotes |
In conclusion, CoV recognition of 9-O-Ac-SAs for infection is based on a conserved sequence for engagement of SA-related carbohydrate ligands across CoVs and orthomyxoviruses. |
