LitCovid-sentences  

PMC:7352545 / 39006-43134 JSONTXT 9 Projects

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Id Subject Object Predicate Lexical cue
T382 0-4 Sentence denotes 6.2.
T383 5-98 Sentence denotes SARS-CoV-2 Recognizes 9-O-Acetyl-SAs and MERS-CoV Recognizes α2,3-SAs as Attachment Receptors
T384 99-167 Sentence denotes The S glycoprotein SARS-CoV-2 initiates infection of the host cells.
T385 168-390 Sentence denotes The molecular basis of CoV attachment to sugar/glycan receptors is an important issue, as demonstrated by recent cryo-EM defining the structure of the CoV-OC43 S glycoprotein trimer complexed with a 9-O-acetylated SA [56].
T386 391-613 Sentence denotes Cryo-EM structures of the trimeric ectodomain of S glycoprotein were observed using forms complexed with Neu5Ac, Neu5Gc, sialyl–LewisX (SLeX), α2,3-sialyl-N-acetyl-lactosamine (α2,3-SLacNAc) and α2,6-SLacNAc, respectively.
T387 614-867 Sentence denotes The receptor-binding site is commonly conserved in all CoV S glycoproteins, which attach to 9-O-Ac-SA species with similar ligand-binding pockets to the CoV HEs and influenza virus C/D HEF glycoproteins, indicating conserved recognizing structures [25].
T388 868-1009 Sentence denotes The S glycoprotein-9-O-acetyl-SA interaction resembles the ligand-binding pockets of CoV HEs and influenza virus C/D HE fusion glycoproteins.
T389 1010-1049 Sentence denotes HCoV-OC43 and BCoV recognize 9-O-Ac-SA.
T390 1050-1088 Sentence denotes S glycoproteins engage 9-O-acetyl-SAs.
T391 1089-1330 Sentence denotes The 9-O-acetyl SAs are the binding site for HCoV-OC43 S glycoprotein and related β-1 CoV S glycoproteins, however SA-binding sites on the 9-O-acetyl sialyl receptors of MERS-CoV S glycoprotein and HCoV-OC43 S glycoprotein are different [71].
T392 1331-1391 Sentence denotes Thus, CoVs use two different entry and attachment receptors.
T393 1392-1528 Sentence denotes Therefore, S glycoproteins of CoVs are distinct from influenza virus A HAs, which bind to the Neu5Ac species by conserved binding sites.
T394 1529-1782 Sentence denotes The ligand-binding sites of BCoV HE enzyme, influenza HEF enzyme and CoV S glycoprotein have evolved 9-O-Ac-SA binding through hydrogen bonding with the 9-O-acetyl carbonyl group and hydrophobic pocket formation with the 9-O-acetyl methyl group [71,72].
T395 1783-1863 Sentence denotes However, influenza HA cannot bind to 9-O-acetyl-SAs but can bind to NeuGcs [73].
T396 1864-2173 Sentence denotes The HCoV-OC43 S glycoprotein, HCoV-HKU1 S glycoprotein, BCoV S glycoprotein and PHEV S glycoprotein, therefore, share the ligand-binding specificity of influenza C/D HEF enzyme, although they are functionally more similar to influenza virus A/B HA, whereas CoV HE or influenza virus A/B NA have RDE activities
T397 2174-2248 Sentence denotes CoV HEs are functionally similar to influenza virus C/D HEF glycoproteins.
T398 2249-2423 Sentence denotes In CoV, the S glycoprotein recognizes the 9-O-Ac-SA sugar, while the HE acts as the RDE enzyme with SA-O-acetyl-esterase activity to release virions from infected host cells.
T399 2424-2484 Sentence denotes For example, HCoV-OC43 also has a similar HE as an RDE [71].
T400 2485-2566 Sentence denotes In influenza C and D viruses, HEF glycoproteins act similarly to the CoV HE [74].
T401 2567-2629 Sentence denotes In influenza A virus, RDE NA releases virions from host cells.
T402 2630-3051 Sentence denotes However, MERS-CoV does not have a similar enzyme and thus MER-CoV binding to SA receptors is mediated by energetically reversible interactions of the lipid rafts with increased SA receptors [75], thus enhancing dipeptidyl peptidase 4 (DPP4) or carcinoembryonic antigen-related cell adhesion molecule 5 (CEACAM5) recognition power and viral entry [76] and membrane-associated 78-kDa glucose-regulated protein (GRP78) [77].
T403 3052-3179 Sentence denotes MERS-CoV S glycoprotein can hemagglutinate human erythrocytes and mediates virus entry into human respiratory epithelial cells.
T404 3180-3329 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 3330-3493 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 3494-3599 Sentence denotes MERS-CoV recognizes α2,3-SA and to a lesser extent the α2,6-SAs and sulfated SLeX for binding preference.
T407 3600-3668 Sentence denotes Thus, S glycoproteins may have independently evolved SA recognition.
T408 3669-3952 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 3953-4128 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.