LitCovid-sentences  

PMC:7712180 / 33657-40127 JSONTXT 3 Projects

Annnotations TAB TSV DIC JSON TextAE

Id Subject Object Predicate Lexical cue
T193 0-58 Sentence denotes 3.6. β1 HCoV-OC43 and β1 HCoV-HKU1 Use Neu5,9Ac2 Receptors
T194 59-259 Sentence denotes HCoV-OC43 strain was first detected in 1967 by an organ culture technique from throat washings of patients with common colds [186], but its complete genomic sequence was not reported until 2004 [187].
T195 260-418 Sentence denotes HCoV-HKU1 was first characterized in 2005 by Woo et al. at the University of Hong Kong (HKU) from a nasopharyngeal aspirate of a patient with pneumonia [188].
T196 419-514 Sentence denotes Based on genomic sequences reported so far, there is no bat CoV classified as a βCoV lineage A.
T197 515-627 Sentence denotes Based on phylogenetic analysis, both HCoV-OC43 and HCoV-HKU1 βCoV lineage A probably originated in rodents [85].
T198 628-781 Sentence denotes While an intermediate host of HCoV-HKU1 remains unknown, HCoV-OC43 is believed to have cattle serving as intermediate hosts from rodents to humans [189].
T199 782-924 Sentence denotes HCoV-OC43 does not bind to and agglutinate erythrocytes pretreated with 9-O-acetyl esterase from either influenza C virus or bovine CoV [190].
T200 925-1113 Sentence denotes HCoV-HKU1 does not infect primary human ciliated airway epithelial cells pretreated with an expressed HKU1 hemagglutinin-esterase (HE) protein possessing 9-O-acetylesterase activity [191].
T201 1114-1276 Sentence denotes These findings suggest that both HCoV-OC43 and HCoV-HKU1 bind to 9-O-acetylated sialyl glycans (Figure 4a) on the host cell surface for mediating virus infection.
T202 1277-1693 Sentence denotes As shown in Table 2, the 9-O-Ac-Sia receptor-binding function of homodimeric HE proteins, comprised of a receptor-binding (lectin) domain and receptor-destroying domain, of HCoV-OC43 and HCoV-HKU1 was reported to be lost, and its loss was reported to be associated with an accumulation of mutations in the OC43-HE lectin domain or massive deletions found in the HKU1-HE lectin domain during evolution in humans [94].
T203 1694-2043 Sentence denotes Binding of the S1 subunit of another type of spike, a homotrimeric spike (S) protein (Figure 2), of HCoV-OC43 and HCoV-HKU1 on human rhabdomyosarcoma cells was shown and was reported to be reduced by pretreating the cells with HKU1-HE, OC43-HE or BCoV-HE, but not by pretreating the cells with MHV-S-HE, possessing 4-O-acetylesterase activity [191].
T204 2044-2198 Sentence denotes These findings suggested that 9-O-Ac-Sia is an essential receptor for infection of HCoV-OC43 and HCoV-HKU1 mediated by the S1 subunit of their S proteins.
T205 2199-2324 Sentence denotes The S1 subunit of the S protein is composed of four domains, A through D (S1A through S1D) domains from the N-terminus [112].
T206 2325-2556 Sentence denotes By using OC43 or HKU1 S1A–Fc proteins in a direct binding assay, HCoV-OC43 and HCoV-HKU1 were shown to bind to the receptors via domain A (S1-NTD (Figure 5a), residues 15–302 based on the S protein of OC43 strain ATCC VR-759) [92].
T207 2557-2883 Sentence denotes However, binding of HKU1 S1A to its receptors on rat erythrocytes can be detected when HKU1 S1A–Fc proteins have been conjugated to nanoparticles but cannot be detected by using free HKU1 S1A–Fc proteins (the standard method), indicating the requirement of multivalency of HKU1 S1A–Fc proteins for binding to rat erythrocytes.
T208 2884-3048 Sentence denotes Based on structural analysis, residues 28–34 (element 1) and/or residues 243–252 (element 2) in HKU1 S1A (Figure 5b) were thought to hamper the binding of HKU1 S1A.
T209 3049-3242 Sentence denotes The mutant HKU1 S1A was generated by replacement of one or both of their elements with the corresponding element(s) from bovine coronavirus (BCoV), which is believed to be the ancestor of OC43.
T210 3243-3358 Sentence denotes The free mutant HKU1 S1A–Fc proteins with only one replacement at element 2 were found to bind to rat erythrocytes.
T211 3359-3473 Sentence denotes The free mutant HKU1 S1A–Fc proteins with replacement of both elements showed greater binding to rat erythrocytes.
T212 3474-3827 Sentence denotes In comparison with binding of the wild-type HKU1 S1A conjugated with nanoparticles to rat erythrocytes, the mutant HKU1 S1A with removal of a glycosylation site at element 2 (N251Q) showed increased binding, and the mutant HKU1 S1A with removal of the glycosylation sites in both elements (N29Q in element 1 + N251Q in element 2) showed greater binding.
T213 3828-3985 Sentence denotes These findings indicated that binding of HKU1 S1A to its receptors on rat erythrocytes is impeded by both the RBS architecture and N-glycans on the RBS [92].
T214 3986-4287 Sentence denotes Binding of free HKU1 S1 or free HKU1 S1A not only to rat erythrocytes but also to mouse erythrocytes and to BSM cannot be detected by the standard method unlike other 9-O-Ac-Sia-binding β1CoVs, including HCoV-OC43 for which their free S1 and S1A detectably bind to those erythrocytes and BSM [92,191].
T215 4288-4432 Sentence denotes The difference of HKU1 from other 9-O-Ac-Sia-binding β1CoVs was suggested to be due to receptor fine-specificity determined by elements 1 and 2.
T216 4433-4629 Sentence denotes The effects of the internal part of the glycan structure, such as Siaα2,3/2,6Gal and LN repeats, on binding of HKU1 in comparison with other 9-O-Ac-Sia-binding β1CoVs should be further determined.
T217 4630-4845 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 4846-5187 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 5188-5576 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 5577-5741 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 5742-5942 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 5943-6024 Sentence denotes Interestingly, HCoV-OC43 S1A recognized 9-O-Ac-Sia bound to Gal via α2,6 linkage.
T223 6025-6470 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.