LitCovid-sentences  

PMC:7556165 / 44914-49334 JSONTXT 13 Projects

Annnotations TAB TSV DIC JSON TextAE

Id Subject Object Predicate Lexical cue
T275 0-37 Sentence denotes SARS-CoV-2 RBD and Its Receptor, ACE2
T276 38-185 Sentence denotes Since SARS-CoV-2 and SARS-CoV share the same host cell receptor, it was early questioned whether SARS-CoV-2 retains the same RBD motif of SARS-CoV.
T277 186-262 Sentence denotes SARS-CoV RBD corresponds to residues 306–527 of S protein (Li et al., 2005).
T278 263-402 Sentence denotes Sequence analysis shows that residues 319–541 of SARS-CoV-2 (S319–341) share 73.9% sequence identity with SARS-CoV RBD (Wang et al., 2020).
T279 403-533 Sentence denotes Accordingly, Wang et al. (2020) clearly demonstrated that S319–341 corresponds to SARS-CoV-2 RBD by immunofluorescence microscopy.
T280 534-737 Sentence denotes Indeed SARS-CoV-2 S1 and S319–341 positively colocalized with GFP-tagged ACE2 expressed on cell surface of HEK cells, whereas this interaction did not occur with membrane-expressed hDPP4 (MERS receptor).
T281 738-867 Sentence denotes Additionally, soluble ACE2 inhibited the interaction between viral proteins and ACE2-expressing cells in a dose-dependent manner.
T282 868-944 Sentence denotes The SARS-CoV-2 RBD sequence was further investigated by structural analysis.
T283 945-1342 Sentence denotes X-ray crystallography showed that SARS-CoV-2 RBD folds into two structural domains (Figure 8): (1) the core subdomain with five antiparallel β-strands (β1, β2, β3, β4, β7), (2) the external subdomain, which inserts between β4 and β7, and it is characterized by the two small β5 and β6 strands [β1’ and β2’ in Wang et al. (2020)] connected by a disulfide bond (Lan et al., 2020; Wang et al., 2020).
T284 1343-1610 Sentence denotes In keeping with their high sequence homology, the 3D structure of SARS-COV-2 and SARS-CoV RBD nearly superimpose (RMSD = 0.475 Å for 128 Cα atoms; Wang et al., 2020) with the exception of the β5/β6 loop, which actually entailed the larger primary sequence difference.
T285 1611-1845 Sentence denotes FIGURE 8 Crystal structure of SARS-CoV-2 spike receptor-binding domain bound with ACE2. (A) Cartoon representation. (B) Gaussian surface representation. hACE2 is in green, the core of SARS-CoV-2 RBD is in red, and the RBM is in blue.
T286 1846-1918 Sentence denotes The β1-β7 typical motifs of RBD (Lan et al., 2020) are indicated in (A).
T287 1919-2009 Sentence denotes The structures have been drawn from PDB 6MOJ (Lan et al., 2020) by Mol on the PDB website.
T288 2010-2087 Sentence denotes Several researchers investigated the interaction of SARS-CoV-2 RBD with ACE2.
T289 2088-2174 Sentence denotes Unfortunately, each group committed to slightly different sequences of SARS-CoV-2 RBD.
T290 2175-2335 Sentence denotes To avoid confusion, we will always report the actual sequence with respect to the S protein when the RBD under study differs from the canonical 319–541 stretch.
T291 2336-2450 Sentence denotes In vitro affinity studies revealed dissociation constants of the ACE2-RBD complex in the 1–100 nM range (Table 1).
T292 2451-2599 Sentence denotes Non univocal data are attributable to the dissimilar sequences that were investigated and/or to the immobilization procedures (Shang et al., 2020b).
T293 2600-2791 Sentence denotes In spite of this variability, SARS-CoV-2 RBD was always found to bind ACE2 4–10 fold stronger than SARS-CoV RBD (Lan et al., 2020; Shang et al., 2020b; Walls et al., 2020; Wang et al., 2020).
T294 2792-3009 Sentence denotes The affinity difference in vitro was confirmed also in vivo by the stronger binding of SARS-CoV-2 S331–524 to ACE2 expressed on cells (SARS-CoV-2: EC50 = 0.08 μg/ml vs. SARS-CoV: EC50 = 0.96 μg/ml) (Tai et al., 2020).
T295 3010-3187 Sentence denotes Paradoxically, however, it has been shown that the ACE2 binding affinity for the entire SARS-CoV-2 S protein is lower than or comparable to that of SARS S (Shang et al., 2020a).
T296 3188-3431 Sentence denotes This surprising result suggests that SARS-CoV-2 RBD, albeit more potent, is less efficiently exposed than SARS-CoV RBD by the dynamic transition between the “closed” and “open” states, probably in order to escape the immune system of the host.
T297 3432-3758 Sentence denotes Thus, the non-identical S1 sequences of SARS-CoV-2 and SARS-CoV reflect the molecular evolution of SARS-CoV-2 toward: (1) much stronger affinity toward ACE2, (2) reduced antigenicity of the RBD region (which is one of the most antigenic segments in the S protein), (3) greater and less specific cleavability by host proteases.
T298 3759-3876 Sentence denotes Taken together, these properties account for the sophisticated strategy exploited by SARS-CoV-2 to invade host cells.
T299 3877-3970 Sentence denotes TABLE 1 Binding affinity between SARS-CoV-2 spike (S) protein and S subset regions and ACE2.
T300 3971-4008 Sentence denotes Sequence KD (nM) Method References
T301 4009-4048 Sentence denotes SARS-2 S 14.7 SPR Wrapp et al., 2020
T302 4049-4086 Sentence denotes SARS-2 S 11.2 SPR Lei et al., 2020
T303 4087-4136 Sentence denotes SARS-2 S20–685 (S1) 94.6 SPR Wang et al., 2020
T304 4137-4189 Sentence denotes SARS-2 S319–541 (RBD) 133.3 SPR Wang et al., 2020
T305 4190-4239 Sentence denotes SARS-2 S319–541 (RBD) 4.7 SPR Lan et al., 2020
T306 4240-4287 Sentence denotes SARS-2 S319–529 44.2 SPR Shang et al., 2020b
T307 4288-4354 Sentence denotes SARS-2 S319–591 34.6 Biolayer interferometry Wrapp et al., 2020
T308 4355-4420 Sentence denotes SARS-2 S328–533 1.2 Biolayer interferometry Walls et al., 2020