LitCovid-sentences  

PMC:7219429 / 10058-13415 JSONTXT 11 Projects

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Id Subject Object Predicate Lexical cue
T75 0-54 Sentence denotes 3.1 Molecular mimicry between ATM and ganglioside GM1
T76 55-106 Sentence denotes The chemical structure of ATM is shown in Fig. 1 a.
T77 107-245 Sentence denotes The molecule contains two sugar-like pyranyl rings, one with a nitrogen-containing group (N-pyr), the other with an acetyl group (Ac-pyr).
T78 246-425 Sentence denotes The remaining part of the molecule is cyclic, so that its overall conformational flexibility, although significant, is restricted to a limited spatial volume of 2082 Å3 (Fig. 1b).
T79 426-700 Sentence denotes Interestingly, this volume is almost the same as that of the saccharide part of ganglioside GM1 (2293 Å3, Fig. 1b), a lipid raft ganglioside that plays a critical role in the binding and endocytosis of respiratory viruses [26], including pathogenic human coronaviruses [27].
T80 701-920 Sentence denotes Beyond their similar spatial volume, the saccharide part of GM1 and ATM also share some analogous chemical features, including sugar rings and a solvent-accessible surface dotted with several CH and OH groups (Fig. 1b).
T81 921-1039 Sentence denotes This molecular similarity is further illustrated in Figure S1 where ATM is superimposed on the saccharide part of GM1.
T82 1040-1189 Sentence denotes Fig. 1 Structures of azithromycin (ATM) and SARS-CoV-2 spike protein trimer. (a) ATM, with both sugar-like pyranyl groups N-pyr and Ac-pyr indicated.
T83 1190-1414 Sentence denotes The molecules are shown in chemical, tube and sphere rendering (carbon in green, nitrogen in blue, oxygen in red, hydrogen in white). (b) Molecular structure similarity between ATM and the saccharide part of ganglioside GM1.
T84 1415-1554 Sentence denotes Both structures can adopt a globular shape the surface of which is covered with a patchwork of OH (arrows 1 and 2) and CH groups (arrow 3).
T85 1555-1834 Sentence denotes The volume occupied by ATM and the saccharide part of GM1 can be estimated to be 2082 and 2293 Å3, respectively. (c) front and above views of the trimeric spike, each spike protein subunit with a distinct surface colour (cyan for chain A, yellow for chain B, purple for chain C).
T86 1835-1957 Sentence denotes Atoms belonging to the ganglioside-binding domain of each subunit are visible underneath the slightly transparent surface.
T87 1958-2025 Sentence denotes The ganglioside-binding domains, the NTD and the RBD are indicated.
T88 2026-2226 Sentence denotes Given that the SARS-CoV-2 spike protein displays a ganglioside-binding site at the tip of its NTD [10], the possibility that ATM, as a “ganglioside mimic”, could also bind to this site was considered.
T89 2227-2331 Sentence denotes The structural features of the SARS-CoV-2 spike in the prefusion conformation [20] are shown in Fig. 1c.
T90 2332-2466 Sentence denotes It consists of three interdigitated spike proteins that provide the virus its typical corona-like shape in electron microscopy images.
T91 2467-2588 Sentence denotes In each subunit, the most distant part from the viral envelope is divided into two separate domains, the NTD and the RBD.
T92 2589-2768 Sentence denotes The NTD has a flat surface available for ganglioside binding [10], and this process is independent from the ACE-2 receptor recognition, which occurs at the tip of the RBD [11,20].
T93 2769-2884 Sentence denotes When seen from above, the viral spike has a typical triangle shape, with a ganglioside-binding domain at each apex.
T94 2885-3024 Sentence denotes Thus, the spike central area is devoted to ACE-2 binding, leaving three peripheric flat surface areas available for ganglioside attachment.
T95 3025-3165 Sentence denotes Such dual ganglioside/receptor binding is commonly used by pathogenic viruses such as HIV-1 [28], [29], [30] and bacterial neurotoxins [16].
T96 3166-3357 Sentence denotes By combining the high affinity for a single protein receptor with multiple low affinity attachment sites, these pathogens have selected a very efficient pathway to gain entry into host cells.