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10.1002/anie.202201432

http://scihub22266oqcxt.onion/10.1002/anie.202201432
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35191576!9074024!35191576
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suck abstract from ncbi


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pmid35191576      Angew+Chem+Int+Ed+Engl 2022 ; 61 (18): e202201432
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  • The SARS-CoV-2 Spike Glycoprotein Directly Binds Exogeneous Sialic Acids: A NMR View #MMPMID35191576
  • Unione L; Moure MJ; Lenza MP; Oyenarte I; Ereno-Orbea J; Arda A; Jimenez-Barbero J
  • Angew Chem Int Ed Engl 2022[Apr]; 61 (18): e202201432 PMID35191576show ga
  • The interaction of the SARS CoV2 spike glycoprotein with two sialic acid-containing trisaccharides (alpha2,3 and alpha2,6 sialyl N-acetyllactosamine) has been demonstrated by NMR. The NMR-based distinction between the signals of those sialic acids in the glycans covalently attached to the spike protein and those belonging to the exogenous alpha2,3 and alpha2,6 sialyl N-acetyllactosamine ligands has been achieved by synthesizing uniformly (13) C-labelled trisaccharides at the sialic acid and galactose moieties. STD-(1) H,(13) C-HSQC NMR experiments elegantly demonstrate the direct interaction of the sialic acid residues of both trisaccharides with additional participation of the galactose moieties, especially for the alpha2,3-linked analogue. Additional experiments with the spike protein in the presence of a specific antibody for the N-terminal domain and with the isolated receptor binding and N-terminal domains of the spike protein unambiguously show that the sialic acid binding site is located at the N-terminal domain.
  • |*COVID-19[MESH]
  • |*Spike Glycoprotein, Coronavirus/chemistry[MESH]
  • |Binding Sites[MESH]
  • |Galactose[MESH]
  • |Humans[MESH]
  • |N-Acetylneuraminic Acid/chemistry[MESH]
  • |SARS-CoV-2[MESH]
  • |Sialic Acids/chemistry[MESH]


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