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STD NMR experiments confirm the binding of sialoglycans to the S\u2010protein of the prototypic Wuhan strain virus and yield dissociation constants in the millimolar range. The absence of STD effects for sialoglycans in the presence of the Omicron\/BA.1 S\u2010protein reflects a loss of binding as a result of S\u2010protein evolution. Likewise, no STD effects are observed for the deletion mutant \u0394143\u2013145 of the Wuhan S\u2010protein, thus supporting localization of the binding site in the N\u2010terminal domain (NTD). The glycomimetics Oseltamivir and Zanamivir bind weakly to the S\u2010protein of both virus strains. Binding of blood group antigens to the Wuhan S\u2010protein cannot be confirmed by STD NMR. Using <jats:sup>1<\/jats:sup>H,<jats:sup>15<\/jats:sup>N TROSY HSQC\u2010based chemical shift perturbation (CSP) experiments, we excluded binding of any of the ligands studied to the RBD of the Wuhan S\u2010protein. Our results put reported data on glycan binding into perspective and shed new light on the potential role of glycan\u2010binding to the S\u2010protein.<\/jats:p>","DOI":"10.1002\/chem.202202614","type":"journal-article","created":{"date-parts":[[2022,9,26]],"date-time":"2022-09-26T14:33:42Z","timestamp":1664202822000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":13,"title":["Binding of Glycans to the SARS CoV\u20102 Spike Protein, an Open Question: NMR Data on Binding Site Localization, Affinity, and Selectivity"],"prefix":"10.1002","volume":"28","author":[{"given":"Thorben","family":"Maass","sequence":"first","affiliation":[{"name":"Institute of Chemistry and Metabolomics Center of Structural and Cell Biology in Medicine University of L\u00fcbeck  Ratzeburger Allee 160 23562 L\u00fcbeck 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