Recombinant SARS-CoV-2 S Protein Binds to Glycans of the Lactosamine Family in vitro

Many viruses, beside binding to their main cell target, interact with other molecules that promote virus adhesion to the cell; often, these additional targets are glycans. The main receptor for SARS-CoV-2 is a peptide motif in the ACE2 protein. We studied interaction of the recombinant SARS-CoV-2 sp...

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Veröffentlicht in:Biochemistry (Moscow) 2021-03, Vol.86 (3), p.243-247
Hauptverfasser: Ryzhikov, Alexandr B., Onkhonova, Galina S., Imatdinov, Ilnaz R., Gavrilova, Elena V., Maksyutov, Rinat A., Gordeeva, Elena A., Pazynina, Galina V., Ryzhov, Ivan M., Shilova, Nadezhda V., Bovin, Nicolai V.
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Sprache:eng
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Zusammenfassung:Many viruses, beside binding to their main cell target, interact with other molecules that promote virus adhesion to the cell; often, these additional targets are glycans. The main receptor for SARS-CoV-2 is a peptide motif in the ACE2 protein. We studied interaction of the recombinant SARS-CoV-2 spike (S) protein with an array of glycoconjugates, including various sialylated, sulfated, and other glycans, and found that the S protein binds some (but not all) glycans of the lactosamine family. We suggest that parallel influenza infection will promote SARS-CoV-2 adhesion to the respiratory epithelial cells due to the unmasking of lactosamine chains by the influenza virus neuraminidase.
ISSN:0006-2979
1608-3040
1608-3040
DOI:10.1134/S0006297921030019