Author: 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.
Title: Recombinant SARS-CoV-2 S Protein Binds to Glycans of the Lactosamine Family in vitro Cord-id: oc3sttwb Document date: 2021_2_25
ID: oc3sttwb
Snippet: 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
Document: 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. ELECTRONIC SUPPLEMENTARY MATERIAL: Supplementary material is available in the online version of this article at 10.1134/S0006297921030019 and on the journal website (http://protein.bio.msu.ru/biokhimiya).
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