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


Alexandr B. Ryzhikov1, Galina S. Onkhonova1, Ilnaz R. Imatdinov1, Elena V. Gavrilova1, Rinat A. Maksyutov1, Elena A. Gordeeva2, Galina V. Pazynina2, Ivan M. Ryzhov2, Nadezhda V. Shilova2,3, and Nicolai V. Bovin2,a*

1Vector State Research Center of Virology and Biotechnology, Rospotrebnadzor, 630559 Koltsovo, Novosibirsk Region, Russia

2Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, 117997 Moscow, Russia

3Kulakov National Medical Research Center for Obstetrics, Gynecology and Perinatology, 117997 Moscow, Russia

* To whom correspondence should be addressed.

Received November 7, 2020; Revised November 11, 2020; Accepted November 11, 2020
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.
KEY WORDS: SARS-CoV-2, spike glycoprotein, glycoconjugates, lactosamine

DOI: 10.1134/S0006297921030019