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

18Citations
Citations of this article
38Readers
Mendeley users who have this article in their library.

Abstract

Abstract: 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.

Cite

CITATION STYLE

APA

Ryzhikov, A. B., Onkhonova, G. S., Imatdinov, I. R., Gavrilova, E. V., Maksyutov, R. A., Gordeeva, E. A., … Bovin, N. V. (2021). Recombinant SARS-CoV-2 S Protein Binds to Glycans of the Lactosamine Family in vitro. Biochemistry (Moscow), 86(3), 243–247. https://doi.org/10.1134/S0006297921030019

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free