| Literature DB >> 33838626 |
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, Nicolai V Bovin4.
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.Entities:
Keywords: SARS-CoV-2; glycoconjugates; lactosamine; spike glycoprotein
Mesh:
Substances:
Year: 2021 PMID: 33838626 PMCID: PMC7905424 DOI: 10.1134/S0006297921030019
Source DB: PubMed Journal: Biochemistry (Mosc) ISSN: 0006-2979 Impact factor: 2.487