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Biochemistry (Mosc) ; 86(3): 243-247, 2021 Mar.
Article in English | MEDLINE | ID: covidwho-1136063

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.


Subject(s)
Amino Sugars/metabolism , COVID-19/metabolism , COVID-19/virology , Polysaccharides/metabolism , SARS-CoV-2/metabolism , Spike Glycoprotein, Coronavirus/metabolism , Amino Sugars/chemistry , Carbohydrate Sequence , Humans , In Vitro Techniques , Models, Molecular , Polysaccharides/chemistry , Protein Binding , Recombinant Proteins/chemistry , Recombinant Proteins/metabolism , SARS-CoV-2/chemistry , SARS-CoV-2/isolation & purification , SARS-CoV-2/physiology , Spike Glycoprotein, Coronavirus/chemistry , Virus Internalization
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