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

Biochemistry (Mosc). 2021 Mar;86(3):243-247. doi: 10.1134/S0006297921030019.

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.

Keywords: SARS-CoV-2; glycoconjugates; lactosamine; spike glycoprotein.

MeSH terms

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

Substances

  • Amino Sugars
  • Polysaccharides
  • Recombinant Proteins
  • Spike Glycoprotein, Coronavirus
  • spike protein, SARS-CoV-2
  • lactosamine