NMR Experiments Shed New Light on Glycan Recognition by Human and Murine Norovirus Capsid Proteins

Viruses. 2021 Mar 5;13(3):416. doi: 10.3390/v13030416.


Glycan-protein interactions are highly specific yet transient, rendering glycans ideal recognition signals in a variety of biological processes. In human norovirus (HuNoV) infection, histo-blood group antigens (HBGAs) play an essential but poorly understood role. For murine norovirus infection (MNV), sialylated glycolipids or glycoproteins appear to be important. It has also been suggested that HuNoV capsid proteins bind to sialylated ganglioside head groups. Here, we study the binding of HBGAs and sialoglycans to HuNoV and MNV capsid proteins using NMR experiments. Surprisingly, the experiments show that none of the norovirus P-domains bind to sialoglycans. Notably, MNV P-domains do not bind to any of the glycans studied, and MNV-1 infection of cells deficient in surface sialoglycans shows no significant difference compared to cells expressing respective glycans. These findings redefine glycan recognition by noroviruses, challenging present models of infection.

Keywords: chemical shift perturbation; histo blood group antigens; norovirus P-domain; protein-carbohydrate recognition; sialoglycans.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Binding Sites
  • Blood Group Antigens / immunology*
  • Caliciviridae Infections* / immunology
  • Caliciviridae Infections* / virology
  • Capsid Proteins / immunology*
  • Humans
  • Mice
  • Models, Molecular
  • Norovirus / immunology*
  • Polysaccharides*
  • Protein Binding
  • Virus Attachment


  • Blood Group Antigens
  • Capsid Proteins
  • Polysaccharides