NMR experiments shed new light on glycan recognition by human and murine norovirus capsid proteins

Robert Creutznacher, Thorben Maass, Patrick Ogrissek, Georg Wallmann, Clara Feldmann, Hannelore Peters, Marit Lingemann, Stefan Taube*, Thomas Peters, Alvaro Mallagaray

*Corresponding author for this work
8 Citations (Scopus)


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.

Original languageEnglish
Article number416
Issue number3
Publication statusPublished - 03.2021

Research Areas and Centers

  • Academic Focus: Center for Infection and Inflammation Research (ZIEL)
  • Centers: Center for Structural and Cell Biology (CSCM/ZMSZ)

DFG Research Classification Scheme

  • 204-04 Virology


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