TY - JOUR
T1 - NMR experiments shed new light on glycan recognition by human and murine norovirus capsid proteins
AU - Creutznacher, Robert
AU - Maass, Thorben
AU - Ogrissek, Patrick
AU - Wallmann, Georg
AU - Feldmann, Clara
AU - Peters, Hannelore
AU - Lingemann, Marit
AU - Taube, Stefan
AU - Peters, Thomas
AU - Mallagaray, Alvaro
N1 - Publisher Copyright:
© 2021 by the authors. Licensee MDPI, Basel, Switzerland.
PY - 2021/3
Y1 - 2021/3
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=85103863251&partnerID=8YFLogxK
U2 - 10.3390/v13030416
DO - 10.3390/v13030416
M3 - Journal articles
C2 - 33807801
AN - SCOPUS:85103863251
VL - 13
JO - Viruses
JF - Viruses
SN - 1999-4915
IS - 3
M1 - 416
ER -