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

doi:10.3390/v13030416

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

18 Citations (Scopus)

Abstract

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 language	English
Article number	416
Journal	Viruses
Volume	13
Issue number	3
DOIs	https://doi.org/10.3390/v13030416
Publication status	Published - 03.2021

Funding

This research was funded by the Deutsche Forschungsgemeinschaft (DFG) via grants Pe494/12-2 (T.P.) and TA1093-2 (S.T.) within the research unit FOR2327 (ViroCarb). T.P. thanks the State of Schleswig-Holstein for supplying the NMR infrastructure (European Funds for Regional Development, LPW-E/1.1.2/857). P.O. and C.F. thank the Studienstiftung des deutschen Volkes for fellowships. Funding: This research was funded by the Deutsche Forschungsgemeinschaft (DFG) via grants Pe494/12-2 (T.P.) and TA1093-2 (S.T.) within the research unit FOR2327 (ViroCarb). T.P. thanks the State of Schleswig-Holstein for supplying the NMR infrastructure (European Funds for Regional Development, LPW-E/1.1.2/857). P.O. and C.F. thank the Studienstiftung des deutschen Volkes for fellowships.

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

SDG 3 Good Health and Well-being

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

2.21-04 Virology

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10.3390/v13030416

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title = "NMR experiments shed new light on glycan recognition by human and murine norovirus capsid proteins",

abstract = "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.",

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

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year = "2021",

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doi = "10.3390/v13030416",

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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

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.

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

Abstract

Funding

UN SDGs

Research Areas and Centers

DFG Research Classification Scheme

Access to Document

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