Next Article in Journal
Interactions of HIV-1 Capsid with Host Factors and Their Implications for Developing Novel Therapeutics
Next Article in Special Issue
Site-Specific O-Glycosylation Analysis of SARS-CoV-2 Spike Protein Produced in Insect and Human Cells
Previous Article in Journal
Antiviral Activity of the PropylamylatinTM Formula against the Novel Coronavirus SARS-CoV-2 In Vitro Using Direct Injection and Gas Assays in Virus Suspensions
Previous Article in Special Issue
ABO Blood Types and COVID-19: Spurious, Anecdotal, or Truly Important Relationships? A Reasoned Review of Available Data
Article

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

1
Institute of Chemistry and Metabolomics, University of Lübeck, Ratzeburger Allee 160, 23562 Lübeck, Germany
2
Institute of Virology and Cell Biology, University of Lübeck, Ratzeburger Allee 160, 23562 Lübeck, Germany
*
Authors to whom correspondence should be addressed.
Academic Editors: Jacques Le Pendu and Göran Larson
Viruses 2021, 13(3), 416; https://doi.org/10.3390/v13030416
Received: 4 February 2021 / Revised: 2 March 2021 / Accepted: 3 March 2021 / Published: 5 March 2021
(This article belongs to the Special Issue Glycans in Viral Infection and Immunity)
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. View Full-Text
Keywords: norovirus P-domain; chemical shift perturbation; histo blood group antigens; sialoglycans; protein-carbohydrate recognition norovirus P-domain; chemical shift perturbation; histo blood group antigens; sialoglycans; protein-carbohydrate recognition
Show Figures

Figure 1

MDPI and ACS Style

Creutznacher, R.; Maass, T.; Ogrissek, P.; Wallmann, G.; Feldmann, C.; Peters, H.; Lingemann, M.; Taube, S.; Peters, T.; Mallagaray, A. NMR Experiments Shed New Light on Glycan Recognition by Human and Murine Norovirus Capsid Proteins. Viruses 2021, 13, 416. https://doi.org/10.3390/v13030416

AMA Style

Creutznacher R, Maass T, Ogrissek P, Wallmann G, Feldmann C, Peters H, Lingemann M, Taube S, Peters T, Mallagaray A. NMR Experiments Shed New Light on Glycan Recognition by Human and Murine Norovirus Capsid Proteins. Viruses. 2021; 13(3):416. https://doi.org/10.3390/v13030416

Chicago/Turabian Style

Creutznacher, Robert, Thorben Maass, Patrick Ogrissek, Georg Wallmann, Clara Feldmann, Hannelore Peters, Marit Lingemann, Stefan Taube, Thomas Peters, and Alvaro Mallagaray. 2021. "NMR Experiments Shed New Light on Glycan Recognition by Human and Murine Norovirus Capsid Proteins" Viruses 13, no. 3: 416. https://doi.org/10.3390/v13030416

Find Other Styles
Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Article Access Map by Country/Region

1
Back to TopTop