The ability of norovirus to infect host cells depends on the interaction between the Protruding domain (P domain) of its capsid protein VP1 and Histo-Blood Group Antigens (HBGAs) on the surface of host cells. Furthermore, previous cell-based studies found, that Human Milk Oligosaccharides (HMOs) prevent norovirus infection to cells, by acting as a decoy receptor and blocking the interaction between HBGAs and human noroviruses. Therefore, understanding the structure of the P domain is essential for the development of effective antiviral drugs and vaccines.

Expression And NMR Characterization Of Labelled P-domains Of Emerging Norovirus / S. Lin, I.Z.. - ELETTRONICO. - (2025), pp. 1-1. (“Structural Glycoscience” Summer School ).

Expression And NMR Characterization Of Labelled P-domains Of Emerging Norovirus

I. Zeravica;R. Calamandrei;L. Cerofolini;C. Nativi;M. Fragai
2025

Abstract

The ability of norovirus to infect host cells depends on the interaction between the Protruding domain (P domain) of its capsid protein VP1 and Histo-Blood Group Antigens (HBGAs) on the surface of host cells. Furthermore, previous cell-based studies found, that Human Milk Oligosaccharides (HMOs) prevent norovirus infection to cells, by acting as a decoy receptor and blocking the interaction between HBGAs and human noroviruses. Therefore, understanding the structure of the P domain is essential for the development of effective antiviral drugs and vaccines.
2025
Book of abstract “Structural Glycoscience” Summer School
“Structural Glycoscience” Summer School
S. Lin, I. Zeravica, H. Flatau, L. Pisapia, R. Calamandrei, L. Cerofolini, A. Varrot, A. Imberty, J. Angulo, C. Nativi, M. Fragai
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Utilizza questo identificatore per citare o creare un link a questa risorsa: https://hdl.handle.net/2158/1486513
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