Structural basis for norovirus inhibition by human milk oligosaccharides

Histo-blood group antigens (HBGAs) are important binding factors for norovirus infections. We show that two human milk oligosaccharides, 2′-fucosyllactose (2′FL) and 3-fucosyllactose (3FL), could block norovirus from binding to surrogate HBGA samples. We found that 2′FL and 3FL bound at the equivale...

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Hauptverfasser: Weichert, Stefan (VerfasserIn) , Koromyslova, Anna D. (VerfasserIn) , Singh, Bishal (VerfasserIn) , Hansman, Satoko (VerfasserIn) , Schroten, Horst (VerfasserIn) , Hansman, Grant S. (VerfasserIn)
Dokumenttyp: Article (Journal)
Sprache:Englisch
Veröffentlicht: 17 February 2016
In: Journal of virology
Year: 2016, Jahrgang: 90, Heft: 9, Pages: 4843-4848
ISSN:1098-5514
DOI:10.1128/JVI.03223-15
Online-Zugang:Verlag, Volltext: https://doi.org/10.1128/JVI.03223-15
Verlag, Volltext: https://jvi.asm.org/content/90/9/4843
Volltext
Verfasserangaben:Stefan Weichert, Anna Koromyslova, Bishal K. Singh, Satoko Hansman, Stefan Jennewein, Horst Schroten, Grant S. Hansman
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Zusammenfassung:Histo-blood group antigens (HBGAs) are important binding factors for norovirus infections. We show that two human milk oligosaccharides, 2′-fucosyllactose (2′FL) and 3-fucosyllactose (3FL), could block norovirus from binding to surrogate HBGA samples. We found that 2′FL and 3FL bound at the equivalent HBGA pockets on the norovirus capsid using X-ray crystallography. Our data revealed that 2′FL and 3FL structurally mimic HBGAs. These results suggest that 2′FL and 3FL might act as naturally occurring decoys in humans.
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Beschreibung:Online Resource
ISSN:1098-5514
DOI:10.1128/JVI.03223-15