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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| Main Authors: | , , , , , |
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| Format: | Article (Journal) |
| Language: | English |
| Published: |
17 February 2016
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| In: |
Journal of virology
Year: 2016, Volume: 90, Issue: 9, Pages: 4843-4848 |
| ISSN: | 1098-5514 |
| DOI: | 10.1128/JVI.03223-15 |
| Online Access: | Verlag, Volltext: https://doi.org/10.1128/JVI.03223-15 Verlag, Volltext: https://jvi.asm.org/content/90/9/4843 
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| Author Notes: | Stefan Weichert, Anna Koromyslova, Bishal K. Singh, Satoko Hansman, Stefan Jennewein, Horst Schroten, Grant S. Hansman |
| Summary: | 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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| Item Description: | Gesehen am 21.05.2019 |
| Physical Description: | Online Resource |
| ISSN: | 1098-5514 |
| DOI: | 10.1128/JVI.03223-15 |