Structural Basis for Norovirus Inhibition by Human Milk Oligosaccharides
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Author(s)
Weichert, S
Koromyslova, A
Singh, BK
Hansman, S
Jennewein, S
Schroten, H
Hansman, GS
Griffith University Author(s)
Year published
2016
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Show full item recordAbstract
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.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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Journal Title
Journal of Virology
Volume
90
Issue
9
Copyright Statement
© 2016 American Society for Microbiology. The attached file is reproduced here in accordance with the copyright policy of the publisher. Please refer to the journal's website for access to the definitive, published version.
Subject
Biological sciences
Virology
Health sciences
Agricultural, veterinary and food sciences
Science & Technology
Life Sciences & Biomedicine
BLOOD-GROUP ANTIGENS
BINDING SPECIFICITY