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  • Structural Basis for Norovirus Inhibition by Human Milk Oligosaccharides

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    Hansman505337-Published.pdf (1.771Mb)
    File version
    Version of Record (VoR)
    Author(s)
    Weichert, S
    Koromyslova, A
    Singh, BK
    Hansman, S
    Jennewein, S
    Schroten, H
    Hansman, GS
    Griffith University Author(s)
    Hansman, Grant S.
    Year published
    2016
    Metadata
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    Abstract
    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
    DOI
    https://doi.org/10.1128/JVI.03223-15
    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
    Publication URI
    http://hdl.handle.net/10072/407048
    Collection
    • Journal articles

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