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  • Relative roles of GM1 ganglioside, N-acylneuraminic acids, and α2β1 integrin in mediating rotavirus infection

    Author(s)
    Fleming, Fiona E
    Boehm, Raphael
    Dang, Vi T
    Holloway, Gavan
    Haselhorst, Thomas
    Madge, Paul D
    Deveryshetty, Jaigeeth
    Yu, Xing
    Blanchard, Helen
    von Itzstein, Mark
    Coulson, Barbara S
    Griffith University Author(s)
    von Itzstein, Mark
    Haselhorst, Thomas E.
    Madge, Paul D.
    Coulson, Barbara
    Blanchard, Helen
    Yu, Xing
    Bohm, Raphael
    Deveryshetty, Jaigeeth
    Year published
    2014
    Metadata
    Show full item record
    Abstract
    N-acetyl- and N-glycolylneuraminic acids (Sia) and a2߱ integrin are frequently used by rotaviruses as cellular receptors through recognition by virion spike protein VP4. The VP4 subunit VP8*, derived from Wa rotavirus, binds the internal N-acetylneuraminic acid on ganglioside GM1. Wa infection is increased by enhanced internal Sia access following terminal Sia removal from main glycan chains with sialidase. The GM1 ligand cholera toxin B (CTB) reduces Wa infectivity. Here, we found sialidase treatment increased cellular GM1 availability and the infectivity of several other human (including RV-3) and animal rotaviruses, ...
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    N-acetyl- and N-glycolylneuraminic acids (Sia) and a2߱ integrin are frequently used by rotaviruses as cellular receptors through recognition by virion spike protein VP4. The VP4 subunit VP8*, derived from Wa rotavirus, binds the internal N-acetylneuraminic acid on ganglioside GM1. Wa infection is increased by enhanced internal Sia access following terminal Sia removal from main glycan chains with sialidase. The GM1 ligand cholera toxin B (CTB) reduces Wa infectivity. Here, we found sialidase treatment increased cellular GM1 availability and the infectivity of several other human (including RV-3) and animal rotaviruses, typically rendering them susceptible to methyl a-d-N-acetylneuraminide treatment, but did not alter a2߱ usage. CTB reduced the infectivity of these viruses. Aceramido-GM1 inhibited Wa and RV-3 infectivity in untreated and sialidase-treated cells, and GM1 supplementation increased their infectivity, demonstrating the importance of GM1 for infection. Wa recognition of a2߱ and internal Sia were at least partially independent. Rotavirus usage of GM1 was mapped to VP4 using virus reassortants, and RV-3 VP8* bound aceramido-GM1 by saturation transfer difference nuclear magnetic resonance (STD NMR). Most rotaviruses recognizing terminal Sia did not use GM1, including RRV. RRV VP8* interacted minimally with aceramido-GM1 by STD NMR. Unusually, TFR-41 rotavirus infectivity depended upon terminal Sia and GM1. Competition of CTB, Sia, and/or aceramido-GM1 with cell binding by VP8* from representative rotaviruses showed that rotavirus Sia and GM1 preferences resulted from VP8*-cell binding. Our major finding is that infection by human rotaviruses of commonly occurring VP4 serotypes involves VP8* binding to cell surface GM1 glycan, typically including the internal N-acetylneuraminic acid.
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    Journal Title
    Journal of Virology
    Volume
    88
    Issue
    8
    DOI
    https://doi.org/10.1128/JVI.03431-13
    Subject
    Biological sciences
    Virology
    Agricultural, veterinary and food sciences
    Biomedical and clinical sciences
    Publication URI
    http://hdl.handle.net/10072/66797
    Collection
    • Journal articles

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