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  • Crystallisation and preliminary X-ray diffraction analysis of the carbohydrate-recognizing domain (VP8*) of bovine rotavirus strain NCDV

    Author(s)
    Yu, Xing
    Guillon, Annabel
    Szyczew, Alex J
    Kiefel, Milton J
    Coulson, Barbara S
    von Itzstein, Mark
    Blanchard, Helen
    Griffith University Author(s)
    von Itzstein, Mark
    Kiefel, Milton
    Coulson, Barbara
    Szyczew, Alexander J.
    Blanchard, Helen
    Yu, Xing
    Year published
    2008
    Metadata
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    Abstract
    Infectivity of rotavirus is dramatically enhanced by proteolytic cleavage of its outer layer VP4 spike protein into two function domains, VP8* and VP5*. The carbohydrate-recognising domain VP8* is proposed to bind sialic acid-containing host cell-surface glycans, followed by a series of subsequent virus-cell interactions. Live attenuated human and bovine rotavirus vaccine candidates to prevent gastroenteritis have been derived from bovine rotavirus strain NCDV. The NCDV VP8*64-224 was over-expressed, purified to homogeneity and crystallized in the presence of a N-acetylneuraminic acid derivative. X-ray diffraction data were ...
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    Infectivity of rotavirus is dramatically enhanced by proteolytic cleavage of its outer layer VP4 spike protein into two function domains, VP8* and VP5*. The carbohydrate-recognising domain VP8* is proposed to bind sialic acid-containing host cell-surface glycans, followed by a series of subsequent virus-cell interactions. Live attenuated human and bovine rotavirus vaccine candidates to prevent gastroenteritis have been derived from bovine rotavirus strain NCDV. The NCDV VP8*64-224 was over-expressed, purified to homogeneity and crystallized in the presence of a N-acetylneuraminic acid derivative. X-ray diffraction data were collected to a resolution of 2.0 Šand the crystallographic structure of NCDV VP8*64-224 determined by molecular replacement.
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    Journal Title
    Acta Crystallographica Section F - Structural Biology and Crystallization Communications
    Volume
    F64
    Publisher URI
    http://journals.iucr.org/f/issues/2008/06/00/issconts.html
    Subject
    Chemical Sciences
    Biological Sciences
    Publication URI
    http://hdl.handle.net/10072/20267
    Collection
    • Journal articles

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