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  • Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of the VP8* carbohydrate-binding protein of the human rotavirus strain Wa.

    Author(s)
    Kraschnefski, MJ
    Scott, SA
    Holloway, G
    Coulson, BS
    von Itzstein, M
    Blanchard, H
    Griffith University Author(s)
    von Itzstein, Mark
    Coulson, Barbara
    Blanchard, Helen
    Kraschnefski, Mark
    Scott, Stacy
    Year published
    2005
    Metadata
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    Abstract
    Rotaviruses exhibit host-specificity and the first crystallographic information on a rotavirus strain that infects humans is reported here. Recognition and attachment to host cells, leading to invasion and infection, is critically linked to the function of the outer capsid spike protein of the rotavirus particle. In some strains the VP8* component of the spike protein is implicated in recognition and binding of sialic-acid-containing cell-surface carbohydrates, thereby enabling infection by the virus. The cloning, expression, purification, crystallization and initial X-ray diffraction analysis of the VP8* core from human Wa ...
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    Rotaviruses exhibit host-specificity and the first crystallographic information on a rotavirus strain that infects humans is reported here. Recognition and attachment to host cells, leading to invasion and infection, is critically linked to the function of the outer capsid spike protein of the rotavirus particle. In some strains the VP8* component of the spike protein is implicated in recognition and binding of sialic-acid-containing cell-surface carbohydrates, thereby enabling infection by the virus. The cloning, expression, purification, crystallization and initial X-ray diffraction analysis of the VP8* core from human Wa rotavirus is reported. Two crystal forms (trigonal P3221 and monoclinic P21) have been obtained and X-ray diffraction data have been collected, enabling determination of the VP8*64-223 structure by molecular replacement.
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    Journal Title
    Acta Crystallographica Section F: Structural Biology and Crystallization Communications
    Volume
    F61
    DOI
    https://doi.org/10.1107/S1744309105032999
    Subject
    Chemical Sciences
    Biological Sciences
    Publication URI
    http://hdl.handle.net/10072/4189
    Collection
    • Journal articles

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