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    Molecular Model of Prion Transmission to Humans

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    Published Version (521.7Kb)
    Date
    2009-12
    Author
    Jones, Michael
    Wight, Darren
    Barron, Rona
    Jeffrey, Martin
    Manson, Jean
    Prowse, Christopher
    Ironside, James W.
    Head, Mark W.
    Metadata
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    Citation
    Jones, M., Wight, D., Barron, R., Jeffrey, M., Manson, J., Prowse, C., Ironside, J.W. and Head, M.W. (2009) ‘Molecular model of prion transmission to humans’, Emerging Infectious Diseases, 15(12), pp. 2013–2016. Available at: https://doi.org/10.3201/eid1512.090194.
    Abstract
    To assess interspecies barriers to transmission of transmissible spongiform encephalopathies, we investigated the ability of disease-associated prion proteins (PrPd) to initiate conversion of the human normal cellular form of prion protein of the 3 major PRNP polymorphic variants in vitro. Protein misfolding cyclic amplification showed that conformation of PrPd partly determines host susceptibility.
    URI
    https://eresearch.qmu.ac.uk/handle/20.500.12289/12719
    Official URL
    https://doi.org/10.3201%2Feid1512.090194
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    • Dietetics, Nutrition and Biological Sciences

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