Journal article
Prion subcellular fractionation reveals infectivity spectrum, with a high titre-low PrP res level disparity
V Lewis, CL Haigh, CL Masters, AF Hill, VA Lawson, SJ Collins
Molecular Neurodegeneration | BMC | Published : 2012
Abstract
Background: Prion disease transmission and pathogenesis are linked to misfolded, typically protease resistant (PrP res) conformers of the normal cellular prion protein (PrP C), with the former posited to be the principal constituent of the infectious 'prion'. Unexplained discrepancies observed between detectable PrP res and infectivity levels exemplify the complexity in deciphering the exact biophysical nature of prions and those host cell factors, if any, which contribute to transmission efficiency. In order to improve our understanding of these important issues, this study utilized a bioassay validated cell culture model of prion infection to investigate discordance between PrP res levels ..
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Grants
Awarded by Australian Research Council
Funding Acknowledgements
The authors thank Professor Charles Weissmann for the gift of the Tga20 transgenic mice, the Animal Housing Facility staff in the Faculty of Medicine, Dentistry and Health Sciences, the University of Melbourne for their assistance with animal husbandry, and Ms Laura Leone for technical assistance with preparation of the mouse brains for neuropathological assessment. This work was funded by an Australian Government National Health and Medical Research Council (NHMRC) Program Grant (#400202). VL is supported by NHMRC Training Fellowship (#567123). SJC is supported by NHMRC Practitioner Fellowship (#400183). VAL is supported by The University of Melbourne CR Roper Fellowship. AFH is supported by an Australian Research Council Future Fellowship (FT10100560).