Title |
Prion subcellular fractionation reveals infectivity spectrum, with a high titre-low PrPreslevel disparity
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Published in |
Molecular Neurodegeneration, April 2012
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DOI | 10.1186/1750-1326-7-18 |
Pubmed ID | |
Authors |
Victoria Lewis, Cathryn L Haigh, Colin L Masters, Andrew F Hill, Victoria A Lawson, Steven J Collins |
Abstract |
Prion disease transmission and pathogenesis are linked to misfolded, typically protease resistant (PrPres) conformers of the normal cellular prion protein (PrPC), with the former posited to be the principal constituent of the infectious 'prion'. Unexplained discrepancies observed between detectable PrPres 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 PrPres levels and infectivity titres at a subcellular resolution. |
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Researcher | 7 | 27% |
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Veterinary Science and Veterinary Medicine | 1 | 4% |
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