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• W2014517573 abstract "Crude brain homogenates of terminally diseased hamsters infected with the 263K strain of scrapie (PrP^Sc) and purified prion fibrils were heated or pressurized at 800 megapascals and 60 °C for 2 h in different buffers and in water. Prion proteins (PrP) were analyzed for their proteinase K resistance in immunoblots and for their infectivity in hamster bioassays. A notable decrease in the proteinase K resistance of unpurified prion proteins, probably because of pressure-induced changes in the protein conformation of native PrP^Sc or the <i>N</i>-truncated PrP-(27–30), could be demonstrated when pressurized at initially neutral conditions in several buffers and in water but not in a slightly acidic pH. A subsequent 6–7 log₁₀ reduction of infectious units/g in phosphate-buffered saline buffer, pH 7.4, was found. The proteinase K-resistant core was also not detectable after purification of prions extracted from pressurized samples, confirming pressure effects at the level of the secondary structure of prion proteins. However, opposite results were found after pressurizing purified prions, arguing for the existence of pressure-sensitive β-structures (PrP^Sc_ΔPsen) and extremely pressure-resistant β-structures (PrP^Sc_ΔPres). Remarkably, after the first centrifugation step at 540,000 × <i>g</i> during isolation, prions remained proteinase K-resistant when pressurized in all tested buffers and in water. It is known that purified fibrils retain infectivity, but the isolated protein (full and <i>N</i>-truncated) behaved differently from native PrP^Sc under pressure, suggesting a kind of semicrystalline polymer structure." @default.
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• W2014517573 date "2005-03-01" @default.
• W2014517573 modified "2023-10-18" @default.
• W2014517573 title "Dual Nature of the Infectious Prion Protein Revealed by High Pressure" @default.
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• W2014517573 doi "https://doi.org/10.1074/jbc.m410679200" @default.
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