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The infectious agents of the transmissible spongiform encephalopathies are composed of amyloidogenic prion protein, PrP Sc . Real-time quaking-induced conversion can amplify very small amounts of PrP Sc  seeds in tissues/body fluids of patients or animals. Using this  in vitro  PrP-amyloid amplification assay, we quantitated the seeding activity of affected human brains. End-point assay using serially diluted brain homogenates of sporadic Creutzfeldt–Jakob disease patients demonstrated that 50% seeding dose (SD 50 ) is reached approximately 10 10 /g brain (values varies 10 8.79–10.63 /g). A genetic case (GSS-P102L) yielded a similar level of seeding activity in an autopsy brain sample. The range of PrP Sc  concentrations in the samples, determined by dot-blot assay, was 0.6–5.4 μg/g brain; therefore, we estimated that 1 SD 50  unit was equivalent to 0.06–0.27 fg of PrP Sc . The SD 50  values of the affected brains dropped more than three orders of magnitude after autoclaving at 121°C. This new method for quantitation of human prion activity provides a new way to reduce the risk of iatrogenic prion transmission.

Rapid and Quantitative Assay of Amyloid-Seeding Activity in Human Brains Affected with Prion Diseases