Sergio Migliore

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Sheep CH1641-like transmissible spongiform encephalopathy isolates have shown molecular similarities to bovine spongiform encephalopathy (BSE) isolates. We report that the prion protein PrPSc from sheep BSE is extremely resistant to denaturation. This feature, combined with the N-terminal PrPSc cleavage, allowed differentiation of classical scrapie,(More)
The ability of PrP Sc to convert PrP C into protease-resistance isoforms has been exploited using a variety of techniques such as protein misfolding cyclic amplification (PMCA), quaking induced conversion (QuIC) and most recently, real-time quaking induced conversion (RT-QuIC). 1 These cell-free assays have enabled a better understanding of prion diseases(More)
BACKGROUND Transmissible spongiform encephalopathies (TSE) are fatal neurodegenerative diseases of several mammalian species, including humans. In Italy, the active surveillance through rapid tests on brain stem from small ruminants started in 2002 on randomly selected samples of healthy slaughtered animals. Sampling number was proportionally related to the(More)
It is widely known that prion strains can mutate in response to modification of the replication environment and we have recently reported that prion mutations can occur in vitro during amplification of vole-adapted prions by Protein Misfolding Cyclic Amplification on bank vole substrate (bvPMCA). Here we exploited the high efficiency of prion replication by(More)
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