Abstract

We have observed that hamster prion protein (PrPC) undergoes conformational changes on exposure to heat or sonication. If a sonication induced new conformer is seeded with a small amount of its abnormal pathogenic isoform (PrPSc) it undergoes a significant conversion to a proteinase-resistant isoform. This suggests the presence of a third stable PrP conformer, which may be intermediate in the conversion of PrPC to PrPSc.

Keywords: Prion protein, scrapie, PMCA, sonication, protein aggregation