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Abstract: Self-propagation is characteristic property for a prion conformation. Previous studies revealed that prion protein expressed in the cytoplasm gained a PrPSc-like conformation. However, it remains unclear whether the PrPSc-like conformation has the self-propagating property. We found that PrP partially purified from yeast cytoplasm formed amyloid fiber like structures, and we found that the PrPSc-like conformation is able to convert normal PrPC in the brain homogenate to a proteinase K-resistant conformation. These results suggest that yeast cytoplasm expressed recombinant PrPSc-like conformation has the characteristic self-propagating property of a prion, which may have implications in the pathogenesis of sporadic and inherited prion diseases. [Copyright &y& Elsevier]

Abstract: We used a bovine brain cDNA library to perform a yeast two-hybrid assay with bovine mature PrPC as bait. The screening result showed that αB-crystalline interacted with PrPC. The interaction was further evaluated both in vivo and in vitro with different methods, such as immunofluorescent colocalization, native polyacrylamide-gel electrophoresis, and IAsys biosensor assays. The results suggested that αB-crystalline may have the ability to refold denatured prion proteins, and provided first evidence that αB-crystalline is directly associated with prion protein. [Copyright &y& Elsevier]