NR AVAB
AU Yang,W.; Yang,H.; Tien,P.
TI In vitro self-propagation of recombinant PrPsc-like conformation generated in the yeast cytoplasm
QU FEBS Letters 2006 Jul 24; 580(17): 4231-5
PT journal article
AB 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.
MH Amyloid/*chemistry/genetics/metabolism/ultrastructure; Animals; Brain Chemistry; Cell-Free System/chemistry/metabolism; Endopeptidase K/*chemistry; Mice; Mice, Inbred BALB C; PrPsc Proteins/*chemistry/genetics/metabolism; Prion Diseases/genetics/metabolism; Protein Conformation; Rats; Rats, Sprague-Dawley; Recombinant Proteins/chemistry/genetics/metabolism; Research Support, Non-U.S. Gov't; Saccharomyces cerevisiae
AD Research Center of Molecular Virology, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100080, China.
SP englisch
PO Niederlande