In vitro self-propagation of recombinant PrPSc-like conformation generated in the yeast cytoplasm.
Self-propagation is characteristic property for a prion conformation. Previous studies revealed that prion protein expressed in the cytoplasm gained a PrP(Sc)-like conformation. However, it remains unclear whether the PrP(Sc)-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 PrP(Sc)-like conformation is able to convert normal PrP(C) in the brain homogenate to a proteinase K-resistant conformation. These results suggest that yeast cytoplasm expressed recombinant PrP(Sc)-like conformation has the characteristic self-propagating property of a prion, which may have implications in the pathogenesis of sporadic and inherited prion diseases.
Yang
Wenbin
W
Research Center of Molecular Virology, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100080, China.
Yang
Huaiyi
H
Tien
Po
P
D000682:Amyloid / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism / Q000648:ultrastructure; D000818:Animals; D001923:Brain Chemistry; D002474:Cell-Free System / Q000737:chemistry / Q000378:metabolism; D019286:Endopeptidase K / Q000737:chemistry*; D051379:Mice; D008807:Mice, Inbred BALB C; D018620:PrPSc Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D017096:Prion Diseases / Q000235:genetics / Q000378:metabolism; D011487:Protein Conformation; D051381:Rats; D017207:Rats, Sprague-Dawley; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D012441:Saccharomyces cerevisiae
D000682:Amyloid; D018620:PrPSc Proteins; D011994:Recombinant Proteins; D019286:Endopeptidase K