Ontology highlight
ABSTRACT:
SUBMITTER: Colby DW
PROVIDER: S-EPMC2409241 | biostudies-other | 2007 Dec
REPOSITORIES: biostudies-other
Colby David W DW Zhang Qiang Q Wang Shuyi S Groth Darlene D Legname Giuseppe G Riesner Detlev D Prusiner Stanley B SB
Proceedings of the National Academy of Sciences of the United States of America 20071220 52
Polymerization of recombinant prion protein (recPrP), which was produced in bacteria, into amyloid fibers was accompanied by the acquisition of prion infectivity. We report here that partially purified preparations of prions seed the polymerization of recPrP into amyloid as detected by a fluorescence shift in the dye Thioflavin T. Our amyloid seeding assay (ASA) detected PrP(Sc), the sole component of the prion, in brain samples from humans with sporadic Creutzfeldt-Jakob disease, as well as in ...[more]