Recombinant mouse prion protein (recMoPrP) produced in Escherichia coli was polymerized into amyloid fibrils that represent a subset of beta sheet-rich structures. Fibrils consisting of recMoPrP(89-230) were inoculated intracerebrally into transgenic (Tg) mice expressing MoPrP(89-231). The mice developed neurologic dysfunction between 380 and 660 days after inoculation. Brain extracts showed protease-resistant PrP by Western blotting; these extracts transmitted disease to wild-type FVB mice and Tg mice overexpressing PrP, with incubation times of 150 and 90 days, respectively. Neuropathological findings suggest that a novel prion strain was created. Our results provide compelling evidence that prions are infectious proteins.
|Titolo:||Synthetic mammalian prions|
|Autori:||Legname, G.; Baskakov, I. V.; Nguyen, H. -O. B.; Riesner, D.; Cohen, F. E.; Dearmond, S. J.; Prusiner, S. B.|
|Data di pubblicazione:||2004|
|Digital Object Identifier (DOI):||10.1126/science.1100195|
|Appare nelle tipologie:||1.1 Journal article|