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Cell-free propagation of prion strains
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Journal Article
Cell-free propagation of prion strains
2008
Overview
Prions are the infectious agents responsible for prion diseases, which appear to be composed exclusively by the misfolded prion protein (PrP
Sc
). Disease is transmitted by the autocatalytic propagation of PrP
Sc
misfolding at the expense of the normal prion protein. The biggest challenge of the prion hypothesis has been to explain the molecular mechanism by which prions can exist as different strains, producing diseases with distinguishable characteristics. Here, we show that PrP
Sc
generated
in vitro
by protein misfolding cyclic amplification from five different mouse prion strains maintains the strain‐specific properties. Inoculation of wild‐type mice with
in vitro
‐generated PrP
Sc
caused a disease with indistinguishable incubation times as well as neuropathological and biochemical characteristics as the parental strains. Biochemical features were also maintained upon replication of four human prion strains. These results provide additional support for the prion hypothesis and indicate that strain characteristics can be faithfully propagated in the absence of living cells, suggesting that strain variation is dependent on PrP
Sc
properties.
Publisher
John Wiley & Sons, Ltd,Nature Publishing Group UK,Springer Nature B.V,Nature Publishing Group
Subject
