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Propagation of PrP Sc in mice reveals impact of aggregate composition on prion disease pathogenesis
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Propagation of PrP Sc in mice reveals impact of aggregate composition on prion disease pathogenesis
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Journal Article
Propagation of PrP Sc in mice reveals impact of aggregate composition on prion disease pathogenesis
2023
Overview
Infectious prions consist of PrP
, a misfolded, aggregation-prone isoform of the host's prion protein. PrP
assemblies encode distinct biochemical and biological properties. They harbor a specific profile of PrP
species, from small oligomers to fibrils in different ratios, where the highest infectivity aligns with oligomeric particles. To investigate the impact of PrP
aggregate complexity on prion propagation, biochemical properties, and disease pathogenesis, we fractionated elk prions by sedimentation velocity centrifugation, followed by sub-passages of individual fractions in cervidized mice. Upon first passage, different fractions generated PrP
with distinct biochemical, biophysical, and neuropathological profiles. Notably, low or high molecular weight PrP
aggregates caused different clinical signs of hyperexcitability or lethargy, respectively, which were retained over passage, whereas other properties converged. Our findings suggest that PrP
quaternary structure determines an initial selection of a specific replication environment, resulting in transmissible features that are independent of PrP
biochemical and biophysical properties.
