Evidence against efficient spontaneous disassembly of prions into small oligomers.

ABSTRACT: Infectious prion assemblies must fragment to replicate, spread, and trigger disease. However, the extent to which various types of amyloid fibrils fragment on their own versus being driven by other cellular processes is unclear. In the case of highly infectious, tissue-derived prion (PrP^Sc) preparations, over 40 years of previous studies have yielded starkly contradictory indications on this question. Many have reported high stability of PrP^Sc multimers in even strong detergents. However, others using nondisinfecting detergents and size-exclusion chromatography combined with light scattering measurements have described complete spontaneous disassembly into dimeric-tetrameric units. In attempting to replicate the latter experiments, we determined that PrP^Sc

SUBMITTER: Shoup D 

PROVIDER: S-EPMC12301739 | biostudies-literature | 2025 Jun

REPOSITORIES: biostudies-literature