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TitleEx vivo mammalian prions are formed of paired double helical prion protein fibrils.
Journal, issue, pagesOpen Biol, Vol. 6, Issue 5, Year 2016
Publish dateMay 4, 2016
AuthorsCassandra Terry / Adam Wenborn / Nathalie Gros / Jessica Sells / Susan Joiner / Laszlo L P Hosszu / M Howard Tattum / Silvia Panico / Daniel K Clare / John Collinge / Helen R Saibil / Jonathan D F Wadsworth /
PubMed AbstractMammalian prions are hypothesized to be fibrillar or amyloid forms of prion protein (PrP), but structures observed to date have not been definitively correlated with infectivity and the three- ...Mammalian prions are hypothesized to be fibrillar or amyloid forms of prion protein (PrP), but structures observed to date have not been definitively correlated with infectivity and the three-dimensional structure of infectious prions has remained obscure. Recently, we developed novel methods to obtain exceptionally pure preparations of prions from mouse brain and showed that pathogenic PrP in these high-titre preparations is assembled into rod-like assemblies. Here, we have used precise cell culture-based prion infectivity assays to define the physical relationship between the PrP rods and prion infectivity and have used electron tomography to define their architecture. We show that infectious PrP rods isolated from multiple prion strains have a common hierarchical assembly comprising twisted pairs of short fibres with repeating substructure. The architecture of the PrP rods provides a new structural basis for understanding prion infectivity and can explain the inability to systematically generate high-titre synthetic prions from recombinant PrP.
External linksOpen Biol / PubMed:27249641 / PubMed Central
MethodsEM (tomography)
Structure data

EMDB-4092:
Tomographic reconstruction of ex vivo mammalian prions
Method: EM (tomography)

Source
  • Mus musculus (house mouse)

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