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TitleHigh-resolution structure and strain comparison of infectious mammalian prions.
Journal, issue, pagesMol Cell, Vol. 81, Issue 21, Page 4540-44551.e6, Year 2021
Publish dateNov 4, 2021
AuthorsAllison Kraus / Forrest Hoyt / Cindi L Schwartz / Bryan Hansen / Efrosini Artikis / Andrew G Hughson / Gregory J Raymond / Brent Race / Gerald S Baron / Byron Caughey /
PubMed AbstractWithin the extensive range of self-propagating pathologic protein aggregates of mammals, prions are the most clearly infectious (e.g., ∼10 lethal doses per milligram). The structures of such lethal ...Within the extensive range of self-propagating pathologic protein aggregates of mammals, prions are the most clearly infectious (e.g., ∼10 lethal doses per milligram). The structures of such lethal assemblies of PrP molecules have been poorly understood. Here we report a near-atomic core structure of a brain-derived, fully infectious prion (263K strain). Cryo-electron microscopy showed amyloid fibrils assembled with parallel in-register intermolecular β sheets. Each monomer provides one rung of the ordered fibril core, with N-linked glycans and glycolipid anchors projecting outward. Thus, single monomers form the templating surface for incoming monomers at fibril ends, where prion growth occurs. Comparison to another prion strain (aRML) revealed major differences in fibril morphology but, like 263K, an asymmetric fibril cross-section without paired protofilaments. These findings provide structural insights into prion propagation, strains, species barriers, and membrane pathogenesis. This structure also helps frame considerations of factors influencing the relative transmissibility of other pathologic amyloids.
External linksMol Cell / PubMed:34433091
MethodsEM (single particle)
Resolution3.14 Å
Structure data

23459

7lna

EMDB-23459, PDB-7lna:
Infectious mammalian prion fibril (263K scrapie)
Method: EM (single particle) / Resolution: 3.14 Å

Source
  • mesocricetus auratus (golden hamster)
  • Golden hamster (golden hamster)
KeywordsPROTEIN FIBRIL / infectious mammalian prion / templating / glycosylated glycophophatidlyinositol-anchored amyloid / PIRIBS

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