2.7 Å cryo-EM structure of ex vivo RML prion fibrils

Szymon W. Manka, Wenjuan Zhang, Adam Wenborn, Jemma Betts, Susan Joiner, Helen R. Saibil (), John Collinge () and Jonathan D. F. Wadsworth ()
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Szymon W. Manka: University College London
Wenjuan Zhang: University College London
Adam Wenborn: University College London
Jemma Betts: University College London
Susan Joiner: University College London
Helen R. Saibil: University of London
John Collinge: University College London
Jonathan D. F. Wadsworth: University College London

Nature Communications, 2022, vol. 13, issue 1, 1-11

Abstract: Abstract Mammalian prions propagate as distinct strains and are composed of multichain assemblies of misfolded host-encoded prion protein (PrP). Here, we present a near-atomic resolution cryo-EM structure of PrP fibrils present in highly infectious prion rod preparations isolated from the brains of RML prion-infected mice. We found that prion rods comprise single-protofilament helical amyloid fibrils that coexist with twisted pairs of the same protofilaments. Each rung of the protofilament is formed by a single PrP monomer with the ordered core comprising PrP residues 94–225, which folds to create two asymmetric lobes with the N-linked glycans and the glycosylphosphatidylinositol anchor projecting from the C-terminal lobe. The overall architecture is comparable to that of recently reported PrP fibrils isolated from the brain of hamsters infected with the 263K prion strain. However, there are marked conformational variations that could result from differences in PrP sequence and/or represent distinguishing features of the distinct prion strains.

Date: 2022
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DOI: 10.1038/s41467-022-30457-7

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