Cryo-EM structure of anchorless RML prion reveals variations in shared motifs between distinct strains

Forrest Hoyt, Heidi G. Standke, Efrosini Artikis, Cindi L. Schwartz, Bryan Hansen, Kunpeng Li, Andrew G. Hughson, Matteo Manca, Olivia R. Thomas, Gregory J. Raymond, Brent Race, Gerald S. Baron, Byron Caughey () and Allison Kraus ()
Additional contact information
Forrest Hoyt: National Institutes of Health
Heidi G. Standke: Case Western Reserve University School of Medicine
Efrosini Artikis: National Institutes of Health
Cindi L. Schwartz: National Institutes of Health
Bryan Hansen: National Institutes of Health
Kunpeng Li: Case Western Reserve University
Andrew G. Hughson: National Institutes of Health
Matteo Manca: Case Western Reserve University School of Medicine
Olivia R. Thomas: Case Western Reserve University School of Medicine
Gregory J. Raymond: National Institutes of Health
Brent Race: National Institutes of Health
Gerald S. Baron: National Institutes of Health
Byron Caughey: National Institutes of Health
Allison Kraus: Case Western Reserve University School of Medicine

Nature Communications, 2022, vol. 13, issue 1, 1-7

Abstract: Abstract Little is known about the structural basis of prion strains. Here we provide a high (3.0 Å) resolution cryo-electron microscopy-based structure of infectious brain-derived fibrils of the mouse anchorless RML scrapie strain which, like the recently determined hamster 263K strain, has a parallel in-register β-sheet-based core. Several structural motifs are shared between these ex vivo prion strains, including an amino-proximal steric zipper and three β-arches. However, detailed comparisons reveal variations in these shared structural topologies and other features. Unlike 263K and wildtype RML prions, the anchorless RML prions lack glycophosphatidylinositol anchors and are severely deficient in N-linked glycans. Nonetheless, the similarity of our anchorless RML structure to one reported for wildtype RML prion fibrils in an accompanying paper indicates that these post-translational modifications do not substantially alter the amyloid core conformation. This work demonstrates both common and divergent structural features of prion strains at the near-atomic level.

Date: 2022
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DOI: 10.1038/s41467-022-30458-6

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