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• W4285395722 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." @default.
• W4285395722 created "2022-07-14" @default.
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• W4285395722 date "2022-07-13" @default.
• W4285395722 modified "2023-10-18" @default.
• W4285395722 title "Cryo-EM structure of anchorless RML prion reveals variations in shared motifs between distinct strains" @default.
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• W4285395722 doi "https://doi.org/10.1038/s41467-022-30458-6" @default.
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