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Cryo-EM structure of a human prion fibril with a hydrophobic, protease-resistant core
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Cryo-EM structure of a human prion fibril with a hydrophobic, protease-resistant core
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Journal Article
Cryo-EM structure of a human prion fibril with a hydrophobic, protease-resistant core
2020
Overview
Self-templating assemblies of the human prion protein are clinically associated with transmissible spongiform encephalopathies. Here we present the cryo-EM structure of a denaturant- and protease-resistant fibril formed in vitro spontaneously by a 9.7-kDa unglycosylated fragment of the human prion protein. This human prion fibril contains two protofilaments intertwined with screw symmetry and linked by a tightly packed hydrophobic interface. Each protofilament consists of an extended beta arch formed by residues 106 to 145 of the prion protein, a hydrophobic and highly fibrillogenic disease-associated segment. Such structures of prion polymorphs serve as blueprints on which to evaluate the potential impact of sequence variants on prion disease.A cryo-EM structure of a stable, protease-resistant fibril formed by a fragment of the human prion protein shows two intertwined protofilaments with a tightly packed hydrophobic interface.
Publisher
Nature Publishing Group
