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Cryo-EM structure of disease-related prion fibrils provides insights into seeding barriers
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Cryo-EM structure of disease-related prion fibrils provides insights into seeding barriers
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Journal Article
Cryo-EM structure of disease-related prion fibrils provides insights into seeding barriers
2022
Overview
One of the least understood aspects of prion diseases is the structure of infectious prion protein aggregates. Here we report a high-resolution cryo-EM structure of amyloid fibrils formed by human prion protein with the Y145Stop mutation that is associated with a familial prion disease. This structural insight allows us not only to explain previous biochemical findings, but also provides direct support for the conformational adaptability model of prion transmissibility barriers.
A cryo-EM structure of disease-related human Y145Stop prion protein amyloid fibrils explains species-dependent seeding barriers in prion protein amyloid propagation.
