Cryo-EM structure of disease-related prion fibrils provides insights into seeding barriers

Li, Q.; Jaroniec, C. P.; Surewicz, W. K.

doi:10.1101/2021.08.10.455830

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bioRxiv · 10.1101/2021.08.10.455830

Cryo-EM structure of disease-related prion fibrils provides insights into seeding barriers

Li, Q.·Jaroniec, C. P.·Surewicz, W. K.

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Abstract

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 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.

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Li, Q., Jaroniec, C. P., Surewicz, W. K.. 2021-08-11. Cryo-EM structure of disease-related prion fibrils provides insights into seeding barriers. https://doi.org/10.1101/2021.08.10.455830

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