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

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 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.

SUBMITTER: Li Q

PROVIDER: S-EPMC9639217 | biostudies-literature | 2022 Oct

REPOSITORIES: biostudies-literature

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

Li Qiuye Q Jaroniec Christopher P CP Surewicz Witold K WK

Nature structural & molecular biology 20220912 10

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. ...[more]

PMID: 36097290

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