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