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 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.
02 /Specification & Classification
Click any tag to browse matching papers- Organism
- Assay
- Research Focus
- Approach
Reproducibility ledger
Nobody has reported trying to reproduce this paper yet. Did you replicate an experiment or run the code? Your report saves the next lab a week.
Sign in to file a reproducibility report.
Related papers
- Familial prion disease-related mutation E196K displays a novel amyloid fibril structure revealed by cryo-EM
L.-Q. Wang, K. Zhao, … Y. Liang·bioRxiv·Feb 18, 2021
- Structural evolution of a yeast amyloid in vivo is shaped by chaperones
Z.P. Wang, Samantha L. Weetman, … Wenjuan Zhang·bioRxiv·Aug 11, 2026
- 2.7 A cryo-EM structure of ex vivo RML prion fibrils
S. W. Manka, W. Zhang, … J. D. F. Wadsworth·bioRxiv·Dec 13, 2021
- Structure of an infectious mammalian prion
A. Kraus, F. Hoyt, … B. Caughey·bioRxiv·Feb 14, 2021
- Cryo-EM structure of an amyloid fibril from systemic amyloidosis
F. Liberta, S. Loerch, … M. Schmidt·bioRxiv·Jun 29, 2018
- Full Atomistic Model Of Prion Structure And Conversion
G. Spagnolli, M. Rigoli, … J. R. Requena·bioRxiv·Dec 22, 2018