ArticleThe Journal of biological chemistry2013
Heterogeneous seeding of a prion structure by a generic amyloid form of the fungal prion-forming domain HET-s(218-289).
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- Cryo-Electron Tomography of Reconstituted Biomolecular Condensates.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Insights into protein misfolding and aggregation enabled by solid-state NMR spectroscopy.Solid state nuclear magnetic resonance · 2017Review
- A 31-residue peptide induces aggregation of tau's microtubule-binding region in cells.Nature chemistry · 2017Article
- Structural Biology of PrP Prions.Cold Spring Harbor perspectives in medicine · 2017Review
- Protein folding, misfolding and aggregation: The importance of two-electron stabilizing interactions.PloS one · 2017Article
- New Molecular Insight into Mechanism of Evolution of Mammalian Synthetic Prions.The American journal of pathology · 2016Article
- Two alternative pathways for generating transmissible prion disease de novo.Acta neuropathologica communications · 2015Article
- Structural studies of truncated forms of the prion protein PrP.Biophysical journal · 2015Article
- Truncated forms of the prion protein PrP demonstrate the need for complexity in prion structure.Prion · 2015Article
- Contribution of specific residues of the β-solenoid fold to HET-s prion function, amyloid structure and stability.PLoS pathogens · 2014Article
- Fiber diffraction of the prion-forming domain HET-s(218-289) shows dehydration-induced deformation of a complex amyloid structure.Biochemistry · 2014Article
- Fungal prion HET-s as a model for structural complexity and self-propagation in prions.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
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6 authors.
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Abstract
The fungal prion-forming domain HET-s(218-289) forms infectious amyloid fibrils at physiological pH that were shown by solid-state NMR to be assemblies of a two-rung β-solenoid structure. Under acidic conditions, HET-s(218-289) has been shown to form amyloid fibrils that have very low infectivity in vivo, but structural information about these fibrils has been very limited. We show by x-ray fiber diffraction that the HET-s(218-289) fibrils formed under acidic conditions have a stacked β-sheet architecture commonly found in short amyloidogenic peptides and denatured protein aggregates. At physiological pH, stacked β-sheet fibrils nucleate the formation of the infectious β-solenoid prions in a process of heterogeneous seeding, but do so with kinetic profiles distinct from those of spontaneous or homogeneous (seeded with infectious β-solenoid fibrils) fibrillization. Several serial passages of stacked β-sheet-seeded solutions lead to fibrillization kinetics similar to homogeneously seeded solutions. Our results directly show that structural mutation can occur between substantially different amyloid architectures, lending credence to the suggestion that the processes of strain adaptation and crossing species barriers are facilitated by structural mutation.
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