Direct Observation of Competing Prion Protein Fibril Populations with Distinct Structures and Kinetics Article Swipe
Yuanzi Sun
,
Kezia Jack
,
Tiziana Ercolani
,
Daljit Sangar
,
Laszlo L. P. Hosszu
,
John Collinge
,
Jan Bieschke
·
YOU?
·
· 2022
· Open Access
·
· DOI: https://doi.org/10.1101/2022.08.10.503301
YOU?
·
· 2022
· Open Access
·
· DOI: https://doi.org/10.1101/2022.08.10.503301
Summary In prion diseases, fibrillar assemblies of misfolded prion protein (PrP) self-propagate by incorporating PrP monomers. Using total internal reflection and transient amyloid binding super-resolution microscopy, our study analyses elongation of single PrP fibrils to reveal polymorphic populations, featuring structural and dynamic heterogeneity similar to prion strains, which were previously hidden in ensemble measurements. PrP fibrils elongated along a preferred direction by an intermittent ‘stop- and-go’ mechanism. Fibrils fell into three main populations, which each displayed distinct elongation mechanisms incorporating different monomer structures and which maintained their properties even under elongation conditions favouring a different fibril type. Elongation of RML and ME7 prion rods likewise exhibited unique kinetic features. The discovery of polymorphic fibril populations of amyloid and prions growing in competition suggests that prions may present as quasispecies of structural isomorphs and that the replication environment may tilt the balance between prion isomorphs and amyloid species. Highlights Synthetic prion fibril populations contain structurally distinct fibril types Fibril types faithfully elongate by different mechanisms Fibril types compete for substrate depending on environment Fibril populations model quasi-species behavior of prion strains eTOC Replication of different prion strains causes distinct disease phenotypes. Sun et al. analyzed the growth of individual synthetic prion protein fibrils by super-resolution microscopy and found populations of structurally distinct fibril types, which grew in competition to each other as a quasi-species, recapitulating basic prion strain characteristics in vitro .
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- Type
- preprint
- Language
- en
- Landing Page
- https://doi.org/10.1101/2022.08.10.503301
- https://www.biorxiv.org/content/biorxiv/early/2022/08/13/2022.08.10.503301.full.pdf
- OA Status
- green
- References
- 52
- Related Works
- 10
- OpenAlex ID
- https://openalex.org/W4291287665
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- OpenAlex ID
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https://openalex.org/W4291287665Canonical identifier for this work in OpenAlex
- DOI
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https://doi.org/10.1101/2022.08.10.503301Digital Object Identifier
- Title
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Direct Observation of Competing Prion Protein Fibril Populations with Distinct Structures and KineticsWork title
- Type
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preprintOpenAlex work type
- Language
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enPrimary language
- Publication year
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2022Year of publication
- Publication date
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2022-08-13Full publication date if available
- Authors
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Yuanzi Sun, Kezia Jack, Tiziana Ercolani, Daljit Sangar, Laszlo L. P. Hosszu, John Collinge, Jan BieschkeList of authors in order
- Landing page
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https://doi.org/10.1101/2022.08.10.503301Publisher landing page
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https://www.biorxiv.org/content/biorxiv/early/2022/08/13/2022.08.10.503301.full.pdfDirect link to full text PDF
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YesWhether a free full text is available
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greenOpen access status per OpenAlex
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https://www.biorxiv.org/content/biorxiv/early/2022/08/13/2022.08.10.503301.full.pdfDirect OA link when available
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Fibril, Biophysics, Amyloid (mycology), Elongation, Chemistry, Protein folding, Biology, Cell biology, Materials science, Inorganic chemistry, Ultimate tensile strength, MetallurgyTop concepts (fields/topics) attached by OpenAlex
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10Other works algorithmically related by OpenAlex
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