The physical dimensions of amyloid aggregates control their infective potential as prion particles

Marchante, Ricardo, Beal, David M, Koloteva-Levine, Nadejda, Purton, Tracey J, Tuite, Mick F, Xue, Wei-Feng (2017) The physical dimensions of amyloid aggregates control their infective potential as prion particles. eLife, 6 . e27109. ISSN 2050-084X. (doi:10.7554/eLife.27109.001)

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Abstract

Transmissible amyloid particles called prions are associated with infectious prion diseases in mammals and inherited phenotypes in yeast. All amyloid aggregates can give rise to potentially infectious seeds that accelerate their growth. Why some amyloid seeds are highly infectious prion particles while others are less infectious or even inert, is currently not understood. To address this question, we analyzed the suprastructure and dimensions of synthetic amyloid fibrils assembled from the yeast (Saccharomyces cerevisiae) prion protein Sup35NM. We then quantified the ability of these particles to induce the [PSI(+)] prion phenotype in cells. Our results show a striking relationship between the length distribution of the amyloid fibrils and their ability to induce the heritable [PSI(+)] prion phenotype. Using a simple particle size threshold model to describe transfection activity, we explain how dimensions of amyloid fibrils are able to modulate their infectious potential as prions.

Item Type: Article
DOI/Identification number: 10.7554/eLife.27109.001
Subjects: Q Science
Q Science > QP Physiology (Living systems) > QP517 Biochemistry
Divisions: Faculties > Sciences > School of Biosciences
Depositing User: Wei-Feng Xue
Date Deposited: 11 Sep 2017 13:52 UTC
Last Modified: 29 May 2019 19:31 UTC
Resource URI: https://kar.kent.ac.uk/id/eprint/63367 (The current URI for this page, for reference purposes)
Marchante, Ricardo: https://orcid.org/0000-0003-3153-6329
Tuite, Mick F: https://orcid.org/0000-0002-5214-540X
Xue, Wei-Feng: https://orcid.org/0000-0002-6504-0404
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