Prions

Prions are an infectious protein usually referring to the protein in mammals called prion (PrP), but the term prions or scrapie protein can be generically applied to any protein that exhibits the same properties of taking on a misfolded conformation (PrPsc form) and templating and propagating further misfolding that leads to its infectivity.

Latest Research and Reviews

Research
31 January 2023 | Open Access

Food protein-derived amyloids do not accelerate amyloid β aggregation
- M. Mahafuzur Rahman
- , Rodrigo Sanches Pires
- & Christofer Lendel
Scientific Reports 13, 985
Research
09 January 2023 | Open Access

Prion protein amino acid sequence influences formation of authentic synthetic PrP^Sc
- Alyssa J. Block
- , Taylor C. York
- & Jason C. Bartz
Scientific Reports 13, 441
Research
12 October 2022 | Open Access

Structural analysis of the overoxidized Cu/Zn-superoxide dismutase in ROS-induced ALS filament formation

Characterization of the structure of an overoxidation-mimicking double mutant of superoxide dismutase SOD1 shows the production of more cytotoxic filaments seen in amyotrophic lateral sclerosis (ALS) neurons.
- Yeongjin Baek
- , Tae-Gyun Woo
- & Nam-Chul Ha
Communications Biology 5, 1085
Research
30 September 2022 | Open Access

Quaternary structure of patient-homogenate amplified α-synuclein fibrils modulates seeding of endogenous α-synuclein

Quaternary structure of α-synuclein fibrils characterized from human patients with Parkinson’s disease and Multiple System Atrophy modulates seeding in mouse primary oligodendroglial cultures.
- Benedikt Frieg
- , James A. Geraets
- & Gunnar F. Schröder
Communications Biology 5, 1040
Research
10 August 2022 | Open Access

A conformational switch controlling the toxicity of the prion protein

The H-latch is a well-defined structural change occurring in PrP^C bound to the neurotoxic antibody POM1, and its presence shows a positive correlation with neurotoxicity. Inhibition of the H-latch prolongs the lifespan of prion-diseased mice.
- Karl Frontzek
- , Marco Bardelli
- & Adriano Aguzzi
Nature Structural & Molecular Biology 29, 831-840
Research
05 August 2022 | Open Access

Disease-associated mutations within the yeast DNAJB6 homolog Sis1 slow conformer-specific substrate processing and can be corrected by the modulation of nucleotide exchange factors

Here the authors describe mechanisms through which analogous LGMDD1 (Limb-Girdle Muscular Dystrophy Type D1) mutations affect Sis1 (a yeast functional homolog of human DNAJB6) chaperone activity and poison the function of wild-type protein; potentially uncovering a new therapeutic route to explore.
- Ankan K. Bhadra
- , Michael J. Rau
- & Heather L. True
Nature Communications 13, 4570

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News and Comment

News & Views | 10 August 2022

Unlatching a window into the molecular landscape of prion toxicity

A study published in Nature Structural & Molecular Biology now unveils, at the atomic level, the initial mechanisms of prion toxicity, providing insights into the pathogenic mechanisms of a protein neurodegenerative disease caused by protein misfolding.
- Jesús R. Requena
Nature Structural & Molecular Biology 29, 733-735
Comments & Opinion
13 July 2022 | Open Access

The shape of things to come: structural insights into how prion proteins encipher heritable information

The prion hypothesis embodies the radical concept that prion proteins contain the necessary information for infectious replication within their shape, thus obviating the requirement for genomic material. Two elegant papers by Hoyt et al. and Manka et al. describing high-resolution structures of infectious prions bring us closer to answering the long-standing question of how different prion conformations produce heritably distinct diseases.
- Glenn C. Telling
Nature Communications 13, 4003
News & Views | 02 March 2020

Prion protein — mediator of toxicity in multiple proteinopathies

A new study shows that interactions of the cellular prion protein with amyloid-β, tau and α-synuclein oligomers are important in mediating the toxicity of these proteins in Alzheimer disease and Parkinson disease. The findings suggest a shared pathway that could be a therapeutic target common to multiple neurodegenerative diseases.
- Jacob I. Ayers
- & Stanley B. Prusiner
Nature Reviews Neurology 16, 187-188
Research Highlights | 04 September 2019

Does prion protein help amyloid-β accelerate spread of tau pathology?
- Sarah Lemprière
Nature Reviews Neurology 15, 558
Research Highlights | 23 January 2018

Reversible sequestration over irreversible aggregation

In stress conditions the intrinsically disordered region of the prion and translation factor Sup35 promotes reversible protein phase separation instead of the more stable fibrillar aggregation.
- Eytan Zlotorynski
Nature Reviews Molecular Cell Biology 19, 73
Research Highlights | 01 December 2017

A yTRAP for protein aggregates

Nature Methods 14, 1130

All News & Comment

Prions

Latest Research and Reviews

Food protein-derived amyloids do not accelerate amyloid β aggregation

Prion protein amino acid sequence influences formation of authentic synthetic PrP^Sc

Structural analysis of the overoxidized Cu/Zn-superoxide dismutase in ROS-induced ALS filament formation

Quaternary structure of patient-homogenate amplified α-synuclein fibrils modulates seeding of endogenous α-synuclein

A conformational switch controlling the toxicity of the prion protein

Disease-associated mutations within the yeast DNAJB6 homolog Sis1 slow conformer-specific substrate processing and can be corrected by the modulation of nucleotide exchange factors

News and Comment

Unlatching a window into the molecular landscape of prion toxicity

The shape of things to come: structural insights into how prion proteins encipher heritable information

Prion protein — mediator of toxicity in multiple proteinopathies

Does prion protein help amyloid-β accelerate spread of tau pathology?

Reversible sequestration over irreversible aggregation

A yTRAP for protein aggregates

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