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Related Experiment Video

Updated: Jun 27, 2026

Investigating the Spreading and Toxicity of Prion-like Proteins Using the Metazoan Model Organism C. elegans

Investigating the Spreading and Toxicity of Prion-like Proteins Using the Metazoan Model Organism C. elegans

Published on: January 8, 2015

Aggregated, wild-type prion protein causes neurological dysfunction and synaptic abnormalities.

Roberto Chiesa¹, Pedro Piccardo, Emiliano Biasini

¹Department of Neuroscience, Dulbecco Telethon Institute, Istituto di Ricerche Farmacologiche Mario Negri, Milan, Italy.

The Journal of Neuroscience : the Official Journal of the Society for Neuroscience

|December 5, 2008

Summary

Noninfectious prion protein (PrP) aggregates cause neurodegeneration, particularly damaging synapses. This study in transgenic mice reveals PrP

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Last Updated: Jun 27, 2026

Investigating the Spreading and Toxicity of Prion-like Proteins Using the Metazoan Model Organism C. elegans

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Isolation of Soluble and Insoluble PrP Oligomers in the Normal Human Brain

Isolation of Soluble and Insoluble PrP Oligomers in the Normal Human Brain

Published on: October 3, 2012

Area of Science:

Neuroscience
Molecular Biology
Protein Chemistry

Background:

The exact neurotoxic forms of prion protein (PrP) causing neurodegeneration in prion diseases are not fully identified.
Noninfectious PrP oligomers are strongly implicated in the disease's pathogenic process.

Purpose of the Study:

To investigate the neurotoxic potential of noninfectious, aggregated wild-type prion protein (PrP).
To characterize the pathological changes in transgenic mice overexpressing wild-type PrP.

Main Methods:

Generation of Tg(WT) transgenic mice overexpressing wild-type PrP at approximately 5-fold or 10-fold levels.
Clinical and pathological assessment of neurodegeneration, PrP deposition, and synaptic integrity.
Biochemical analysis of PrP aggregation, solubility, and protease resistance.

Main Results:

Homozygous Tg(WT) mice developed spontaneous neurodegenerative disease with tremor and paresis.
Both hemizygous and homozygous Tg(WT) mice exhibited punctate PrP deposits and enlarged synaptic terminals with membranous structure proliferation.
Overexpressed PrP formed insoluble, mildly protease-resistant aggregates that were noninfectious.

Conclusions:

Noninfectious aggregates of wild-type PrP are demonstrably neurotoxic, with a particular impact on synapses.
These findings suggest shared pathogenic mechanisms between prion diseases and other protein-misfolding neurodegenerative disorders.