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Updated: Oct 12, 2025

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

Prion protein complexed to a DNA aptamer induce behavioral and synapse dysfunction in mice.

Mariana P B Gomes¹, Emanuelle V de Lima², Fernanda G Q Barros-Aragão³

¹Faculty of Pharmacy, Federal University of Rio de Janeiro, RJ 21941-902, Brazil; Instituto de Tecnologia em Imunobiológicos, Bio-Manguinhos, FIOCRUZ, Rio de Janeiro 21040-900, Brazil.

Behavioural Brain Research

|November 25, 2021

Summary

Prion protein (PrP) aggregates, induced by DNA aptamer D67, caused cognitive impairment and synapse loss in mice. Glial cell activation in the hippocampus suggests a role in prion disease progression.

Keywords:

Behavior Memory Neurotoxicity Nucleic acid Prion protein Protein aggregation Protein-DNA interaction Scrapie Synapse

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Monitoring Cell-to-cell Transmission of Prion-like Protein Aggregates in Drosophila Melanogaster

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Area of Science:

Neuroscience
Biochemistry
Molecular Biology

Background:

Transmissible spongiform encephalopathies (TSEs) are fatal neurodegenerative diseases caused by prion protein (PrP) conversion.
In vitro studies show nucleic acids can induce PrP aggregation, but in vivo effects remain largely unexplored.

Purpose of the Study:

To investigate the in vivo effects of PrP aggregates formed with the D67 DNA aptamer.
To establish a mouse model for studying prion-induced neurotoxicity and cognitive dysfunction.

Main Methods:

Recombinant PrP (rPrP) was aggregated with the D67 aptamer.
Aggregates were injected into the lateral ventricle of Swiss mice.
Behavioral, cognitive, and histological analyses were performed.

Main Results:

rPrP:D67 aggregates did not affect emotional or motor behavior.
Mice developed cognitive impairment and hippocampal synapse loss.
Intense glial cell activation was observed in the hippocampus.

Conclusions:

In vivo administration of rPrP:D67 aggregates provides a model for studying PrP neurotoxicity.
Glial cell activation is implicated in the cognitive deficits associated with prion diseases.