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Updated: Jul 9, 2026

Investigating the Spreading and Toxicity of Prion-like Proteins Using the Metazoan Model Organism C. elegans
Published on: January 8, 2015
A bacterial pore-forming toxin forms aggregates in cells that resemble those associated with neurodegenerative
Julie P M Viala1, Sofia N Mochegova, Nicole Meyer-Morse
1Department of Molecular and Cell Biology, University of California, Berkeley, CA, USA.
Abstract:
Listeria monocytogenes is a bacterial, facultative intracellular pathogen, which secretes a pore-forming toxin called listeriolysin O (LLO). LLO mediates the dissolution of the phagosomal membrane allowing L. monocytogenes to reach and grow in the host cytosolic compartment. In this study we report the localization of LLO secreted in infected cells. We described that LLO (i) forms small perinuclear aggregates, (ii) accumulates in large autophagosome-like structures and (iii) sequesters to large protein aggregates. The formation of protein aggregates required full LLO activity. Further characterization of protein aggregates indicated that they not only contained the active form of LLO but also polyubiquitinated proteins and p62, which are both common components of protein aggregates found in neurological diseases. Hence, a protein of bacterial origin could potentially follow the same fate as a toxic protein associated with neurodegenerative disease.
Insights
Listeria monocytogenes secretes listeriolysin O (LLO), a toxin that helps bacteria invade cells. This study found LLO can form aggregates similar to those seen in neurodegenerative diseases.
Area of Science:
- Microbiology
- Cell Biology
- Neuroscience
Background:
- Listeria monocytogenes is a facultative intracellular bacterium.
- Listeriolysin O (LLO) is a pore-forming toxin secreted by L. monocytogenes.
- LLO facilitates bacterial escape into the host cell cytoplasm by disrupting the phagosomal membrane.
Purpose of the Study:
- To investigate the intracellular localization of secreted LLO in infected host cells.
- To characterize the nature and formation of LLO-containing structures within host cells.
Main Methods:
- Immunofluorescence microscopy to visualize LLO localization.
- Analysis of LLO aggregation and its dependence on LLO activity.
- Biochemical characterization of protein aggregates containing LLO.
Main Results:
- Secreted LLO was found to localize in distinct cellular compartments.
- LLO forms perinuclear aggregates and accumulates in autophagosome-like structures.
- Active LLO sequesters into large protein aggregates, also containing polyubiquitinated proteins and p62.
Conclusions:
- Bacterial protein LLO can form aggregates within host cells.
- These aggregates share characteristics with protein aggregates associated with neurodegenerative diseases.
- This suggests a potential link between bacterial infection and host cellular protein aggregation pathways.
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