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Updated: Nov 28, 2025
Interactions with and Membrane Permeabilization of Brain Mitochondria by Amyloid Fibrils
Published on: September 28, 2019
Mechanisms and therapeutic potential of interactions between human amyloids and viruses
Emiel Michiels1,2, Frederic Rousseau3,4, Joost Schymkowitz5,6
1VIB Center for Brain and Disease Research, Leuven, Belgium.
Abstract:
The aggregation of specific proteins and their amyloid deposition in affected tissue in disease has been studied for decades assuming a sole pathogenic role of amyloids. It is now clear that amyloids can also encode important cellular functions, one of which involves the interaction potential of amyloids with microbial pathogens, including viruses. Human expressed amyloids have been shown to act both as innate restriction molecules against viruses as well as promoting agents for viral infectivity. The underlying molecular driving forces of such amyloid-virus interactions are not completely understood. Starting from the well-described molecular mechanisms underlying amyloid formation, we here summarize three non-mutually exclusive hypotheses that have been proposed to drive amyloid-virus interactions. Viruses can indirectly drive amyloid depositions by affecting upstream molecular pathways or induce amyloid formation by a direct interaction with the viral surface or specific viral proteins. Finally, we highlight the potential of therapeutic interventions using the sequence specificity of amyloid interactions to drive viral interference.
Insights
Amyloids, once viewed as disease-causing, can interact with viruses. These interactions can restrict or promote viral infections, with potential for new antiviral therapies.
Area of Science:
- Biochemistry
- Molecular Biology
- Virology
Background:
- Amyloid proteins are traditionally studied for their pathogenic role in diseases.
- Emerging evidence reveals amyloids possess crucial cellular functions, including interactions with pathogens.
- Human amyloids exhibit dual roles in viral interactions, acting as restriction factors or infectivity enhancers.
Purpose of the Study:
- To explore the molecular mechanisms driving amyloid-virus interactions.
- To summarize proposed hypotheses explaining how viruses and amyloids interact.
- To highlight therapeutic potential in targeting these interactions.
Main Methods:
- Review and synthesis of existing literature on amyloid formation and viral interactions.
- Analysis of proposed hypotheses for amyloid-virus interplay.
- Discussion of therapeutic strategies based on amyloid-virus specificities.
Main Results:
- Amyloids can directly or indirectly influence viral infection processes.
- Three non-mutually exclusive hypotheses explain amyloid-virus interactions.
- Viruses may induce amyloid formation or be affected by existing amyloid structures.
Conclusions:
- Amyloid-virus interactions are complex and multifaceted.
- Understanding these interactions is key to developing novel antiviral strategies.
- Targeting sequence-specific amyloid-virus interactions offers therapeutic promise for viral interference.
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