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Updated: Mar 23, 2026
Investigating the Spreading and Toxicity of Prion-like Proteins Using the Metazoan Model Organism C. elegans
Published on: January 8, 2015
Transmissible amyloid
L O Tjernberg1, A Rising1,2, J Johansson1,2
1Department of Neurobiology Care Sciences and Society, Division of Neurogeriatrics, Center for Alzheimer Research, Karolinska Institutet, Huddinge, Sweden.
Abstract:
There are around 30 human diseases associated with protein misfolding and amyloid formation, each one caused by a certain protein or peptide. Many of these diseases are lethal and together they pose an enormous burden to society. The prion protein has attracted particular interest as being shown to be the pathogenic agent in transmissible diseases such as kuru, Creutzfeldt-Jakob disease and bovine spongiform encephalopathy. Whether similar transmission could occur also in other amyloidoses such as Alzheimer's disease, Parkinson's disease and serum amyloid A amyloidosis is a matter of intense research and debate. Furthermore, it has been suggested that novel biomaterials such as artificial spider silk are potentially amyloidogenic. Here, we provide a brief introduction to amyloid, prions and other proteins involved in amyloid disease and review recent evidence for their potential transmission. We discuss the similarities and differences between amyloid and silk, as well as the potential hazards associated with protein-based biomaterials.
Insights
Protein misfolding causes about 30 lethal human diseases. Research investigates if diseases like Alzheimer's and Parkinson's, and biomaterials like artificial spider silk, could be transmissible like prion diseases.
Area of Science:
- Biochemistry
- Neuroscience
- Materials Science
Background:
- Approximately 30 human diseases are linked to protein misfolding and amyloid formation, posing significant societal and health burdens.
- Prion proteins are established pathogenic agents in transmissible diseases like Creutzfeldt-Jakob disease and bovine spongiform encephalopathy.
- Emerging research explores the potential transmissibility of other amyloid diseases and the amyloidogenic nature of novel biomaterials.
Purpose of the Study:
- To introduce amyloid, prions, and related proteins involved in amyloid diseases.
- To review current evidence regarding the potential transmission of amyloid diseases.
- To discuss the implications of protein-based biomaterials, such as artificial spider silk, in the context of amyloidosis.
Main Methods:
- Literature review of scientific articles on protein misfolding diseases.
- Analysis of research on prion protein and transmissible spongiform encephalopathies.
- Comparative study of amyloid structures and artificial silk properties.
Main Results:
- Established role of prions in transmissible neurodegenerative diseases.
- Ongoing debate and research into the potential transmissibility of Alzheimer's, Parkinson's, and other amyloidoses.
- Identification of potential amyloidogenic properties in novel biomaterials like artificial spider silk.
Conclusions:
- Protein misfolding diseases represent a significant health challenge with potential for transmission.
- Further research is crucial to understand the risks associated with protein-based biomaterials and their potential to form amyloids.
- Distinguishing between amyloid structures and their disease-causing potential is vital for both medicine and biomaterial development.
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