Lichen Protease Degrades Prion Protein
Author Information
Author(s): Johnson Christopher J., Bennett James P., Biro Steven M., Duque-Velasquez Juan Camilo, Rodriguez Cynthia M., Bessen Richard A., Rocke Tonie E.
Primary Institution: Prion Research Laboratory, United States Geological Survey National Wildlife Health Center, Madison, Wisconsin, United States of America
Hypothesis
Can lichens degrade the disease-associated prion protein (PrPTSE)?
Conclusion
Lichen extracts can efficiently degrade PrPTSE, suggesting their potential role in inactivating prions in the environment.
Supporting Evidence
- Lichen extracts from three species were shown to reduce prion protein levels significantly.
- Degradation was mediated by a serine protease found in the lichen extracts.
- Intact lichen tissue also demonstrated the ability to degrade prion proteins in infected brain homogenates.
Takeaway
Lichens can break down harmful proteins that cause diseases in animals, which might help reduce these diseases in nature.
Methodology
The study involved testing lichen extracts on prion proteins in vitro and assessing their degradation through immunoblotting and protein misfolding cyclic amplification.
Limitations
The study was conducted in vitro, and further research is needed to assess the effectiveness of lichen extracts in natural environments.
Digital Object Identifier (DOI)
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