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Assessing Transmissible Spongiform Encephalopathy Species Barriers with an In Vitro Prion Protein Conversion Assay
Published on: March 10, 2015
PrP knock-out and PrP transgenic mice in prion research
1MRC Prion Unit, Department of Neurodegenerative Disease, Institute of Neurology, London, UK.
British Medical Bulletin
|October 3, 2003
Summary
Prions, the agents causing spongiform encephalopathies, are thought to be misfolded proteins. Animals lacking the prion protein (PrP) are resistant to these diseases, supporting the
Area of Science:
- Neuroscience
- Molecular Biology
- Biochemistry
Background:
- Spongiform encephalopathies, including BSE and CJD, are fatal neurodegenerative diseases.
- These diseases are caused by prions, infectious agents.
- The 'protein only' hypothesis suggests prions are misfolded forms of the host prion protein (PrP).
Purpose of the Study:
- To investigate the role of the prion protein (PrP) in spongiform encephalopathies.
- To provide evidence for the 'protein only' hypothesis of prion disease.
- To explore the physiological function of PrP using genetic approaches.
Main Methods:
- Biochemical and genetic analysis of prion protein (PrP).
- Generation and study of PrP knock-out mice.
- Experimental infection models for scrapie.
Main Results:
- Strong correlation established between prion agents and PrP.
- PrP knock-out mice demonstrated resistance to experimental scrapie.
- PrP knock-out mice failed to propagate prion infectivity.
Conclusions:
- The findings strongly support the 'protein only' hypothesis.
- PrP is essential for prion propagation and the development of spongiform encephalopathies.
- PrP knock-out mice are valuable tools for studying prion diseases and PrP function.
