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Updated: Jun 26, 2026

Investigating the Spreading and Toxicity of Prion-like Proteins Using the Metazoan Model Organism C. elegans
Published on: January 8, 2015
Prion protein misfolding and disease
Roger A Moore1, Lara M Taubner, Suzette A Priola
1Rocky Mountain Laboratories, Laboratory of Persistent Viral Diseases, NIAID, NIH, 903 S. 4th Street, Hamilton, MT 59840, United States. rmoore@niaid.nih.gov
Abstract:
Transmissible spongiform encephalopathies (TSEs or prion diseases) are a rare group of invariably fatal neurodegenerative disorders that affect humans and other mammals. TSEs are protein misfolding diseases that involve the accumulation of an abnormally aggregated form of the normal host prion protein (PrP). They are unique among protein misfolding disorders in that they are transmissible and have different strains of infectious agents that are associated with unique phenotypes in vivo. A wealth of biological and biophysical evidence now suggests that the molecular basis for prion diseases may be encoded by protein conformation. The purpose of this review is to provide an overview of the existing structural information for PrP within the context of what is known about the biology of prion disease.
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