The Structure of Human Prions: From Biology to Structural Models — Considerations and Pitfalls

Viruses

Claudia Y. Acevedo-Morantes²  Holger Wille¹ 

[1]Department of Biochemistry and Centre for Prions and Protein Folding Diseases, University of Alberta, Edmonton, AB T6G 2M8, Canada

[2] E-Mail

关键词: prion;    cellular prion protein;    PrP^C;    misfolded prion protein;    PrP^Sc;    PRNP;    amyloid;    α-helices;    β-sheets;   

DOI  :  10.3390/v6103875

来源: mdpi

【 摘 要 】

Prion diseases are a family of transmissible, progressive, and uniformly fatal neurodegenerative disorders that affect humans and animals. Although cross-species transmissions of prions are usually limited by an apparent “species barrier”, the spread of a prion disease to humans by ingestion of contaminated food, or via other routes of exposure, indicates that animal prions can pose a significant public health risk. The infectious agent responsible for the transmission of prion diseases is a misfolded conformer of the prion protein, PrP^Sc, a pathogenic isoform of the host-encoded, cellular prion protein, PrP^C. The detailed mechanisms of prion conversion and replication, as well as the high-resolution structure of PrP^Sc, are unknown. This review will discuss the general background related to prion biology and assess the structural models proposed to date, while highlighting the experimental challenges of elucidating the structure of PrP^Sc.

【 授权许可】

CC BY   
© 2014 by the authors; licensee MDPI, Basel, Switzerland.