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Transmissible spongiform encephalopathies, amyloidoses and yeast prions: Common threads?

Nature Medicine volume 6, pages 751–754 (2000)Cite this article

Abstract

Mammalian transmissible spongiform encephalopathy (prion) and amyloid diseases seem to involve the self-propagation of abnormal fibrillar or sub-fibrillar protein aggregates. Similar processes explain protein-mediated inheritance by yeast prions. Indeed, yeast prions are more surely mediated solely by aberrant protein aggregates than are their mammalian namesakes. Tantalizing parallels make yeast prions attractive models of mammalian protein-folding diseases.

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Figure 1: Electron micrographs of amyloid-like fibrils of PrP-res, ure2p and sup35p.
Figure 2: Seeded (nucleated) polymerization models for prion or amyloid formation.
Figure 3: Domain structures of PrP, ure2p and sup35p.

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Acknowledgements

I thank W. Caughey, K. Hasenkrug and S. Priola for critically reading this manuscript and S.F. Hayes for assistance in obtaining the electron graph of PrP-res in Fig. 1.

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  1. Laboratory of Persistent Viral Diseases National Institute for Allergy and Infectious Diseases National Institutes of Health, Rocky Mountain Laboratories, 903 S. 4th St., Hamilton , 59840, Montana, USA

    Byron Caughey

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Caughey, B. Transmissible spongiform encephalopathies, amyloidoses and yeast prions: Common threads?. Nat Med 6, 751–754 (2000). https://doi.org/10.1038/77476

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