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Nature 447, 541-542 (31 May 2007) | doi:10.1038/447541b; Published online 30 May 2007
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Protein science: Discriminating taste of prions
Witold K. Surewicz1
Abstract
Prions are infectious proteins that are involved in brain-wasting disorders such as mad cow disease. In yeast, specific sequences of amino acids in prions seem to mediate prion propagation and cross-species transmissibility.
Few diseases have generated as much interest and controversy in recent years as transmissible spongiform encephalopathies (TSEs) — a group of fatal neurodegenerative disorders that includes Creutzfeldt–Jakob disease in humans and 'mad cow' disease1, 2. The protein-only hypothesis of TSE propagation postulates that the infectious pathogen, called a prion, is devoid of the nucleic acids that comprise genes, and is an abnormally shaped version of the normal prion protein, a naturally occurring molecule of unknown function.
- Witold K. Surewicz is in the Department of Physiology and Biophysics, Case Western Reserve University, Cleveland, Ohio 44106, USA.
Email: witold.surewicz@case.edu
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