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Prion propagation, toxicity and degradation

Nature Neuroscience volume 15, pages 936–939 (2012)Cite this article

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Abstract

Prion science has been on a rollercoaster for two decades. In the mid 1990s, the specter of mad cow disease (bovine spongiform encephalopathy, BSE) provoked an unprecedented public scare that was first precipitated by the realization that this animal prion disease could be transmitted to humans and then rekindled by the evidence that BSE-infected humans could pass on the infection through blood transfusions. Along with the gradual disappearance of BSE, the interest in prions has waned with the general public, funding agencies and prospective PhD students. In the past few years, however, a bewildering variety of diseases have been found to share features with prion infections, including cell-to-cell transmission. Here we review these developments and summarize those open questions that we currently deem most interesting in prion biology: how do prions damage their hosts, and how do hosts attempt to neutralize invading prions?

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Figure 1: Prion kinetics.
Figure 2: PrP-mediated amyloid toxicity.

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Acknowledgements

A.A. is the recipient of an Advanced Grant of the European Research Council and is supported by grants from the European Union (PRIORITY, LUPAS), the Swiss National Foundation, the National Competence Center on Neural Plasticity and Repair, the Stammbach Foundation, and the Novartis Research Foundation. J.F. is supported by a grant from the Swiss Center of Transgenic Expertise and by a career development award of the University of Zürich.

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  1. Institute of Neuropathology, University Hospital Zürich, Zürich, Switzerland

    Adriano Aguzzi & Jeppe Falsig

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  1. Adriano Aguzzi
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The concepts discussed here were developed by A.A. and discussed with J.F. A.A. and J.F. both wrote the manuscript.

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Correspondence to Adriano Aguzzi.

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Aguzzi, A., Falsig, J. Prion propagation, toxicity and degradation. Nat Neurosci 15, 936–939 (2012). https://doi.org/10.1038/nn.3120

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