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Conformational conversion and prion disease

Nature Reviews Molecular Cell Biology volume 12, page 273 (2011)Cite this article

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Because of mechanistic similarities between prion propagation in mammals and fungi, Tuite and Serio recently proposed (The prion hypothesis: from biological anomaly to basic regulatory mechanism. Nature Rev. Mol. Cell Biol. 11, 823–833 (2010))1 that similarly to fungal prions, which are thought to act as phenotype regulators, prions in mammals should be considered as a basic regulatory mechanism instead of a biological anomaly. However, by considering the behaviour of prions, we argue that the fact that mammalian and fungal prions use a similar mechanism of conformational conversion is not enough to suggest that they are not just infectious agents.

Conformational conversion of a protein from an α-helix to a β-strand is usually associated with a major change in the tertiary structure, which may alter its physiological function and even be implicated in severe diseases. Prion diseases in mammals are one such example; they are caused by the conformational conversion of normal cellular prion protein (PrPC) into an abnormal isoform (PrPSc)2,3. Some fungal proteins can, like prions, also exist in a range of stable conformations and transition between these states under physiological conditions4; thus, this type of protein is known as a fungal prion.

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Acknowledgements

The authors' work is supported by the National Natural Science Foundation of China (grants 30700113 and 30800184).

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  1. Liang Shen and Hong-Fang Ji are at the Shandong Provincial Research Center for Bioinformatic Engineering and Technique, Shandong University of Technology, Zibo 255049, China.,

    Liang Shen & Hong-Fang Ji

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Correspondence to Hong-Fang Ji.

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Shen, L., Ji, HF. Conformational conversion and prion disease. Nat Rev Mol Cell Biol 12, 273 (2011). https://doi.org/10.1038/nrm3007-c1

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