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Unlatching a window into the molecular landscape of prion toxicity

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A study published in Nature Structural & Molecular Biology now unveils, at the atomic level, the initial mechanisms of prion toxicity, providing insights into the pathogenic mechanisms of a protein neurodegenerative disease caused by protein misfolding.

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Fig. 1: Binding of the prion mimic POM1 induces an H-latch in PrPC as the first event in the toxicity cascade.
Fig. 2: A latch-blunt antibody is not only innocuous to COCS cells, but protects the culture from prion-induced toxicity.

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Acknowledgements

J.R.R. is supported by the Spanish Ministry of Science and Innovation (grant PID2020-117465GB-I00, partially funded by EU funds).

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Correspondence to Jesús R. Requena.

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Requena, J.R. Unlatching a window into the molecular landscape of prion toxicity. Nat Struct Mol Biol 29, 733–735 (2022). https://doi.org/10.1038/s41594-022-00817-4

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