Trouble Unfolds

Prions are like a single misshapen piece of paper in a printing press that causes every subsequent sheet in the print run to crumple too. They are misfolded proteins that act like an infection, causing other proteins to change shape and can lead to fatal brain disorders such as Creutzfeldt-Jakob disease. The crucial first steps in the process that causes neurodegeneration are not clear, so researchers conducted a broad search for factors involved in prions’ toxicity at synapses – the joints between neurons (brain cells). They identified some linchpins of prion synapse disruption: inhibitors of three protein-altering enzymes (protein kinases, including protein kinase C, pictured accumulating in a mouse neuron 30 minutes after exposure to prions and illustrating a crucial window before damage begins). Potential treatments might target these early stages of interaction between prions and synapses, and block the toxic pathway before damage occurs.

Written by Anthony Lewis

Anthony Lewis

Writer

Ant was the web editor in the early days of BPoD, and has since worked with the UK’s top science organisations as a writer and multimedia producer. He now splits his time between freelance work and managing multimedia at The Lancet.

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• Image from work by Nhat T. T. Le and colleagues
• Department of Biochemistry and Cell Biology, Boston University Chobanian and Avedisian School of Medicine, Boston, MA, USA
• Image originally published with a Creative Commons Attribution 4.0 International (CC BY 4.0)
• Published in PLOS Pathogens, June 2026