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Prions propagate by transmitting a misfolded protein state. If a prion enters a healthy organism, it induces existing, properly folded proteins to convert into the disease-associated, prion form; the prion acts as a template to guide the misfolding of more proteins into prion form. These newly formed prions can then go on to convert more proteins themselves; this triggers a chain reaction that produces large amounts of the prion form. All known prions induce the formation of an amyloid fold, in which the protein polymerises into an aggregate consisting of tightly packed beta sheets.
The transmissible agent of prion disease consists of prion protein (PrP) in β-sheet-rich state (PrPSc) that can replicate its conformation according to a template-assisted mechanism. This mechanism postulates that the folding pattern of a newly recruited polypeptide accurately reproduces that of the PrPSc template.
Prion molecules are found at the cell surface, where they are anchored to the nerve cell membrane by short fatty acid molecules called glycosylphosphatidylinositols (GPIs), which are attached to the prions following synthesis of the proteins. Prions are, therefore, most likely to play a role (or roles) in some aspect of the cell-to-cell signalling process.
This illustration is the first step to full-length animation covering all prion transmitting mechanism - from delivery inside neuron until forming amyloid strands. This animation will be available this fall.
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