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To the Editor: The term prion connotes an iconoclastic paradigm for an infectious agent afflicting humans and other animals.^1-3 It imputes pathogenicity to the 3-dimensional shape of the PrP^sc (prion protein scrapie). The normal cellular protein, PrP^c, by exposure to PrP^sc, adopts the SC conformation, maintaining a cascade of SC production in vivo. Unlike other self-replicating infectious viruses and bacteria, no unique sequences of DNA or RNA are necessary for this alteration, as the amino acid sequence of PrP^c and PrP^scare identical. The SC isoform does exhibit protease resistance as 1 marker. How this conformer modulation occurs is obscure; it may be similar to the "chaperone" functions of some auxiliary proteins that facilitate folding, or to the "epitaxial" outgrowth from a single crystal face, which is exploited in high-performance metallurgy. The propagation of prions is formally similar to that of centrioles, which are aggregates of tubulin that . . . [Full Text of this Article]