One of us remembers sitting in a high school biology class in 1977 being taught about scrapie, a naturally occurring disorder of sheep. The teacher had no particular interest in agriculture, but was pointing out some peculiar characteristics of this disease as a biological curiosity on a wet Friday afternoon. The prion disorders captured the imagination of a range of biologists (including that teacher) well before the epidemic of bovine spongiform encephalopathy (BSE) and the appearance of a new variant of the human prion disease, Creutzfeldt Jakob disease (CJD), in the UK, because of their extraordinary biology and the unique properties of the infectious agent. We review the results of studies leading to a convergence of evidence that the causative infectious agent, the `prion', is devoid of nucleic acid and is composed of an abnormal isoform of a host-encoded protein, the prion protein (PrP).
Mammalian Genome – Springer Journals
Published: Jul 1, 1998
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