Scrapie and Creutzfeldt-Jakob Disease Prion Proteins Share Physical Properties and Antigenic Determinants

摘要

Scrapie of sheep and goats as well as Creutzfeldt-Jakob disease (CJD) of humans are neurologic disorders caused by slow infectious pathogens. The novel molecular properties of the pathogenscausing scrapies have prompted introduction of the term prion to denote a small proteinaceous infectious particle that resists inactivation by nucletic acid modifying procedures. Antiserum of the major hamster scrapie prion protein (PrP 27-30) was found to cross-react with murine CJD proteins. The CJD proteins had molecular weights similar to those observed for scrapie prion proteins. The CJD proteins were resistant to digestion by proteniase K and appear to polymerize into rod-shaped particles. The purification procedure developed for scrapie prions was found to be useful in purifying the CJD agent. Purification of the two infectious pathogens by virtually identical procedures provided further evidence from similarities in their molecular structures. We conclude that the molecular and biologic properties of the CJD agent are sufficiently similar to those of the scrapie prion protein that CJD should be classified as a prion disease.