Central biological dogma dictated that every infectious disease on Earth must carry genetic DNA or RNA to reproduce; Stanley Prusiner proved that a misfolded shape of a normal human protein can act like an infectious zombie, converting healthy brain proteins into lethal brain-destroying amyloids. Awarded the 1997 Nobel Prize in Medicine after enduring a decade of intense scientific ridicule, Prusiner’s discovery of "prions" solved Mad Cow disease and unlocked the unified protein-folding mechanism behind Alzheimer’s and Parkinson’s diseases.

In biology, the central rule of life was absolute: every virus, bacterium, fungus, and parasite requires genetic material (DNA or RNA) to multiply and cause disease. When mysterious fatal brain diseases like Mad Cow and Creutzfeldt-Jakob destroyed brains into spongy swiss cheese, scientists searched desperately for a hidden "slow virus" that never existed.
Neurologist Stanley Prusiner subjected the infectious brain material to intense ultraviolet radiation and acid baths that destroyed all genetic material, yet the sample remained fully infectious. He proved that the killer was a "prion"—a single misfolded rogue protein that acts like a zombie, tapping healthy brain proteins on the shoulder and forcing them to flip into indestructible toxic clumps.
Prusiner’s paper earned the 1997 Nobel Prize and transformed neuroscience. By containing the global Mad Cow epidemic, by securing surgical tools and the beef food supply against heat-proof prions, and by explaining protein misfolding in Alzheimer's and ALS, prion biology revolutionized medical science.
Novel Proteinaceous Infectious Particles Cause Scrapie
After infection and a prolonged incubation period, the scrapie agent causes a degenerative disease of the central nervous system in sheep and goats. Six lines of evidence including sensitivity to proteases demonstrate that this agent contains a protein that is required for infectivity. Although the scrapie agent is irreversibly inactivated by alkali, five procedures with more specificity for modifying nucleic acids failed to cause inactivation. The agent shows heterogeneity with respect to size, apparently a result of its hydrophobicity; the smallest form may have a molecular weight of 50,000 or less. Because the novel properties of the scrapie agent distinguish it from viruses, plasmids, and viroids, a new term "prion" is proposed to denote a small proteinaceous infectious particle which is resistant to inactivation by most procedures that modify nucleic acids. Knowledge of the scrapie agent structure may have significance for understanding the causes of several degenerative diseases.
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