Stanley B. Prusiner, MD, UCSF professor of neurology and biochemistry and biophysics, was awarded the Nobel Prize in Physiology or Medicine yesterday.

Prusiner received the prize “for his pioneering discovery of an entirely new genre of disease-causing agents and the elucidation of the underlying principles of their mode of action," according to the Nobel committee in Stockholm, Sweden.

Prusiner discovered an entirely new disease agent, called a prion, which is implicated in rare, slowly progressing brain diseases.

Prion Protein Model (Andrew Wallace) High Resolution Image available (79K)

This illustration compares a normal prion protein to a disease-causing form. The two structures exhibit two different, classic protein motifs, called "alpha helices," and "beta sheets." Alpha helices, seen here in the normal prion (left), consist of linked amino-acid building blocks that spiral around like a coiled spring. Beta sheets form when amino acid chains line up in a flat plane within the protein, as in the disease-causing protein shown here. Research discoveries by Stanley Prusiner, MD, Fred Cohen, MD, PhD, and their UCSF colleagues suggest that the propagation of infectious prions arises from a rearrangement of a normal prion protein into a disease-causing form, a process that can be spurred by the initial presence of the infectious protein. The infectious form of the prion protein (right) arises when alpha-helical regions in the normal protein unfold and beta sheets form within the protein, according to the UCSF researchers. When the protein converts to the form exhibiting more sheet-like regions, it is able to clump together and react in ways that contribute to disease in some as-yet undefined manner. Prion diseases might one day become preventable or treatable with drugs that stabilize the alpha helices of the normal prion protein and prevent the conversion to the beta structure observed in the disease-causing prion form.

Prusiner is in Bethesda, MD, at a meeting of the Food and Drug Administration’s Advisory Committee on Transmissible Spongiform Encephalopathies.

Prusiner’s Nobel Prize-winning research has demonstrated that unlike other pathogens--bacteria, viruses, protozoans and fungi--the prion contains no genetic material. It is mostly a protein.

The prion is the infectious agent that causes scrapie, a disease of sheep and goats, "mad cow disease," which has been epidemic among cattle in Great Britain, and rare but fatal human diseases of the central nervous system. These diseases are in some ways similar to Alzheimer's. They result in dementia and death after a long process.

A better understanding of prion diseases may advance research into neurodegenerative disorders, and could provide insight into the processes by which nerve cells assume specific forms and functions, perform these roles for decades, and then become senescent.

1st appeared 10/06/97

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