ARS | Publication request: Prions: The Chemistry of Infectious Proteins

Submitted to: Annual Meeting and Expo of the American Oil Chemists' Society
Publication Type: Abstract Only
Publication Acceptance Date: September 21, 2008
Publication Date: September 22, 2008
Citation: Silva, C.J. 2008. Prions: The Chemistry of Infectious Proteins [Abstract]. American Oil Chemists' Society. S-401. p.63.

Technical Abstract: A prion is pathological protein that causes a set of rare fatal neurological diseases called transmissible spongiform encephalopathies (TSE). TSE diseases occur in humans, sheep, goats, deer, elk, mink, cows and other mammals. A prion and the normal cellular prion protein (PrPC) have the same primary amino acid sequence, disulfide linkage, and post-translational modifications. They differ only in their respective conformations. Prions have the capacity to induce PrPC to adopt the prion’s conformation and thereby propagate an infection that leads to the death of the host. Prions are very stable. They persist in the environment for years and are resistant to autoclaving, and many conventional forms of inactivation. A given host can propagate more than one type of prion. These different prions are derived from the same PrPC and are referred to as strains. Prion strains have distinctive phenotypes with characteristic pathologies, incubation times, and stabilities. Prions have the ability to adapt to new hosts and yet retain their distinct properties. This presentation will provide an introduction to the chemistry of these novel pathogens.