Submitted to: Meeting Abstract
Publication Type: Abstract Only
Publication Acceptance Date: January 25, 2006
Publication Date: April 30, 2006
Repository URL: http://www.aocs.org/archives/am2006/session.asp?session=FM+3%3A+Animal%2DHuman+Linked+Health+and+Nutrition+Issues
Citation: Silva, C.J. 2006. Prions: pathological proteins at the interface of oil and water [Abstract]. 97th AOCS Annual Meeting & Expo, April 30-May3, 2006, St. Louis, MO. Abstract # FM3-1; page 43. Available: http://www.aocs.org/archives/am2006/session.asp?session=FM+3%3A+Animal%2DHuman+Linked+Health+and+Nutrition+Issues Technical Abstract: Prions are infectious proteins that cause of a set of rare fatal neurological diseases referred to as transmissible spongiform encephalopathies (TSEs). TSE diseases occur in humans, sheep, goats, deer, elk, mink, cows and other mammals. This presentation will include an historical review of the science behind the development of the prion model. It will highlight current research on the chemistry and detection of prions. The role of the glycosyl phosphatidylinositol (GPI) anchor in the pathology of this molecule will be discussed. A prion is an infectious isoform (PrPSc) of a normal cellular protein (PrPC). PrPC is a globular protein composed of approximately 209 amino acids, depending on species. It has three post-translational modifications (PTM): a disulfide linkage, two large sugar antennae, and a GPI anchor to covalently link PrPC to the lipids in the cell membrane. Its natural function remains unclear. For a given host, PrPSc and PrPC have the same primary amino acid sequence, disulfide linkage, and PTMs. PrPSc, however, has the capacity to induce PrPC to adopt the PrPSc conformation and thereby propagate an infection that leads to cell death. If PrPSc is completely denatured and then allowed to refold, the resulting protein is PrPC and not PrPSc.