title: Protein conformation determines the sensibility to high pressure treatment of infectious scrapie prions.
abstract: Application of high pressure can be used for gentle pasteurizing of food, minimizing undesirable alterations such as vitamin losses and changes in taste and color. In addition, pressure has become a useful tool for investigating structural changes in proteins. Treatments of proteins with high pressure can reveal conformations that are not obtainable by other physical variables like temperature, since pressure favors structural transitions accompanied with smaller volumes. Here, we discuss both the potential use of high pressure to inactivate infectious TSE material and the application of this thermodynamic parameter for the investigation of prion folding. This review summarizes our findings on the effects of pressure on the structure of native infectious scrapie prions in hamster brain homogenates and on the structure of infectious prion rods isolated from diseased hamsters brains. Native prions were found to be pressure sensitive, whereas isolated prions revealed an extreme pressure-resistant structure. The discussion will be focused on the different pressure behavior of these prion isoforms, which points out differences in the protein structure that have not been taken into consideration before.
authors.affiliation: Federal Research Center for Nutrition and Food, Institute of Chemistry and Biology, Haid-und-Neu-Str. 9, 76131 Karlsruhe, Germany. philipp.heindl@bfel.de
authors.forename: Philipp
authors.initials: P
authors.lastname: Heindl
authors.forename: Avelina Fernández
authors.initials: AF
authors.lastname: García
authors.forename: Peter
authors.initials: P
authors.lastname: Butz
authors.forename: Eberhard
authors.initials: E
authors.lastname: Pfaff
authors.forename: Bernhard
authors.initials: B
authors.lastname: Tauscher
mesh_terms: D000818:Animals; D001921:Brain / Q000378:metabolism; D006224:Cricetinae; D006358:Hot Temperature; D018620:PrPSc Proteins / Q000737:chemistry*; D011312:Pressure; D017096:Prion Diseases / Q000378:metabolism*; D011487:Protein Conformation; D011489:Protein Denaturation; D017510:Protein Folding
chemical_list: D018620:PrPSc Proteins