Protein conformation determines the sensibility to high pressure treatment of infectious scrapie prions.
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.
Heindl
Philipp
P
Federal Research Center for Nutrition and Food, Institute of Chemistry and Biology, Haid-und-Neu-Str. 9, 76131 Karlsruhe, Germany. philipp.heindl@bfel.de
García
Avelina Fernández
AF
Butz
Peter
P
Pfaff
Eberhard
E
Tauscher
Bernhard
B
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
D018620:PrPSc Proteins