NR AURI
AU Heindl,P.; Butz,P.; Pfaff,E.; Tauscher,B.
TI High Pressure as a Tool to Study Prion Folding and Aggregation
QU TSE-Forum, 6. Kongress - Nationale TSE-Forschungsplattform, Greifswald 26.6.-28.6.2006, Poster: Struktur und molekulare Mechanismen MOL-06
PT Konferenz-Poster
AB Application of high pressure can be used for gentle pasteurizing of food, minimizing undesirable alterations such as vitamin losses and changes in taste and colour. 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 favours structural transitions accompanied with smaller volumes. In this presentation, 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 will be discussed. The studies revealed 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 hamster brains. Native prions were found to be pressure sensitive by loosing its characteristic proteinase K resistance and by reducing its infectivity after pressurizing, whereas isolated prions revealed an extreme pressure-resistant structure. This different pressure behavior of these prion isoforms points out differences in the protein structure that have not been taken into consideration before.
AD Philipp Heindl (philipp.heindl@bfel.de), Peter Butz, Bernhard Tauscher, Federal Research Centre for Nutrition and Food, Institute of Chemistry and Biology, Karlsruhe; Eberhard Pfaff, Friedrich-Leoffler-Institute, Institute of Immunology, Tübingen
SP englisch
PO Deutschland
OR Tagungsband