NR AWGR
AU Heindl,P.; Pfaff,E.; Tauscher,B.
TI High pressure treatment as a tool to inactivate TSE agents and to study prion protein folding and aggregation
QU International Conference - Prion 2006: Strategies, advances and trends towards protection of society - 3.10.-6.10.2006, Torino, Italy, Lingotto Conference Centre - Poster sessions SA-06
PT Konferenz-Poster
AB High hydrostatic pressure is a mild processing technology with a promising potential in food pasteurization and sterilization by minimizing undesirable alterations such as vitamin losses and changes in taste and color. In addition, high pressure is a thermodynamic parameter providing useful information about the free-energy landscape of proteins. High pressure treatments of proteins can reveal conformations that are not obtainable by other physical variables like temperature, since pressure favors structural transitions accompanied with smaller volumes. Here, both the potential use of high pressure to inactivate infectious TSE agents and the application of this thermodynamic parameter for the investigation of prion protein aggregation and folding will be discussed. Our results show that high pressures (6-8 kbar) combined with temperatures (60-80 °) below sterilization conditions are able to induce a remarkable lose in the proteinase K resistance and infectivity of prions which can be attributed to changes in the structure of the prion protein. However, discrepancies under non-physiological buffer conditions, and between isolated and native prions, point out that pressure effects hardly depend on prion conformation and aggregation and that fractions exist which are especially high pressure resistant. Any treatment leading to more aggregated and dehydrated prions result in an increased pressure resistance. In general, our results confirm that the biggest amount of prions in conditions close to native are pressure sensitive and loose infectivity soon during pressurization.
AD P. Heindl, B. Tauscher: Federal Research Centre for Nutrition and Food, Institute of Chemistry and Biology, Karlsruhe, Germany; E. Pfaff: Friedrich-Leoffler-Institute, Federal Research Institute for Animal Health, Institute of Immunology, Tübingen, Germany. E-mail: philipp.heindl@bfel.de
SP englisch
PO Italien