NR AWAX
AU Aiken,J.M.; Johnson,C.; Ma,X.; McKenzie,D.; Pedersen,J.P.
TI Prions adhere to soil and remain infectious
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 PA-01
PT Konferenz-Poster
AB An unidentified environmental reservoir of infectivity contributes to the natural transmission of prion diseases (transmissible spongiform encephalopathies, TSEs) in sheep, deer and elk. Prion infectivity may enter soil environments via shedding from diseased animals and decomposition of infected carcasses. We examined the potential for soil to serve as a TSE reservoir by studying the sorption of the disease-associated prion protein (PrPsc) with common soil minerals. We demonstrated substantial PrPsc adsorption to whole soils as well as clay minerals (montmorillonite and kaolinite) and quartz. We quantified the PrPsc binding capacities of each mineral examined. Furthermore, the PrPsc desorbed from montmorillonite (Mte) clay was cleaved at an N-terminal site and the interaction between PrPsc and Mte was strong, making desorption of the protein difficult. Despite cleavage and avid binding, PrPsc bound to Mte remained infectious. Results from our study suggest that PrPsc released into soil environments is maintained in a bioavailable form, perpetuating prion disease epizootics and exposing other species to infectious agent.
AD J.M. Aiken, C. Johnson, D. McKenzie: Department of Animal Health and Biomedical Sciences; X. Ma: Program in Cellular and Molecular Biology; J.P. Pedersen: Department of Soil Science, University of Wisconsin, Madison, WI, USA. E-mail: aiken@svm.vetmed.wisc.edu
SP englisch
PO Italien
EA Poster, Übersicht, Ausschnitt 1, Ausschnitt 2, Ausschnitt 3