Recovery of Infectious Prion Protein from
Environmental Samples
Christian T. Bartholomay1, Debbie McKenzie1,
Katherine McMahon2, Joel Pederson3, and Judd
Aiken1
Departments of Animal Health and Biomedical
Science1, Civil and Environmental Engineering2
and Soil Science3, University of Wisconsin-Madison, Madison, WI
Email:
cbartholomay@svm.vetmed.wisc.edu
The etiological agent responsible for prion
diseases exhibits extraordinary resistance to
degradation and the environmental persistence of prion diseases is
well-established. The
continued expansion of the range of CWD in free-ranging deer in North
America underscores an
urgent need to determine the interaction and/or transport of the infectious
agent (PrPSc) in the
environment. We have initiated studies examining the fate of (PrPSc) in
soils, wastewater
treatment plants and manure digesters. Fundamental to such studies is the
ability to quantitatively
recover the agent, as represented by the infectious prion protein (PrPSc).
We have been testing
the efficacy of extracting PrPSc from soils and sludges. Environmental
samples have been spiked
with PrPSc and recovery determined by Western blot analysis. We examined a
number of
extraction procedures, including sodium dodecylsulfate (SDS) and N-lauroyl
sarkosine
solubilization as well as urea and guanidine denaturation, for their ability
to consistently desorb
PrPSc from environmental samples.