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The protease-resistant infectious prion protein, PrP res , that causes transmissible spongiform encephalopathies, is remarkably resistant to conventional physical and chemical sterilization methods, including heat. It was hypothesized that thermal-dependent PrP res  degradation has been underestimated, and the effect of prolonged incubation at 37°C, 55°C, and 80°C on PrP res  detection was examined using brain homogenates from chronic wasting disease-affected elk and mule deer (PrP CWD ). Immunoblotting demonstrated progressive loss of PrP CWD  immunoreactivity with time in all incubated samples as temperature increased, and PrP CWD  was virtually undetectable after 90 days of incubation at 55°C and 80°C. These results indicate that decontamination methods and tissue disposal systems maintaining elevated temperatures for long periods of time could interfere with immunodetection, and the reliability of assays for PrP res  detection could be compromised when applied to tissues exposed to heat with time. Although these results may suggest that such prolonged heat treatment could destroy prions, the observed loss of immunoreactivity does not necessarily correlate with a concurrent loss of infectivity. Bioassay is needed to determine if samples that have been incubated under these conditions retain infectivity.

Effect of Time and Temperature on PrPCWD Immunoreactivity as Evidenced by Western Blot

Effect of Time and Temperature on PrP^CWD Immunoreactivity as Evidenced by Western Blot