Enzymatic digestion of chronic wasting disease prions bound to soil

Samuel E. Saunders, Jason C. Bartz, Kurt C. Vercauteren, Shannon L. Bartelt-Hunt

Research output: Contribution to journalArticlepeer-review

32 Scopus citations


Chronic wasting disease (CWD) and sheep scrapie can be transmitted via indirect environmental routes, and it is known that soil can serve as a reservoir of prion infectivity. Given the strong interaction between the prion protein (PrP) and soil, we hypothesized that binding to soil enhances prion resistance to enzymatic digestion, thereby facilitating prion longevity in the environment and providing protection from host degradation. We characterized the performance of a commercially available subtilisin enzyme, Prionzyme, to degrade soil-bound and unbound CWD and HY TME PrP as a function of pH, temperature, and treatment time. The subtilisin enzyme effectively degraded PrP adsorbed to a wide range of soils and soil minerals below the limits of detection. Signal loss occurred rapidly at high pH (12.5) and within 7 days under conditions representative of the natural environment (pH 7.4, 22 °C). We observed no apparent difference in enzyme effectiveness between bound and unbound CWD PrP. Our results show that although adsorbed prions do retain relative resistance to enzymatic digestion compared with other brain homogenate proteins, they can be effectively degraded when bound to soil. Our results also suggest a topical application of a subtilisin enzyme solution may be an effective decontamination method to limit disease transmission via environmental "hot spots" of prion infectivity.

Original languageEnglish (US)
Pages (from-to)4129-4135
Number of pages7
JournalEnvironmental Science and Technology
Issue number11
StatePublished - Jun 1 2010

ASJC Scopus subject areas

  • General Chemistry
  • Environmental Chemistry


Dive into the research topics of 'Enzymatic digestion of chronic wasting disease prions bound to soil'. Together they form a unique fingerprint.

Cite this