Abstract
Prions are misfolded, infectious protein agents affecting mammals, including humans. The resulting group of neurodegenerative diseases are called transmissible spongiform encephalopathies (TSEs) and are unfailingly fatal in all species. Prions propagate via template misfolding, in which the host-encoded cellular conformation of the protein, PrPC, comes into contact with the infectious form of prion protein, PrPSc, and misfolds to match this conformation.
Chronic Wasting Disease (CWD) is a highly infectious prion disease of cervids and is endemic in North America. There is evidence that soil may be an environmentally relevant matrix for prion transmission, allowing the proteins to remain stable and infectious for extended periods of time. Using relevant laboratory methodology, we assessed intraspecies infectivity of soil-bound prions.
Structure of PrPSc is paramount to prion disease, impacting strain properties and cross-species transmission. We hypothesized that surface binding, to soil or otherwise, could alter the conformation of PrPSc, resulting in a change in prion strain properties and thus impacting zoonotic potential. With a combination of laboratory assay and bioassay, we investigated interspecies transmission and observable prion strain properties.