Transmissible spongiform encephalopathies (TSEs) are infectious diseases caused by prions – unconventional pathogens that appear to be composed solely of protein. Prions are misfolded conformers of the normally benign cellular prion protein and can template the conformational conversion of normal prion proteins into misfolded forms. Prions also exhibit extraordinary resistance to degradation. Chronic wasting disease (CWD) is a TSE affecting cervids (deer, elk, moose) and is unique among prion diseases in that it spreads among free-ranging animal populations. Prions that are shed into the environment by infected cervids may accumulate in multiple environmental reservoirs with the potential to facilitate transmission of the disease. As herbivores, the majority of a cervid’s diet is vegetation, and the potential role of prion transmission via plants has been suggested but has received little study. Plant matter contains a variety of constituents that in principle may interfere with the analysis of prions in plant tissue. The development of ultra-sensitive <i>in vitro </i>prion amplification assays has improved prospects for detailed study of prions in complex matrices such as plants. In this presentation we discuss progress in using <i>in vitro </i>prion amplification assays to measure CWD prions in the tissues of plant grown in media containing infectious prions. The methods we have developed exhibit high selectivity and sensitivity for prions.

Detection of infectious prions in plants

ACS Fall 2021

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