Pathogenic prion protein (PrPTSE) constitutes the major, if not sole, component of the infectious agent in prion diseases. Prions adhere strongly to montmorillonite, yet remain infectious and enhance oral disease transmission relative to unbound agent. Attachment to mineral microparticles may protect prions from inactivation in the digestive system and contribute to their persistence in contaminated environments. Here, we examine the extent to which attachment to montmorillonite protects PrPTSE against treatments demonstrated to cause conformational and/or covalent modification to the protein in solution and show that the effect of attachment to montmorillonite differed among treatments. For example, attenuated total reflectance-Fourier transform infrared spectroscopy revealed that attachment to montmorillonite stabilized PrPTSE conformation against the effect of the chaotropic agent guanidinium chloride. In contrast, attachment to montmorillonite had little effect on the kinetics and extent of inactivation by concentrated NaOH. This study will inform selection of methods for inactivating prions in contaminated environments.

Inactivation of pathogenic prion protein is modulated by attachment to montmorillonite

242nd National Meeting (2011)

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.