A Rapid Ultrasensitive Assay for Detecting Prions Based on the Seeded Polymerization of Recombinant Normal Prion Protein (rPrP-sen)

Prion diseases are neurodegenerative diseases of great public concern as humans may either develop disease spontaneously or, more rarely, due to mutations in their prion protein gene or exposures to external sources of infection. Prion disease is caused by the accumulation in the nervous system of abnormal aggregates of prion protein. This technology enables rapid, economical, and ultrasensitive detection of disease-associated forms of prion protein. Specifically, prion aggregates (contained in a biological sample) seed the polymerization of recombinant, monomeric prion protein (rPrP-sen) and the polymerized product is detected as a highly amplified indicator of infectious prions in the sample. This assay differs from the protein-misfolding cyclic amplification assay (PMCA) because it enables the effective use of bacterially expressed rPrP-sen and does not require multiple amplification rounds. In its current embodiment, this assay can be used to detect prions in tissues or fluids from humans (Creutzfeldt-Jakob disease (CJD)), sheep (scrapie), cattle (bovine spongiform encephalopathy), and deer (chronic wasting disease (CWD)). For example, analyses of cerebrospinal fluid and/or nasal brushings from living sporadic CJD patients has allowed for nearly 100% accurate diagnosis.

This technology is available for licensing for commercial development in accordance with 35 U.S.C. § 209 and 37 CFR Part 404.