In a recent article published in the Journal of Virology Jan Priem (CVI) et al. demonstrated that they were able to replicate ruminant prions in vitro with a protein-PCR-like test.
With this technique it is possible to assess within a few days whether prions are efficiently transmissible between different animal species. This method means that for prion transmissibility studies the use of experimental animals could be significantly reduced.
TSEs (transmissible spongiform encephalopathies or prion diseases) such as bovine spongiform encephalopathy (BSE), scrapie and Creutzfeldt-Jakob disease (CJD) are fatal neurodegenerative diseases caused by proteinaceous infectious particles called “prions”. After a prion has entered the host it can take years before any clinical signs occur. Priem et al. used the PCMA method (protein misfolding cyclic amplification, sort of protein-PCR) to measure the formation speed of prions at the molecular level.
The research team is now developing a variant of this protein misfolding technique to assess the TSE susceptibility of other species including different genetic variants of goats and humans.
Jan Priem, Jan P.M. Langeveld, Lucien J.M. van Keulen, Fred G. van Zijderveld, Olivier Andreoletti, and Alex Bossers. 2014. Enhanced virulence of sheep-passaged BSE is revealed by decreased polymorphism-barriers in prion protein conversion studies. J.Virol. 88: 2903-2912.