Research Projects

Prion diseases are invariably fatal neurodegenerative disorders that affect both humans and animals. Prion diseases are caused by the propagation of a misfolded form of the normal cellular prion protein. Despite advances in our understanding of the nature of the transmissible agent of prion diseases there is still no treatment that has been shown to be effective in slowing or preventing progression of disease in humans. Furthermore, there is currently no pre-symptomatic diagnostic method that can identify patients with early disease who might respond to therapeutic intervention should it become available or identify individuals who are at risk of transmitting disease. A further challenge to the diagnosis, treatment and prevention of prion diseases is the existence of prion strains that reflect different conformations of the misfolded prion protein. The existence of these strains, which manifest in different disease phenotypes, can affect treatment and diagnosis of disease and effect decontamination of surgical equipment. Projects are available that use mouse adapted human prion strains in cell-free, in vitro and in vivo assays using a range of techniques to investigate the effect of prion strain variation on diagnosis, treatment and prevention of prion disease (Brazier et al 2006, Lawson et al 2007, Lawson et al 2008, Klemm et al 2012). 

Image: Prion diseases share common pathologies of vacuolation (a), a reactive gliosis (b) and deposition of a misfolded form of the prion protein (c). It is the shape of the misfolded protein that is believed to encode strain variation. (From Whitechurch, Welton, Collins, Lawson (2017). Prion Diseases in Adv. Neurobiology, Vol. 15, Philip Beart et al. (Eds): Neurodegenerative Diseases, Springer Nature).

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