Prion Research and Neuropathology

Prion diseases of economic and societal importance.

Our work focuses on prion diseases or transmissible spongiform encephalopathies (TSE) of animals and humans that pose significant risks to health, economic and food security.

Prions are a misfolded form of the host prion protein, whose function is still not fully understood. According to the prion hypothesis, prions replicate without nucleic acids (DNA or RNA) unlike bacterial or viral pathogens. Instead prions replicate by re-folding the host protein into the disease-causing form, resulting in a build-up of prions and damage to the nervous system.

Prions are highly resistant to many common methods of decontamination and may persist in the environment for long periods of time. They are characterised by long incubation periods, the time between infection and the appearance of symptoms. The symptoms of prion diseases are a rapid and progressive neurodegeneration. Prion diseases currently have no effective treatment and are invariably fatal. Prions have zoonotic potential, shown by the transmission of bovine spongiform encephalopathy (BSE or 'mad cow disease') to humans.

Current research interests:

• Differences in host susceptibility and routes of transmission.
• Human and animal prion disease pathogenesis and strain characterisation.
• Molecular mechanisms underlying the pathogenesis of infectious and neurological diseases of ruminant livestock.
• The function of the host prion protein and its role in disease.
• The nature of the prion agent in blood and other body fluids.
• The roles of the host immune and nervous systems in prion diseases.

Key contacts

You can also find us on Twitter @RoslinPRNP.

Related links

TSE Resource Centre

Prions Matter

Brain infection starts in gut, study finds

Protein sheds insight into vCJD

Immune systems fighting prions; older might be better

Comment on BSE case in Aberdeenshire