”PROTECTING THE FOOD CHAIN FROM PRIONS”
About twenty five years ago, the appearance in the UK of Bovine Spongiform Encephalopathy (BSE), quickly brought the previously obscure “prion diseases” to the spotlight. The ensuing health and food crises that spread throughout Europe had devastating consequences. In the UK alone, there were more than 36,000 farms directly affected by BSE and the transmission of BSE prions to humans via the food chain has caused over 200 people in Europe to die from variant Creutzfeldt-Jakob disease (vCJD)
Despite more than a decade of research, many aspects of variant Creutzfeldt-Jakob disease (vCJD) remain a mystery. Now research from Priority scientists at The Roslin Institute is helping us to understand why vCJD appears to mainly affect the young.
Regulation of prion formation by intracellular signalling pathways: possible clues on the fine tuning of prion generation and removal
Cellular mechanisms play a role in conversion of the normal prion protein PrPC to the disease-associated protein PrPSc. The cells provide not only PrPC, but also still largely undefined factors required for efficient prion replication. Work from Priority researchers at the Karolinska Institute in Stockholm, reveals key roles of intracellular signalling pathways in prion formation.
Elucidation of the structure of mammalian prions continues to be one major research challenge. The mechanism of propagation of these infectious agents will not be understood until their structure is solved. However, the polymeric and insoluble nature of prions makes this task very difficult, as high resolution techniques such as NMR or X-ray crystallography cannot be used. Thus, a number of lower resolution analytical approaches have been used and provided important structural information on PrPSc.
Haybaeck J, Heikenwalder M, Klevenz B, Schwarz P, Margalith I, Bridel C, Mertz K, Zirdum E, Petsch B, Fuchs TJ, Stitz L, Aguzzi A.
Department of Pathology, Institute of Neuropathology, University Hospital Zurich, Zurich, Switzerland.
Prions, the agents causing transmissible spongiform encephalopathies, colonize the brain of hosts after oral, parenteral, intralingual, or even transdermal uptake. However, prions are not generally considered to be airborne. Here we report that inbred and crossbred wild-type mice, as well
Priority study shows that the toxicity of antiprion antibodies is mediated by the flexible tail of the prion protein, provides key clues on prion toxicity mechanisms.
Prion infections cause lethal neurodegeneration, a process that requires the presence in target cells of cellular prion protein PrPC, which contains a globular domain hinged to a long amino-proximal flexible tail.