Joaquín Castilla and his
team at CIC bioGUNE

An international research team coordinated by professor Glenn Telling, from the University of Kentucky (USA) with participation of CIC bioGUNE's researchers has discovered a new way to control the stability of certain types of prions (the pathogens responsible for the Transmissible Spongiform Encephalopaties - TSEs) through the selection of specific proteins. This finding has been published in Science.

While scrapie, a fatal degenerative disease in sheep and goats, is the most extended prion disease in Europe, together with the Bovine Spongiform Encephalopathy (BSE) or mad-cow disease epidemic outbreak in the 90's, in US deer prions are of major concern for the scientific community. Even though there is no statistical evidence that deer prions can infect humans, the disease in wild animals is spreading along US and Canada and constitutes a significant epidemic.

The work of CIC bioGUNE's researchers, led by Joaquín Castilla, has deepened into the role of the different prion strains' properties in the transmission and spreading of the prion disease in cervids. The study shows for the first time the presence of at least two biologically distinguishable strains with pathogenic behaviour which are clearly different to that of Chronic Wasting Disease (CWD), a transmissible spongiform encephalopathy affecting deer.

The importance of the study lies in the fact that a single difference in the primary amino acid sequence of the protein giving rise to prion diseases enables the selection of prion strains. This finding gives chance to the potential control of the stability of certain prion strains through the modification of the primary structure of the infectious protein.