The work of University of Alberta researchers and their teams has contributed to an important next step in finding a cure for deadly prion-folding diseases in humans and animals.
Professor Michael James of the University of Alberta Department of Biochemistry, Professor Nat Kav of the Department of Agricultural, Food and Nutritional Science and their labs collaborated to produce mini-antibodies and antibody fragments used by the Institute of Neuropathology in Zurich to study interactions between the antibodies and the prion protein and how it results in cell death.
The work conducted at the University of Alberta in Canada helps to open the door to designing a molecule that would block prion infection.
The research appears in the July 31, 2013 issue of Nature.
“We hope to design a chemical compound that would bind to some part of the prion molecule to prevent the conversion of the normal form of the protein to the disease-causing form,” said James. Prion protein infections, caused by structural misfolding within the prion protein, lead to fatal neurodegenerative disorders such as Creutzfeldt-Jakob Disease in humans, Bovine Spongiform Encephalopathy (BSE) in cattle and Chronic Wasting Disease in deer. There is currently no cure.
Using recombinant DNA technology, Kav and his lab produced the mini-antibodies and antibody fragments that were then used by James and ultimately studied biologically in the Zurich lab. Using a process called X-ray crystallography, James’s lab was able to identify the three-dimensional structure of where antibodies and antibody fragments bind to the prion molecule, pinpointing regions that are susceptible to changing to a diseased state.
The discovery now makes it possible to begin designing ways to prevent prion disease, in everything from developing treatment for human victims to creating a preventative additive for livestock feed.