Professor Michael Woodside, pictured in his lab at the University of Alberta. Photo credit: John Ulan
A federal infusion of funding is supporting research in the University of Alberta’s Faculty of Science on prion diseases.
Prion diseases are caused by the misfolding of certain proteins in the brain, called prions, and are the cause of fatal, neurodegenerative diseases in both humans and animals. The most common prion disease is Creutzfeldt-Jakob disease, more colloquially known as mad cow disease.
“As it turns out, the proteins can take on many different types of diseased structures, or strains, which can quickly adapt to resist drug treatments,” explained Michael Woodside, professor in the Department of Physics and lead investigator on the project. “This characteristic has made it difficult to find effective drugs—and it has been extremely difficult to study, because it requires delicate control over the chemical modifications that cells make naturally to proteins.”
The goal of the new project is to carefully control the proteins in a lab setting, examining how strains adapt as they are exposed to different treatments, and allowing the researchers to identify which features of the proteins control this process of adaptation. “The hope is that we will be able to apply what we learn to support efforts to find more effective drug treatments,” added Woodside. “There is a much larger set of diseases that share the same behaviour of propagated misfolding and strain adaptation, such as Alzheimer's disease and Parkinson's disease. What we learn from prion diseases may have much wider implications for treating more common diseases.”
Prison diseases are also becoming increasingly common among wild deer and elk populations, which have the potential to cross over into human populations in the same way that Creutzfeldt-Jakob disease transferred from cows to humans.
The research team includes Chris Cairo, associate professor in the Department of Chemistry and Valerie Sim, associate professor in the Department of Medicine in the Faculty of Medicine & Dentistry.
“This is a unique team with key expertise in the biophysics and biology of prions as well as glycobiology,” said Cairo. “Glycobiology is the study of carbohydrates, known as glycans, which can be attached to proteins and lipids in cells. Naturally occurring prions, like most proteins, are often modified by glycans. Our plan is to generate samples with defined glycans so we can understand their impact on folding of prions, but also on their spread within the body.”
Funding for this research is provided by the New Frontiers in Research Fund (NFRF), a federal research funding initiative designed to support high-risk, high-reward research.
“This funding will allow us to pursue some important ideas that we've wanted to study for a while, but for which it's been hard to get funding because of the riskiness and technical difficulty of the research,” said Woodside. “The University of Alberta is the ideal place to carry out this work because of the strengths we have in prion and protein misfolding diseases and also in carbohydrate chemistry, the chemistry of the modifications involved in prion diseases.”
The University of Alberta is home to the Centre for Prion and Protein Misfolding Diseases, the largest group of researchers in this field in Canada, as well as GlycoNet, a pan-CanadianNetwork Centre of Excellence of more than 140 researchers, centred at UAlberta.