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Biology Professor’s Grant Furthers Understanding of Prion Biology

Ursinus biology faculty Dale Cameron lands prestigious NIH grant for research with prions, which are linked to neurodegenerative diseases.

Cameron is the recipient of a $331,655 National Institutes of Health grant to continue his research with prions, which are misfolded proteins connected to several neurodegenerative human diseases.

Cameron, associate professor of biology, will be the third Ursinus faculty member in recent years to receive a National Institute of General Medical Sciences Academic Research Enhancement Award (AREA). Amanda Reig, associate professor of Chemistry, and Rebecca Lyczak, associate professor of biology, were each awarded three-year AREA grants in 2014.

“The willingness of the NIH to invest in the sciences here at Ursinus is really a testament to the quality of the scholarly work we do with our students here,” said Cameron.

Cameron’s research uses yeast cells – which have many similarities to human cells and share many genes with humans – to understand how and why some proteins can switch into misshapen, self-propagating, infectious forms called prions (pronounced “pree-ons”).

“In mammals, we know of only one protein that can do this,” he said. Prions formed by this protein are the cause of deadly diseases like Creutzfeldt-Jakob disease in humans and BSE (Mad Cow Disease) in cattle. Several other neurodegenerative diseases of aging – like Alzheimer’s disease – are associated with the misfolding of other types of proteins. “So in humans, protein misfolding is broadly associated with disease.”

In yeast cells, however, several proteins can form prions, which are not always harmful in yeast – in fact, they can actually be advantageous to growth and survival, particularly when cells are subjected to environmental stress, he explained. His research with his students suggested that one such protein can switch into the prion form while it is still being synthesized by the cell.

“In humans, the prion which causes disease may just be a rogue example within a larger class of proteins that can adopt multiple conformations,” Cameron explained, pointing out that it is possible that some proteins may have evolved the ability to switch into different shapes as a way to alter their function, and that prion formation may thus actually be useful to cells.

The frequency with which this switch occurred was heavily influenced by the presence or absence of certain quality control proteins called chaperones, and by changing the abundance and localization of these chaperones, cells could potentially control the frequency with which prions form, he said. “Our preliminary studies now suggest that when this particular prion-forming protein switches into the prion form, it can in turn alter the abundance of many other proteins in the cell – potentially having a profound influence on the physiology of the cell.”

Cameron, who joined the Ursinus faculty in 2009, received his undergraduate degree in molecular genetics, and a Ph. D. in biochemistry and molecular genetics from the University of New South Wales in Sydney. He did post-doctoral work at Brown University and the University of California in San Francisco. – W.G.