Robert C.C. Mercer, Ph.D.

Prion diseases are a group of rare and invariably fatal protein misfolding neurodegenerative diseases that include Creutzfeldt-Jakob disease (CJD) of humans, bovine spongiform encephalopathy (BSE or “mad cow disease”) of cattle, and chronic wasting disease (CWD) of deer, elk, and moose. Although they affect different species, these diseases share a key molecular event: the conversion of the normally soluble prion protein (PrP^C) into a misfolded, disease-causing conformation (PrP^Sc) that is rich in β-sheet structure, insoluble, and resistant to proteolytic degradation.

Prion diseases are especially fascinating because of their unusual etiology: they can arise sporadically (~90%), through inherited mutations (~10%), or by infection (<1%). Remarkably, prions are the only known infectious agents that contain no nucleic acids; they replicate and spread from cell-to-cell through a poorly understood self-templating mechanism.

My laboratory is interested in the molecular and cellular underpinnings of this spread, and how similar “prion-like” mechanisms are at play in more common diseases like Alzheimer’s, Parkinson’s, and frontotemporal dementia. Our work has been supported by the National Institutes of Health, the United States Department of Defense, the United States Department of Agriculture, and the Creutzfeldt-Jakob Disease Foundation.

We welcome curious and motivated students who are eager to gain hands-on experience in molecular neurobiology, protein biochemistry, and therapeutic development.

A list of publications can be found on my Google Scholar profile.