Before getting my B.S. in Molecular Biology at California State University Monterey Bay, I took an emerging diseases course at City College of San Francisco and became fascinated by the history of the disease in humans, how much progress has been made in the past hundred years, and persistent problems due to the increasing incidence of antibiotic-resistance. During undergrad, I began reading papers on infectious disease, and found myself wondering about how unique and novel prions are compared to other diseases. There are no cures for these neurodegenerative conditions, and current studies can only use small sample populations due to the rarity of prion diseases. Prions can be transmitted from between surgical patients as prions survive normal sterilization procedures (1). Corneal and dura matter transplants carry a risk of prion transmission, if the donor had an undetected prion disease (2). Many living in Europe still cannot donate blood due to concerns about vCJD contamination (3). Those diagnosed have a life expectancy of a year or less, as there is no known cure.

Protein to Prion

A normal PrPc protein is water soluble and susceptible to proteases due to its amino acid composition, which in turn causes the two-dimensional sequence of amino acids to fold into a three-dimensional structure. A PrPsc protein is biochemically identical to a normal protein, but its three-dimensional shape has been folded into a structure that does not function the same way a normal PrPc protein should. A normal PrPc protein has a content of 42% alpha helices and 3% beta sheets. A PrPsc protein is 43% beta sheets and 30% alpha helices (4). Alpha helices are hydrophilic and beta sheets are hydrophobic. All of a sudden, hydrophilic sections of the protein are now tucked away and hydrophobic sections form a protective barrier. Because the protein now has this hydrophobic barrier, its now mostly water insoluble and resistant to proteases (5).

Prions begin accumulating in the brain, causing neurotoxicity, which leads to symptoms of ataxia, myoclonus, dementia and eventually leading to akinetic mutism and death (5). For most diseases, we have lots of tools and treatments to help or slow down the progression. After 60+ years of research into prions, we still don't have any treatment, prevention or medication that slows clinical progression. This is a massive puzzle waiting to be understood. There is an untapped frontier, as so much less is known about prions than other pathogen types.

Ruth Hastings

Aspiring Graduate Student in Prion Research

Protein to Prion