Jones Faculty Lecture, Professor Justin Hines

Cannibalism, Kuru, and Mad Cows: the story of prions and what we can learn from baker’s yeast

Proteins are molecular machines, often with multiple moving parts, that accomplish nearly every function of every living organism. Like any machine, the specific three-dimensional structure of a protein is critical for function, and the acquisition of that structure for a protein is called “folding.” In the late 1950s, a strange disease in a remote highland region of Papua New Guinea shook the foundations of biology, biochemistry, and modern medicine. The disease agent was unlike any other on Earth—infectious, 100% lethal, impervious to virtually every assault, and above all, impossible to characterize within the schema of known disease agents—garnering earnest consideration that the disease agent may be the actual “Andromeda Strain,” a disease originating from space.

The subsequent 70 years of study revealed the true nature of these disease agents as improperly folded protein aggregates, called “prions,” upending established notions of protein biochemistry. Self-replicating, self-healing, and impossible to kill (because they aren’t alive), prions are difficult to destroy by conventional sterilization techniques and incredibly persistent in natural environments, leading to the late Lewis Thomas’s famous moniker: “the strangest thing in all biology.”

This lecture will revisit the incredible story that precipitated the discovery of prions and subsequent work which led to the revelation of similar, but harmless, structures in baker’s yeast—the subject of my own laboratory investigations. I will specifically highlight the incredible work of numerous Lafayette students who have investigated prions and the proteins that combat them, which furthered both research in my laboratory and educational initiatives over the past seven years.