Reflection 1: Prion Diseases

Earlier in the course when we discussed protein structure and folding, I was really interested in the application of prion diseases. I knew that prion diseases were caused by a misfolded protein, but I didn’t realize how it modified a key understanding of biochemistry that primary structure determines function: instead, prion diseases demonstrate that tertiary structure might determine function. In my public health course, we have discussed cases like mad cow disease, which wreaked havoc on public health in the UK. It’s interesting to reflect on the biochemical basis and how one protein can multiply to make many copies of the misfolded version to cause disease. Also, since we learned about how durable prions are in extreme environmental conditions, this makes sense in the context of a disease outbreak and how this might contribute to the difficulty with treating or curing prion diseases. This has transformed my personal understanding of epidemiology. I didn’t consider how a singular misfolded protein could lead to development of such a dangerous infectious disease. Usually, I think about infectious disease in terms of immune activity, which was not demonstrated in patients with Kuru in the case study we reviewed in class. Overall, learning about prion diseases has provided me with a new understanding of the relationships between disease and biochemistry.