Answer Happy

Part II - Transmission and Mechanism Upon further investigation, the CDC determined that the graduates were likely afflicted with variant Creutzfeldt-Jacob disease (vCJD). While in college together, all three former students had studied abroad in Scotland, along with 30 other students and two professors. From personal accounts, the students had a wild time studying glaciation patterns during the day and drinking scotch ale and eating haggis and brawn each night. During that same year, Scotland had an outbreak of mad cow disease. Thousands of cows and 49 human deaths were recorded. Mad Cow disease, or bovine spongiform encephalopathy (BSE), is a type of transmissible spongiform encephalopathy (TSE) likely caused by an abnormal, misfolded, form of the prion protein (PrP). The function of normal PrP is unclear, but the structure of the protein is rich in alpha helices and it is expressed as a membrane-bound protein on neurons. In prion diseases, the PrP has fewer alpha helices and is rich in beta-pleated sheets. This abnormal structure causes the protein to clump together, ultimately causing neuronal cell death and sponge-like holes in brain tissue. Evidence suggests that the abnormal PrP converts the normally shaped protein to the disease-causing form; thus the protein, itself, is thought to act as the infectious agent. Given this new information, answer the following questions: Figure 1. Prion structure. Disease-causing PrP (left) and normal PrP (right). Credit: By AJC1 at used in accordance with CC BY-NC 2.0. Questions 1. What was a likely mode of transmission of this prion disease? 2. Is it possible that other members of the study abroad trip could be infected? Why or why not? 3. Is it possible that other members of the university could be infected? Why or why not? 4. Disease-causing prions are a unique infectious agent. What makes this type of infection unique?