Question

Why are the beta-pleated multimers of PrP potentially pathogenic?

A. They are found on the surface of immune cells, resulting in damage to the immune system.
B. The multimers are more stable and resistant to protease.
C. They are not detected by other organisms.
D. They repress the immune system.

Answer 1

Beta-pleated multimers of PrP (PrPSc) are pathogenic because they are resistant to proteolysis and cause aggregation of proteins that lead to brain tissue damage in diseases like Creutzfeldt-Jakob disease.

Step-by-step explanation:

The beta-pleated multimers of PrP are potentially pathogenic because they represent a misfolded and disease-causing form of the normal cellular prion protein (PrPC), known as PrPSC. This abnormal form of PrP folds predominantly into beta-pleated sheets that are resistant to proteolysis, allowing them to aggregate and become toxic. The accumulation of these prion proteins in brain tissue leads to the characteristic spongy texture seen in transmissible spongiform encephalopathies, such as Creutzfeldt-Jakob disease. Moreover, PrPSC can induce the normal PrPC to misfold, thereby amplifying the pathological process.