Which disease is associated with beta-pleated sheets that are resistant to proteases?

Creutzfeldt-Jakob disease is correctly associated with the presence of beta-pleated sheets that are resistant to proteases. This disorder, a form of transmissible spongiform encephalopathy, is linked to abnormal prion proteins that misfold and aggregate into these resistant structures. These misfolded proteins proliferate in the brain, leading to neurodegeneration and the characteristic spongiform changes seen histologically.

In contrast, Huntington's disease primarily involves the abnormal expansion of CAG repeats in the huntingtin gene, leading to the formation of intranuclear inclusions, but does not prominently feature the protease-resistant beta-pleated sheet configuration characteristic of prion diseases. Alzheimer's disease is associated with amyloid-beta plaques and tau protein tangles, which do not exhibit the same protease-resistant properties as prions. Multiple sclerosis is an autoimmune disease that primarily affects the myelin sheath and does not involve prion-like protein misfolding. Thus, Creutzfeldt-Jakob disease is uniquely notable for its association with beta-pleated sheets that are resistant to proteases.