What is Creutzfeldt-Jakob disease primarily assumed to be caused by?

Creutzfeldt-Jakob disease (CJD) is primarily caused by prions, which are misfolded proteins that induce abnormal folding of normal proteins in the brain. This leads to severe neurological damage and is characterized by rapid cognitive decline, memory impairment, and behavioral changes. Unlike infectious agents like viruses and bacteria, prions are unique in that they do not contain any nucleic acids; they propagate by inducing normal proteins in the brain to misfold, resulting in a progressive and fatal neurodegenerative disorder.

The nature of prions explains why traditional methods of sterilization used for bacteria and viruses are often ineffective against them. This distinct pathogenic mechanism underlines the importance of prion research in understanding CJD and similar disorders, which fall under the category of transmissible spongiform encephalopathies (TSEs).

Understanding that CJD is associated with prions rather than other types of pathogens helps clarify the unique challenges faced in diagnosing and managing the disease, as well as the implications for public health, particularly concerning variant forms of the disease linked to dietary exposure.