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Creutzfeld Jakob Disease is the result of the accumulation of abnormal proteins called prions in the brain. There are several possible explanations for this disease, including inheritance of the mutant protein (i.e. genetics) and transmission of aberrant protein to a host. CJD is considered to be a form of transmissible spongiform encephalopathy, a category which includes Scrapie (sheep), Mad Cow Disease (Cattle), and Chronic Wasting Disease (deer).
CJD is due to an aberrant protein, called a prion. The PrP gene is thought to have normal functions in the animal, possibly in nerve cell transmission.
In its normal configuration, the prion protein is folded correctly and is functional. Abnormal folding of the prion protein causes many prions to accumulate and stick together, forming a kind of plaque in the brain that eventually leads to damage tof nervous tissue. Phagocytic uptake of prions into neurons leads to formation of many vacuoles in neurons (hence the name 'spongiform').
CJD remains asymptomatic for 30 years. After this long incubation period, neurological symptoms 9tremors, loss of coordination, dementia) follow and the patient dies within 12 months.
Unfortunately, diagnosis of CJD is almost impossible until symptoms show
No treatments exist for CJD. Prevention of transmission is by careful monitoring of livestock, elimination of infected livestock, and thorough disinfection protocols (extensive autoclaving, 1 M NaOH, etc) since prions resist most conventional disinfectants and heating.