rare fatal degenerative disease of the central nervous system (nervous system, human). Creutzfeldt-Jakob disease occurs throughout the world at an incidence of one person in a million; however, among certain populations, such as Libyan Jews, rates are somewhat higher. The disease commonly occurs in adults between the ages of 40 and 70, although some young adults have been stricken with the disease. Both men and women are affected equally. The onset of the disease is usually characterized by vague psychiatric or behavioral changes, which are followed within weeks or months by a progressive dementia that is often accompanied by abnormal vision and involuntary movements. There is no known cure for the disease, which is usually fatal within a year of the onset of symptoms.

The disease was first described in the 1920s by the German neurologists Hans Gerhard Creutzfeldt and Alfons Maria Jakob. Creutzfeldt-Jakob disease is similar to other neurodegenerative diseases such as kuru, a human disorder, and scrapie, which occurs in sheep and goats. All three diseases are types of transmissible spongiform encephalopathies, so called because of the characteristic spongelike pattern of neuronal destruction that leaves brain tissue filled with holes.

Creutzfeldt-Jakob disease, as well as other spongiform encephalopathies, is caused by an unusual pathogenic agent called a prion. A prion is a deviant form of a normally harmless protein found in the brains of mammals and birds. As prions replicate—by converting normal forms of the protein into their abnormal shape—they accumulate within nerve cells, causing neurodegeneration.

Although Creutzfeldt-Jakob disease can be acquired through infection with the prion protein, all but 1 percent of cases are either inherited or sporadic (i.e., occurring at random). Sporadic forms account for the majority of cases of the disease—between 85 and 90 percent. In these cases it is unclear what molecular process causes the prion protein to appear in the first place. The protein may arise from a mutation incurred as the body ages or as a result of a spontaneous conversion in the protein's shape. The remaining 10 to 15 percent of cases show a familial pattern of inheritance. In these inherited cases a mutation in the prion protein gene (designated PRNP), which encodes the protein, is passed from parent to child in a dominant fashion (i.e., only one of the two copies of the gene that are inherited—one from each parent—need be mutated for disease to occur). More than 30 different mutations in PRNP that give rise to prion proteins have been identified. While some of these mutations cause Creutzfeldt-Jakob disease, others cause Gerstmann-Sträussler-Scheinker syndrome and fatal familial insomnia. In addition, mutations have been identified that do not cause disease but may render individuals more susceptible to infection with the prion. These latter mutations may be involved in some of the sporadic incidences of the disease.

There is no evidence that a person with Creutzfeldt-Jakob disease is contagious. The rare cases of Creutzfeldt-Jakob disease that arise from human-to-human transmission have resulted only from exposure to the prion during medical procedures; this form of the disease is known as iatrogenic Creutzfeldt-Jakob disease (iCJD). Such accidental transmission has occurred in corneal (cornea) transplants and through the use of contaminated medical or surgical instruments. Transmission also may have occurred through the injection of growth hormone derived from human pituitary glands (pituitary gland). Although human-to-animal prion transmission has been demonstrated in the laboratory, researchers are not sure whether prions that cause disease in one species can give rise to a prion disease in humans. Concern about this type of transmission increased in the mid-1990s when a number of young adults in Great Britain developed a new variant form of Creutzfeldt-Jakob disease (nvCJD). There is increasing evidence that these cases resulted from the consumption of tissues (notably nerve tissue) contaminated with the prion that causes bovine spongiform encephalopathy, or mad cow disease. Chronic wasting disease, which is caused by a prion that occurs in elk and deer, is similar in nature to bovine spongiform encephalopathy. Although there have been no cases of animal-to-human transmission of this prion, researchers suspect that eating contaminated tissues of deer and elk could give rise to another variant form of Creutzfeldt-Jakob disease. As a result, scientists have been monitoring cases of Creuztfeldt-Jakob disease in areas where chronic wasting disease is endemic.