Creutzfeldt-Jakob disease (CJD) is a very rare, fatal disease that attacks the nervous system. There are two types of CJD: classical CJD and variant CJD.
Unlike other diseases that are caused by bacteria or viruses, this disease is caused by abnormal pieces of protein called prions. These abnormal prions damage cells of the nervous system, forming holes in the tissue and eventually leading to severe brain damage and death.
Classical CJD is very rare, affecting about 1 person in 1 million each year. About 30 people are diagnosed each year in Canada, most of them are between the ages of 45 and 75 years. The three types of classical CJD include:
Variant CJD (vCJD) typically affects younger people less than 30 years of age and is associated with eating meat from cows infected with bovine spongiform encephalopathy (BSE), popularly known as “mad cow disease.”
The causes of variant and classical forms of CJD seem to be different. Variant CJD is associated with eating meat from cows infected with BSE. Classical CJD is an older form of CJD, which usually appears spontaneously without any apparent cause and has not been linked to eating contaminated meat. It may be associated with genetic factors, and in some cases it may be caused by contaminated medical equipment.
The link between vCJD and eating infected meat was discovered when 23 people in Britain developed CJD in the mid 1990s, about 10 years after Britain was struck by an epidemic of bovine spongiform encephalopathy in 1984 to 1986. The total rate of CJD was only about 15% higher than usual, but these victims stood out because they were young (the average age was 29) and had different symptoms than were thought to be typical of CJD. Because of these unusual features of this variant CJD, scientists started to investigate. It was already known that some neurodegenerative diseases (diseases that destroy the brain or nervous system) can be caught by eating animals that had the disease.
Scientists began to suggest that British cows had been infected with BSE because they had been fed the rendered remains of sheep. Sheep suffer from a neurological disease called scrapie, so-named because the affected sheep would try to scrape off their coat of wool by rubbing against fence posts and trees. It was then that scientists started to explore the theory that if cows could catch BSE by eating sheep who had scrapie, then maybe people could catch variant CJD by eating cows who had BSE. Evidence began to accumulate that confirmed the ability of the disease to cross the species barrier when cases of degenerative neurological disease started to emerge in zoo animals in Europe. These animals had also been fed remnants of sheep.
Previous tests of scrapie and CJD in mice and monkeys showed that it took about 10 years for symptoms to appear after eating nerve tissue from an infected animal. This matched the British timeline perfectly.
There was a problem in the theory, however. No one had found a bacterium or virus that caused any of these diseases. In fact, scrapie-infected tissue was still known to be infectious even after being exposed to radiation that would destroy DNA, and thus kill any bacterium or virus. Finally, it was discovered that a protein called a prion seemed to be causing the damage.
Proteins are long molecules made of smaller parts called amino acids that are folded up into particular shapes. A prion is folded differently from the normal protein. It also has the ability to make normal proteins that touch it fold the same abnormal way, leading to a domino effect, causing abnormal protein folding that spreads from one protein to the protein beside it. This is a completely new form of disease, caused by a protein that’s not alive but is capable transforming the proteins around it.
It now seems that scrapie, BSE, and CJD (classical and variant) are all caused by prions transmitted from one affected brain to another brain.
At this time, it is not believed that prions are spread through casual contact, kissing, or sexual intercourse.
Classical CJD causes rapid deterioration of the brain and nervous system. The first symptoms usually include less coordination, depression, rapid changes in mood, and less interest in interacting with people. The affected person may also become apathetic, have memory lapses, and sleep irregularly.
Later, a person with CJD starts to suffer from aphasia, an inability to complete the mental connections required to understand speech or to formulate words. A person with aphasia may hear you speak but not understand the words, or may know what an object is but be unable to name or describe it. Mental deterioration (dementia) occurs much faster in classical CJD than in conditions such as Alzheimer’s disease.
Muscle coordination fades rapidly, and within a few months the person with CJD may experience frequent collapses, trembling, and muscle spasms. People with the disease eventually become bedridden and slip into a coma. Death occurs 3 to 12 months after the onset of symptoms. About 70% of people with classical CJD die within 6 months after symptoms appear. Autopsy results show the brain to have many small holes, like a sponge. This also appears with BSE and scrapie.
Variant CJD can run a slightly different course. In the early stages, there are psychiatric symptoms like aggression, severe depression, anxiety, or other changes in the person’s behaviour. Later, the person may feel pain in their face or arms and legs, followed by problems with coordination and lower mental capacity. Many early cases of vCJD are often mistaken for psychiatric disease. On average, people with vCJD live one year after symptoms appear.
Until recently there was no clear test for CJD in a living person.
A recent study suggests that a reliable diagnosis can be established by analyzing cerebrospinal fluid (CSF) for 14-3-3 protein and for PrP.
Tests that monitor brain wave activity (EEG), special genetic tests looking for susceptibility to vCJD, magnetic resonance imaging (MRI) to obtain images of the brain, and spinal fluid tests (“spinal taps”) to test for a specific protein can provide clues that point towards a diagnosis of CJD.
Taking a sample of tonsil tissue (tonsil biopsy) may help to diagnose variant CJD. However, the disease can only be confirmed by a direct examination of brain tissue. Taking a sample of brain tissue (called a brain biopsy) can establish the diagnosis late in the disease, but often CJD can only be confirmed by examining a person’s brain tissue after death.
This is a very rare disease, and although some symptoms might look like they are due to CJD, they are more likely to be caused by another condition. Only close observation over time might give the doctor clues that point to a CJD diagnosis. For instance, dementia appears much more quickly in CJD than in conditions like Alzheimer’s.
There is no known cure or treatment for CJD.
Classical CJD cannot be completely prevented or avoided, but it occurs so rarely that the odds are greatly against being infected with it. Health care providers can minimize risk by handling tissues and bodily fluids with extreme caution, and using effective sterilization methods consistently to disinfect equipment. People with classical CJD can have genetic testing done to see if the disease runs in their family. Genetic counselling may be recommended before this testing is done.
The risk of variant CJD can be decreased by not eating the brains and nervous system tissue of prion-infected animals. Obviously, you can’t guarantee that a particular piece of meat is prion-free. However, when reports of infected cows occur, countries and officials are typically quick to isolate and trace the affected animals, making human infection very unlikely.
In North America, there is a prion disease affecting deer and elk, called chronic wasting disease. If you hunt, you might want to think twice before shooting or eating an elk or deer that appears confused, deranged, emaciated, or unconcerned about its own survival. By law, animals with signs of chronic wasting disease must be reported to provincial authorities.
Prions tend to accumulate in nerve cells, and cuts of meat that come from near the spinal cord and brain are the most dangerous. You are probably less likely to eat prions if you eat cuts of meat from other parts of the animal (e.g., steaks, roasts). Keep in mind that prions are not destroyed by cooking meat.
Canada is taking the following steps to prevent the spread of BSE in cattle, which will decrease the risk of variant CJD in humans:
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