BSE - Causes of Creutzfeldt-Jakob disease

Creutzfeldt-Jakob disease (CJD) is caused by an abnormal infectious protein in the brain called a prion.

Proteins are molecules, made up of amino acids, which help the cells in our body to function. They begin as a string of amino acids that then fold themselves into a three-dimensional shape. This 'protein folding' allows them to perform useful functions within our cells.

Normal prion proteins (thought to be the precursors of the infectious prions that cause CJD) are found in almost all body tissues, but at highest levels in brain and nerve cells. The exact role of the normal prion proteins is unknown, but it is thought they may play a role in transporting messages between certain brain cells.

How prions cause CJD 

Sometimes, mistakes happen during protein folding and the prion protein cannot be used by the body. Normally these misfolded prion proteins are recycled by the body, but if they are not they can build up in the brain.

Prions are misfolded prion proteins that surround brain cells and cause normal prion proteins to misfold as well. This causes the brain cell to die, releasing more prions to infect other brain cells.

Eventually, clusters of brain cells are killed and areas where prions have built up, called plaques, may appear in the brain.

Prion infections also result in the appearance of small holes in the brain, causing it to become sponge-like. The damage to the brain causes the mental and physical impairment and eventual death associated with CJD.

Prions can survive in nerve tissue, such as the brain or spinal cord, for a very long time, even after death.

Types of CJD

There are a number of different types of CJD. They are all caused by a build-up of prions in the brain, but the reason why this happens is different for each type.

The causes of the main types of CJD are described below.

Sporadic CJD

Sporadic CJD is the most common type of CJD, accounting for around 8 in every 10 cases, although it is still very rare.

It is not known what triggers sporadic CJD, but it may be that a normal prion protein spontaneously changes into a prion or a normal gene spontaneously changes into a faulty gene that produces prions. 

At present, nothing has been identified that increases your risk of developing sporadic CJD.

Variant CJD

There is clear evidence that variant CJD (vCJD) is caused by the same strain of prions that causes bovine spongiform encephalopathy (BSE or 'mad cow disease').

A government inquiry in 2000 concluded that the prion was spread through cattle that were fed meat-and-bone mix containing traces of infected brains or spinal cords. The prion then ended up in processed meat products, such as beef burgers, and entered the human food chain.

Strict controls have been in place since 1996 to prevent BSE from entering the human food chain and the use of meat-and-bone mix has since been outlawed.

It appears that not everyone who is exposed to BSE-infected meat will go on to develop vCJD.

All definite cases of vCJD occurred in people with a specific version of a gene called codon 129, which affects how the body makes a number of amino acids. It is estimated that up to one half of the UK population have this version of the gene.

Cases of vCJD peaked in the year 2000, in which there were 28 deaths from vCJD. There were no confirmed deaths in 2012. Some experts believe that the food controls have worked and that further cases of vCJD will continue to decline, but this does not rule out the possibility that other cases may be identified in future.

It is also possible for vCJD to be transmitted by blood transfusion, although this is very rare and measures have been put in place to reduce the risk of this happening.

There is considerable uncertainty about how many people in the UK population could develop vCJD in the future and how long it will take for symptoms to appear, if they ever will.

A study published in October 2013 that involved testing random tissue samples suggested that around 1 in 2,000 of the UK population may be infected with vCJD, but show no symptoms to date.

Familial or inherited CJD

This very rare form of CJD is caused by an inherited mutation (abnormality) in the gene that produces the prion protein. The altered gene seems to produce misfolded prions that cause CJD.

Everyone has two copies of the prion protein gene, but the mutated gene is dominant. This means you only need to inherit one mutated gene to develop the illness. So if one of the parents has the mutated gene, there is a 50% chance it will be passed on to each of their children.

As the symptoms of familial CJD do not usually begin until a person is in their 50s many people with familial CJD are unaware that their children are also at risk of inheriting this condition when they decide to start a family.

Iatrogenic CJD

Iatrogenic CJD (iCJD) is when the infection is spread from someone with CJD through medical or surgical treatment.

Most iatrogenic CJD cases have occurred through the use of human growth hormone, which is used to treat children who have restricted growth. Between 1958 and 1985, thousands of children were treated with the hormone, which at the time was extracted from the pituitary glands (a gland at the base of the skull) of human corpses.

A minority of those children developed CJD, as the hormones they received were taken from glands infected with CJD. Since 1985, all human growth hormone in the UK has been artificially manufactured, so there is now no risk.

A few other cases of iCJD occurred when people received transplants of infected dura (tissue that covers the brain) or came into contact with surgical instruments that were contaminated with CJD. This happened because prions are tougher than viruses or bacteria, so the normal process of sterilising surgical instruments had no effect.

Once the risk was recognised, the Department of Health tightened the guidelines on organ donation and the reuse of surgical equipment. As a result, cases of iCJD are now extremely rare.