CJD teenager 'reacting well'

Don Simms: No false hope

Radical treatment being given to the Belfast teenager Jonathan Simms, who is suffering from variant CJD, appears to be working.

As scientists announced on Thursday they had proof that it would one day be possible to prevent diseases such as vCJD and the strain found in animals, BSE, Jonathan's father Don said his son was reacting well to treatment.

It is thought that the disease, and others that also progressively destroy the brain, are caused by rogue particles called prions.

Speaking to BBC Radio Ulster on Thursday, Mr Simms said his son had had two operations.

"Jonathan has remained stable, by the law of averages Jonathan should actually be dead by now," he said.

"That is all I would want to say at this stage because I feel it is too early.

"To claim all sorts of things would be giving false hope to others who unfortunately find themselves with this heinous disease."

The 18-year-old is being given repeated infusions of the drug pentosan polysulphate directly into his brain.

'Rogue proteins'

Jonathan's progress is being monitored using regular scans, checking for the presence of bleeding around the injection site.

His condition had deteriorated in the months that his father had campaigned for him to have the drug and he now requires round-the-clock care.

The disease has severely affected his speech and eyesight.

The family hope the drug will slow the rate of progress of Jonathan's illness - or perhaps even clear the "rogue" proteins that cause it from his brain.

Permission for the drug to be used was given after a hearing at the High Court.

More than 100 people in the UK are known to have died from the variant form of CJD so far, with a handful now living with the illness.

Meanwhile, a team from Imperial College in London has discovered the development of prion disease can be prevented in mice using molecules produced by the immune system called monoclonal antibodies.

Prions are proteins that bind to normal proteins in the brain and twist them into abnormal shapes. These then clump together, causing brain damage.

Monoclonal antibodies work by binding to both prions and normal proteins, blocking them from binding to each other.

Although the work is in its infancy and clinical studies with patients are some years away, the results raise the real possibility that a similar therapy might work on humans.