The three-dimensional structure of healthy human prion protein, which becomes corrupted in the brains of sufferers of Creutz-feldt-Jakob disease, has been revealed for the first time, writes Steve Farrar.
The discovery is a significant step forward in understanding the deadly disease.
Swiss researchers at the Swiss Federal Institute of Technology in Zurich believe it could shed light on how rogue prion proteins operate in diseased individuals and might ultimately help pave the way to therapies to tackle the currently untreatable condition.
Prion proteins are normally present in brain cells and are not harmful. However, it is believed that when they become abnormally folded, they form insoluble clumps in the brain, causing neuronal damage and the degeneration of the central nervous system. The brain wastes away and the condition is always fatal.
The two prion forms are chemically identical but differ in their form. The Swiss advance will help experts study how diseases such as CJD and BSE progress.
The team, lead by Professor Kurt Wuethrich, had previously decoded the three-dimensional structure of a mouse's prion protein in 1997.
Latest figures from the UK Department of Health record 49 deaths from vCJD, the form of the disease that has been linked with BSE in cattle, up to November 1999.