Scientists make breakthrough in CJD detection
A breakthrough by Swiss researchers could make it possible to recognise the human from of mad cow disease from a blood sample.
At present, it can only be diagnosed by examining brain tissue either after death or from a surgically removed sample.
The discovery may also open up new avenues for identifying other similar diseases in animals, such as BSE in cattle and scrapie in sheep.
The family of transmissible spongiform encephalopathy diseases which includes vCJD and BSE are thought to be caused by abnormal ‘‘rogue’’ prion proteins.
A prion that has changed shape to make it dangerous causes other prions it comes in contact with to ‘‘turn bad’’ in a chain reaction.
The discovery from Claudio Soto and colleagues at the Serono Pharmaceutical Research Institute in Geneva shows that even a minute amount of rogue prion protein can convert large amounts of normal prion.
Abnormal prions are present in the blood and tissues other than the brain in such small amounts as to be undetectable.
But the new findings show that they could be revealed in the laboratory by causing large amounts of prion to be converted.
The ‘‘amplification’’ technique offers hope of detecting the agents of prion diseases when previously they would be invisible.
Silvano Fumero, a senior executive at Serano, said: ‘‘The procedure mimics the replication of abnormal prion proteins in the body in ‘fast forward’ mode, compressing years of real-life time into a few hours in the laboratory.
‘‘This is a major scientific breakthrough and has potential applications in improving tests for prion diseases, as well as identifying targets against which future drugs should be aimed.’’
The breakthrough was reported today in the scientific journal Nature.
It could lead to the identification of abnormal prion proteins in human vCJD victims by testing spinal fluid or blood, say the researchers.
