Graham Jackson
Graham Jackson
Molecular diagnostic strategies in prion disease and related neurodegnerative disorders

Graham began his research career at the University of Bristol with a PhD in Biochemistry. His early research focused upon the mechanisms of protein folding; both spontaneous and assisted with a particular interest in the catalytic cycle of the bacterial chaperonin system.

He joined the nascent Prion Disease Group at St Mary’s Hospital, London in 1996 and continued to work with Professor John Collinge after the formation of the MRC’s Prion Unit in 1999. Graham is currently an MRC Programme Leader at the Prion Unit and a Reader in Biochemistry within the Department of Neurodegenerative Disease at the UCL Institute of Neurology. His past work has centred around the structure and stability of the normal form of the human prion protein and in particular the ability of the protein to interact with and bind metal ions such as copper and zinc. Graham’s current research focus is to develop and validate novel methods for diagnosing prion disease from blood and urine samples..

Prion disease is defined by a characteristic change that occurs to the normal prion protein and the detection of this altered protein or PrPSc prion can be used to show someone has CJD. Unfortunately the amounts of PrPSc or prion are very low in easily obtained samples such as blood and urine, and are difficult to tell apart from the large amounts of the normal protein that are always present in both healthy and infected people. A key achievement of my group has been the first demonstration of the ability to detect vCJD infection in patient blood samples and the development of a highly accurate blood test that exploits the ability of prions to bind to metals. Critical to the utility and benefit of a test for vCJD is the accuracy of the assay. Any significant number of wrong results would outweigh the benefits of detecting CJD. By testing thousands of blood samples provided by the American Red Cross from healthy blood donors and hundreds of samples from patients with other neurological diseases we have established that our blood test is absolutely specific for prion disease.


We are particularly interested in the possibility of determining when and if individuals at risk of prion disease may develop disease symptoms. To achieve this we are trying different ways of detecting the rare altered form of the prion protein which accumulates as structured deposits in affected tissues. One approach is to copy the way the prion reproduces itself in the human body during disease. This allows us to ‘amplify’ the very small amounts of prion in patient samples into large amounts that can be easily detected using conventional laboratory tests. In doing so we are also gaining insights into the fundamental processes of prion replication that distinguish this particular protein misfolding event from those involved in other diseases that produce very similar aggregated proteins that do not infect others.