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Dr Graham Jackson
Institute of Prion Diseases
Courtauld Building
Dr Graham Jackson profile picture
  • Programme Leader
  • MRC Prion Unit at UCL
  • UCL Institute of Prion Diseases
  • Faculty of Brain Sciences

I began my research towards a PhD with Professor Anthony Clarke at the University of Bristol to gain an understanding of the mechanisms that determine the acquisition of precise 3-dimensional protein conformations from linear polypeptide sequences. My work diversified from studying solvent effects to the role of chaperones, in particular the bacterial chaperonins cpn60 and cpn10, overturning the trivial concept that caperonins functioned to ‘fold’ proteins. My work showed they functioned in the reverse manner as so called ‘unfoldase’ enzymes in an energy dependent manner. I published my finding in 1993 and this paper remains a seminal paper in the field. Following a brief period of postdoctoral research on the catalytic mechanism of gibberellin C-20 oxidases I joined Professor Collinge’s Prion Disease Group at St Mary’s Hospital in 1996. I worked initially as a postdoctoral fellow with a wide range of activities which focused down to studying the structure and thermodynamics of the prion protein as a Programme Leader Track Scientist with the MRC. I have continued to contribute to research into prion disease and I now lead my own programme of research into novel diagnostic methods for use in prion disease and other protein conformational disorders.

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Research Summary
Prion disease remains a strategic priority area for both the Medical Research Council and the UK Department of Health and is increasingly recognised as a paradigm for other, if not all, neurodegenerative disease. The core mission of the MRC Prion Unit is to understand the molecular basis of prion propagation and to tackle the specific public health issues posed by BSE and vCJD in the UK. While our key focus on the basic science of prions and its wider potential relevance in pathobiology remains, we have developed an increasing translational activity. In particular the Unit has been working to develop effective means of prion sterilisation, early diagnosis, effective therapy and post-exposure prophylaxis. The arrival of blood transfusion-associated vCJD highlighted the need to advance blood-based diagnostics for prion infection. Further, the advances in therapeutics research in the Unit and the development of both conventional drugs and biopharmaceuticals for prion disease necessitates parallel advances in early diagnosis and progression biomarkers. Development of prion diagnostics is a formidable scientific challenge as prions are devoid of nucleic acid detectable by PCR or hybridisation and, being comprised of a ‘self’ protein highly expressed in the immune system, do not elicit a humoral immune response, so that the conventional methods to detect the presence of infectious agents are not applicable. Abnormal prion protein is an excellent disease marker but is present at very low levels and must be differentiated from a large excess of the normal host protein, with which it is chemically identical. My group has made significant advances on prion enrichment from whole blood using novel monoclonal antibodies and austenitic steel capture matrices which has led to the development of the first blood test for vCJD being made available to patients at the National Prion Clinic. A increasing area of effort is studying prion replication to develop synthetic reactions for amplification of the misfolded state. Such reactions are not only of enormous utility for diagnostic test and progression biomarker analysis but will provide fundamental information towards understanding prion propagation in vivo and how it may be slowed or blocked. Further the methods we have been using may be applicable to a range of other protein misfolding disorders and future work will aim to encompass a range of neurodegenerative diseases.
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