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Dr Jonathan Wadsworth
Room 101A
UCL Institute of Prion Diseases
Courtauld Building, 33 Cleveland Street
London
W1W 7FF
Appointment
  • Programme Leader
  • MRC Prion Unit at UCL
  • UCL Institute of Prion Diseases
  • Faculty of Brain Sciences
Biography


I studied Biochemistry at Imperial College London and was awarded a PhD in 1990 for work investigating the neuroparalytic activities of botulinum neurotoxins. My early post-doctoral work at the Royal Postgraduate Medical School, Hammersmith Hospital, London focused upon the pharmacology of neurotoxins from insect, snake and scorpion venoms. In 1997 I joined Professor John Collinge at Imperial College School of Medicine at St. Mary’s Hospital London to work on prion diseases and moved with Professor Collinge to UCL in 2001. I am currently a Programme Leader within the MRC Prion Unit at UCL and Reader in Prion Diseases in the UCL Institute of Prion Diseases.


Research Groups
Research Themes
Research Summary



Mammalian prions are unique pathogens and are composed of infectious polymeric assemblies of misfolded host-encoded prion protein which propagate by means of seeded protein polymerization. Different prion strains can propagate in the same host to produce different disease phenotypes and appear to be encoded by distinct pathogenic prion protein conformations and assembly states. Although historically rare in humans, the appearance of variant Creutzfeldt-Jakob disease (vCJD) in the UK from 1995 onwards, and the experimental confirmation that this was caused by dietary or other exposure to bovine spongiform encephalopathy (BSE) prions from cattle, has led to intense efforts to understand the fundamental details of prion pathogenesis in order to protect public health and to develop rational therapeutics.


My integrated series of research projects conducted within the MRC Prion Unit at UCL aim to define the molecular composition and 3D structure of infectious prions and elucidate the molecular basis of prion strain diversity. Achievement of an accurate classification system for human prion strains by defined molecular criteria will empower detailed aetiological and epidemiological studies and enable comprehensive evaluation of the relationship between the prion strains causing various forms of human disease with those causing animal prion diseases. Understanding these relationships will have direct translation to protecting public health.

 




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