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SUMMARY:Prion propagation and neurotoxicity - Prof. John Collinge\, UCL 
DTSTART:20150219T161500Z
DTEND:20150219T180000Z
UID:TALK57235@talks.cam.ac.uk
CONTACT:Scientific Meetings Co-ordinator
DESCRIPTION:Prions are lethal pathogens causing neurodegenerative diseases
  in humans and other animals. They appear devoid of nucleic acid and compo
 sed of polymerised conformational isomers of host-encoded cellular prion p
 rotein. Their unique biology\, allied with the risks to public health pose
 d by prion zoonoses such as BSE\, has focussed much attention on understan
 ding the molecular basis of prion propagation and the “species barrier
 ” which controls cross-species transmission. Both are intimately linked 
 to understanding how multiple prion “strains” are encoded by a protein
 -only agent\, a challenging question in molecular biology which raises int
 riguing questions in evolution. It is increasingly clear that the underlyi
 ng mechanisms\, involving aggregation of a misfolded host protein\, are of
  much wider relevance in commoner neurodegenerative diseases. Recent advan
 ces suggest that prions themselves may not be directly neurotoxic\, but ra
 ther their propagation leads to production of toxic species which may be u
 ncoupled from infectivity. A general protein-only model\, developed to enc
 ompass prion strains and toxicity\, may be of wider significance. Effectiv
 e treatments for prion infection have been established and clinical trials
  are now being planned. In addition\, emerging evidence suggests that the 
 cellular prion protein may have a direct role in mediating aspects of neur
 otoxicity in Alzheimer’s disease which may allow common therapeutic appr
 oaches.
LOCATION:Max Perutz Lecture Theatre\, Medical Research Council (MRC) (MRC 
 Laboratory of Molecular Biol
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