Spontaneous conformational change within the prion protein--implications for disease pathogenesis?
A recent paper by Leclerc et al(1) describes how recombinant hamster prion protein can undergo a spontaneous change in conformation to a structure that has features in common with PrP(Sc). Structural change in the host prion protein, PrP(C) to an insoluble and aggregated form with increased beta-sheet content (PrP(Sc)) is central to the pathology of prion diseases.(2) A detailed understanding of the nature of these conformational changes will increase our knowledge of the molecular basis of prion pathology. These findings may have implications for how the disease is initiated and provide a format for further investigation.
Jackson
G S
GS
MRC Prion Unit, Department of Neurogenetics, Imperial College School of Medicine at St. Mary's, Norfolk Place, Paddington, London, W2 1NY, UK. g.s.jackson@ic.ac.uk
D000818:Animals; D018621:PrPC Proteins / Q000737:chemistry / Q000472:pathogenicity; D018620:PrPSc Proteins / Q000737:chemistry / Q000472:pathogenicity; D017096:Prion Diseases / Q000503:physiopathology*; D011328:Prions / Q000737:chemistry* / Q000472:pathogenicity*; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D011994:Recombinant Proteins / Q000737:chemistry; D012608:Scrapie / Q000503:physiopathology
D018621:PrPC Proteins; D018620:PrPSc Proteins; D011328:Prions; D011994:Recombinant Proteins