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 PrPSc. Structural change in the host prion protein, PrPC to an insoluble and aggregated form with increased β‐sheet content (PrPSc) 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 patholo…
Read moreA 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 PrPSc. Structural change in the host prion protein, PrPC to an insoluble and aggregated form with increased β‐sheet content (PrPSc) 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. BioEssays 23:772–774, 2001. © 2001 John Wiley & Sons, Inc.
