Premium
Spontaneous conformational change within the prion protein—implications for disease pathogenesis?
Author(s) -
Jackson Graham S.
Publication year - 2001
Publication title -
bioessays
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.175
H-Index - 184
eISSN - 1521-1878
pISSN - 0265-9247
DOI - 10.1002/bies.1112
Subject(s) - prion protein , conformational change , pathogenesis , hamster , disease , recombinant dna , biology , virology , medicine , genetics , immunology , biochemistry , microbiology and biotechnology , pathology , gene
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 β‐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. BioEssays 23:772–774, 2001. © 2001 John Wiley & Sons, Inc.