NR ACJK
AU Caughey,B.W.
TI Formation of protease-resistant prion protein in cell-free systems
QU Current Issues in Molecular Biology 2000 Jul; 2(3): 95-101
PT journal article; review; review, tutorial
AB In transmissible spongiform encephalopathies (TSE) or prion diseases, the endogenous protease-sensitive prion protein (PrP-sen) of the host is converted to an abnormal pathogenic form that has a characteristic partial protease resistance (PrPres). Studies with cell-free reactions indicate that the PrPres itself can directly induce this conversion of PrP-sen. This PrPres induced conversion reaction is highly specific in ways that might account at the molecular level for TSE species barriers, polymorphism barriers, and strains. Not only has this reaction been observed using mostly purified PrP-sen and PrPres reactants, but also in TSE-infected brain slices. The conversion mechanism appears to involve both the binding of PrP-sen to polymeric PrPres and a conformational change that results in incorporation into the PrPres polymer.
ZR 81
MH Animal; Brain/metabolism; Cell-Free System; Drug Resistance; Endopeptidases; Human; In Vitro; Macromolecular Systems; Molecular Biology/methods; Polymorphism (Genetics); Prion Diseases/etiology/genetics/metabolism; Prions/*biosynthesis/chemistry/genetics; Protein Binding; Protein Conformation; Scrapie/etiology/genetics/metabolism; Species Specificity
AD Rocky Mountain Laboratories, National Institute of Allergy and Infectious Diseases, Hamilton, MT 59840, USA
SP englisch
PO England