NR AXPY
AU Kirby,L.; Goldmann,W.; Houston,F.; Gill,A.
TI A Novel Resistance-linked Ovine PrP Variant and Its Equivalnet Mouse Variant Modulate the in Vitro Cell-Free Conversion of rPrP to PrPres
QU International Conference - Prion 2007 (26.-28.9.2007) Edinburgh International Conference Centre, Edinburgh, Scotland, UK - Book of Abstracts: Protein Misfolding P01.27
IA http://www.prion2007.com/pdf/Prion Book of Abstracts.pdf
PT Konferenz-Poster
AB Prion diseases are associated with the conversion of the normal cellular prion protein, PrPc, to the abnormal disease associated PrPsc. This conversion can be mimicked in vitro using the cell-free conversion assay. This assay can be modified to use bacterial recombinant PrP as a substrate and mimic the in vivo transmission characteristics of rodent scrapie. Here we demonstrate that the assay replicates the ovine polymorphism barriers of scrapie transmission. In addition, the recently identified ovine PrP variant ARL168Q, which is associated with increased survival of sheep to experimental BSE, modulates the cell-free conversion of ovine recombinant PrP to PrPres by 3 different types of PrPsc, reducing conversion efficiencies to levels similar to the ovine resistance-associated ARR variant. Also, the equivalent variant in mice (L164) is resistant to conversion by 87V scrapie. Together these results suggest a significant role for this position and/or amino acid in conversion.
AD L. Kirby, W. Goldmann, F. Houston, A. Gill, NPU, Roslin, TSE, UK
SP englisch
PO Schottland