NR AWHX
AU Kirby,L.; Goldmann,W.; Houston,F.; Gill,A.; Manson,J.
TI A novel resistance-linked ovine PrP variant and its equivalent mouse variant modulate the in vitro cell-free conversion of rPrP to PrPres
QU International Conference - Prion 2006: Strategies, advances and trends towards protection of society - 3.10.-6.10.2006, Torino, Italy, Lingotto Conference Centre - Poster sessions GEN-15
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. We have recently shown that 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 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, F. Houston, A. Gill: Institute for Animal Health, Compton Laboratories, Newbury, Berkshire, RG20 7NN, UK; W. Goldmann, J. Manson: Neuropathogenesis Unit, Institute for Animal Health, Ogston Building, West Mains Road, Edinburgh, EH9 3JF, UK. E-mail: Louise.kirby@bbsrc.ac.uk
SP englisch
PO Italien