A novel, resistance-linked ovine PrP variant and its equivalent mouse variant modulate the in vitro cell-free conversion of rPrP to PrPres

Kirby, Louise and Goldmann, Wilfred and Houston, Fiona and Gill, Andrew C. and Manson, Jean C. (2006) A novel, resistance-linked ovine PrP variant and its equivalent mouse variant modulate the in vitro cell-free conversion of rPrP to PrPres. Journal of General Virology, 87 (12). pp. 3747-3751. ISSN 0022-1317

Full content URL: http://doi.org/10.1099/vir.0.82086-0

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Abstract

Prion diseases are associated with the conversion of the normal cellular prion protein, PrPc, to the abnormal, disease-associated form, PrPSc. This conversion can be mimicked in vitro by using a cell-free conversion assay. It has recently been shown that this assay can be modified to use bacterial recombinant PrP as substrate and mimic the in vivo transmission characteristics of rodent scrapie. Here, it is demonstrated that the assay replicates the ovine polymorphism barriers of scrapie transmission. In addition, the recently identified ovine PrP variant ARL168Q, which is associated with resistance of sheep to experimental BSE, modulates the cell-free conversion of ovine recombinant PrP to PrPres by three different types of PrPSc, reducing conversion efficiencies to levels similar to those of 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.

Keywords:prion protein, transmissible spongiform encephalopathies, Protein misfolding
Subjects:C Biological Sciences > C770 Biophysical Science
C Biological Sciences > C760 Biomolecular Science
Divisions:College of Science
ID Code:29560
Deposited On:01 Dec 2017 09:29

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