NR AVOY
AU Picard-Hagen,N.; Gayrard,V.; Viguie,C.; Moudjou,M.; Imbs,C.; Toutain,P.L.
TI Prion protein in the cerebrospinal fluid of healthy and naturally scrapie-affected sheep
QU Journal of General Virology 2006 Dec; 87(12): 3723-7
PT comparative study; journal article; research support, non-u.s. gov't
AB The aim of this study was to characterize the cerebrospinal fluid (CSF) prion protein (PrP) of healthy and naturally scrapie-affected sheep. The soluble form of CSF PrPc immunoblotted with an anti-octarepeat and an anti-C terminus mAb showed two isoforms of approximately 33 and 26 kDa, corresponding to the biglycosylated and unglycosylated isoforms of brain PrPc. Neither the mean concentration nor the electrophoretic profile of CSF PrP differed between healthy and scrapie-affected sheep, whereas a slightly increased resistance of CSF PrP to mild proteolysis by proteinase K was evident in the CSF of scrapie-affected sheep. No difference in susceptibility to proteolysis was observed between the two ARR and VRQ genetic variants of the purified prokaryote recombinant PrP. It was concluded that the physicochemical properties of PrPc in the CSF could be altered during scrapie and that these changes might reflect the physiopathological process of prion disease.
MH Animals; Antibodies, Monoclonal/immunology; Blotting, Western; Electrophoresis, Polyacrylamide Gel; Endopeptidase K/metabolism; Molecular Weight; PrPc Proteins/*cerebrospinal fluid/metabolism; Protein Isoforms; Scrapie/*cerebrospinal fluid; Sheep
AD UMR 181 Physiopathologie et Toxicologie Experimentales INRA/ENVT, Ecole Nationale Veterinaire de Toulouse, 23 chemin des Capelles, 31076 Toulouse, France.
SP englisch
PO England