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Prion protein in the cerebrospinal fluid of healthy and naturally scrapie-affected sheep

¹ UMR 181 Physiopathologie et Toxicologie Expérimentales INRA/ENVT, Ecole Nationale Vétérinaire de Toulouse, 23 chemin des Capelles, 31076 Toulouse, France
² Unité de Virologie et Immunologie Moléculaires, INRA, 78352 Jouy en Josas, France

Correspondence
Pierre-Louis Toutain
pl.toutain{at}envt.fr

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 PrP^C 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 PrP^C. 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 PrP^C in the CSF could be altered during scrapie and that these changes might reflect the physiopathological process of prion disease.

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