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

Abstract : 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 scrapieaffected 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.
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Déposant : Migration Prodinra <>
Soumis le : vendredi 29 mai 2020 - 22:37:04
Dernière modification le : mardi 25 août 2020 - 17:18:05

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Nicole Picard-Hagen, Véronique Gayrard, Catherine Viguié, Mohammed Moudjou, Chantal Imbs, et al.. Prion protein in the cerebrospinal fluid of healthy and naturally scrapie-affected sheep. Journal of General Virology, Microbiology Society, 2006, 87 (12), pp.3723-3727. ⟨10.1099/vir.0.81859-0⟩. ⟨hal-02655586⟩



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