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Characterization of the murine BSE infectious agent

Laboratory of Pharmacology, Department of Pharmaceutical Sciences, School of Health Sciences, Aristotle University of Thessaloniki, Thessaloniki 540 06, Greece¹
Laboratory of Microbiology and Infectious Diseases, Department of Veterinary Sciences, Aristotle University of Thessaloniki, Thessaloniki 540 06, Greece²
Central Veterinary Laboratory, Addlestone, Surrey KT15 3NB, UK³

Author for correspondence: Theodoros Sklaviadis. Fax +3 031 997645. e-mail sklaviadis{at}auth.gr

Bovine spongiform encephalopathy (BSE) is a prion-associated disease where the infectious agent is thought to be a host-encoded protein with a protease-resistant conformation (PrP^Sc). Here, data are presented on the solubilization of purified murine BSE material, using guanidine–HCl as a denaturing agent. This treatment led to loss of infectivity, which was partially recovered on renaturation after dialysis to remove the chaotropic agent. The renatured product was then fractionated on an isopycnic sucrose-density gradient and the fractions were analysed for the presence of PrP^Sc, nucleic acids and infectivity. It was found that the major part of PrP^Sc (>90%) and the endogenous nucleic acids did not contribute towards the formation of infectious particles on renaturation. Infectivity was distributed in the top three, low-density fractions. Among these, the presence of considerable infectivity in the fraction of lowest density, with barely detectable PrP^Sc, is of particular interest.

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