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Journal of Virology, April 2004, p. 3654-3662, Vol. 78, No. 7
0022-538X/04/$08.00+0     DOI: 10.1128/JVI.78.7.3654-3662.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Comparative Molecular Analysis of the Abnormal Prion Protein in Field Scrapie Cases and Experimental Bovine Spongiform Encephalopathy in Sheep by Use of Western Blotting and Immunohistochemical Methods

Stéphane Lezmi,1 Stuart Martin,2 Stéphanie Simon,3 Emmanuel Comoy,4 Anna Bencsik,1 Jean-Philippe Deslys,4 Jacques Grassi,3 Martin Jeffrey,2 and Thierry Baron1*

Agence Française de Sécurité Sanitaire des Aliments, Unité Virologie-ATNC, 69364 Lyon Cedex 07,1 CEA, Service de Pharmacologie et d'Immunologie, CEA/Saclay, 91191 Gif sur Yvette Cedex,3 CEA, GIDTIP/DRM/DSV, CEA/Fontenay aux Roses, Fontenay-aux-Roses, France,4 Veterinary Laboratory Agency, VLA Lasswade, Penicuik, Midlothian EH26 OPZ, United Kingdom2

Received 27 August 2003/ Accepted 10 December 2003

Since the appearance of bovine spongiform encephalopathy (BSE) in cattle and its linkage with the human variant of Creutzfeldt-Jakob disease, the possible spread of this agent to sheep flocks has been of concern as a potential new source of contamination. Molecular analysis of the protease cleavage of the abnormal prion protein (PrP), by Western blotting (PrPres) or by immunohistochemical methods (PrPd), has shown some potential to distinguish BSE and scrapie in sheep. Using a newly developed enzyme-linked immunosorbent assay, we identified 18 infected sheep in which PrPres showed an increased sensitivity to proteinase K digestion. When analyzed by Western blotting, two of them showed a low molecular mass of unglycosylated PrPres as found in BSE-infected sheep, in contrast to other naturally infected sheep. A decrease of the labeling by P4 monoclonal antibody, which recognizes an epitope close to the protease cleavage site, was also found by Western blotting in the former two samples, but this was less marked than in BSE-infected sheep. These two samples, and all of the other natural scrapie cases studied, were clearly distinguishable from those from sheep inoculated with the BSE agent from either French or British cattle by immunohistochemical analysis of PrPd labeling in the brain and lymphoid tissues. Final characterization of the strain involved in these samples will require analysis of the features of the disease following infection of mice, but our data already emphasize the need to use the different available methods to define the molecular properties of abnormal PrP and its possible similarities with the BSE agent.

* Corresponding author. Mailing address: AFSSA, Unité Virologie-ATNC, 31 avenue Tony Garnier, 69364 Lyon Cedex 07, France. Phone: 33(0)4 78 72 65 43. Fax: 33(0)4 78 61 91 45. E-mail: t.baron{at}lyon.afssa.fr.

Journal of Virology, April 2004, p. 3654-3662, Vol. 78, No. 7
0022-538X/04/$08.00+0     DOI: 10.1128/JVI.78.7.3654-3662.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



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