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Journal of Virology, June 2004, p. 6243-6251, Vol. 78, No. 12
0022-538X/04/$08.00+0     DOI: 10.1128/JVI.78.12.6243-6251.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Molecular Analysis of the Protease-Resistant Prion Protein in Scrapie and Bovine Spongiform Encephalopathy Transmitted to Ovine Transgenic and Wild-Type Mice

Thierry Baron,1* Carole Crozet,1,{dagger} Anne-Gaëlle Biacabe,1 Sandrine Philippe,2 Jérémie Verchere,1 Anna Bencsik,1 Jean-Yves Madec,1 Didier Calavas,2 and Jacques Samarut3

Unité Agents Transmissibles Non Conventionnels,1 Unité Epidémiologie, Agence Française de Sécurité Sanitaire des Aliments—Lyon,2 Laboratoire de Biologie, Ecole Normale Supérieure de Lyon, Lyon, France3

Received 27 October 2003/ Accepted 4 February 2004

The existence of different strains of infectious agents involved in scrapie, a transmissible spongiform encephalopathy (TSE) of sheep and goats, remains poorly explained. These strains can, however, be differentiated by characteristics of the disease in mice and also by the molecular features of the protease-resistant prion protein (PrPres) that accumulates into the infected tissues. For further analysis, we first transmitted the disease from brain samples of TSE-infected sheep to ovine transgenic [Tg(OvPrP4)] and to wild-type (C57BL/6) mice. We show that, as in sheep, molecular differences of PrPres detected by Western blotting can differentiate, in both ovine transgenic and wild-type mice, infection by the bovine spongiform encephalopathy (BSE) agent from most scrapie sources. Similarities of an experimental scrapie isolate (CH1641) with BSE were also likewise found following transmission in ovine transgenic mice. Secondly, we transmitted the disease to ovine transgenic mice by inoculation of brain samples of wild-type mice infected with different experimental scrapie strains (C506M3, 87V, 79A, and Chandler) or with BSE. Features of these strains in ovine transgenic mice were reminiscent of those previously described for wild-type mice, by both ratios and by molecular masses of the different PrPres glycoforms. Moreover, these studies revealed the diversity of scrapie strains and their differences with BSE according to labeling by a monoclonal antibody (P4). These data, in an experimental model expressing the prion protein of the host of natural scrapie, further suggest a genuine diversity of TSE infectious agents and emphasize its linkage to the molecular features of the abnormal prion protein.

* Corresponding author. Mailing address: AFSSA-Lyon, 31 ave. Tony Garnier, 69364 Lyon cedex 07, France. Phone: 33-(0)4-78-69-68-33. Fax: 33-(0)4-78-61-91-45. E-mail: t.baron{at}lyon.afssa.fr.

{dagger} Present address: IGH UPR 1142 CNRS, Montpellier, France.

Journal of Virology, June 2004, p. 6243-6251, Vol. 78, No. 12
0022-538X/04/$08.00+0     DOI: 10.1128/JVI.78.12.6243-6251.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



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