Emerging Infectious Disease ISSN: 1080-6059

Molecular Typing of Protease-Resistant Prion Protein in Transmissible Spongiform Encephalopathies of Small Ruminants, France, 2002–2009

Johann Vulin, Anne-Gaëlle Biacabe, Géraldine Cazeau, Didier Calavas, and Thierry Baron

Author affiliations: Author affiliation: Agence Nationale de Sécurité Sanitaire, Lyon, France

Figure 2

Molecular mass obtained for the di-, mono-, and unglycosylated protein bands (A–C) and the glycoform proportions (D–F) between the diglycosylated band and the monoglycosylated band of the protease-resistant prion protein of the reference transmissible spongiform encephalopathies isolates (A, D), CH1641-like isolates in sheep (B, E), and unusual isolates in goats (C, F). Results were obtained from immunoblots detected by Bar233 antibody. BSE, bovine spongiform encephalopathy.

Figure 2. Molecular mass obtained for the di-, mono-, and unglycosylated protein bands (A–C) and the glycoform proportions (D–F) between the diglycosylated band and the monoglycosylated band of the protease-resistant prion protein of the reference transmissible spongiform encephalopathies isolates (A, D), CH1641-like isolates in sheep (B, E), and unusual isolates in goats (C, F). Results were obtained from immunoblots detected by Bar233 antibody. BSE, bovine spongiform encephalopathy.

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