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Journal of Clinical Microbiology, June 2007, p. 1821-1829, Vol. 45, No. 6
0095-1137/07/$08.00+0     doi:10.1128/JCM.00160-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Molecular Discrimination of Atypical Bovine Spongiform Encephalopathy Strains from a Geographical Region Spanning a Wide Area in Europe ^,

Central Institute for Animal Disease Control (CIDC-Lelystad), 8203 AA 2004, Lelystad, The Netherlands,¹ Agence Française de Sécurité Sanitaire des Aliments (AFSSA-Lyon Fr), Unité ATNC, 31 avenue Tony Garnier, 69342 Lyon cedex 07, France,² Centro di Referenza per le Encefalopatie Animali (CEA), Istituto Zooprofilattico Sperimentale del Piemonte, Liguria e Valle d'Aosta, Via Bologna 148, 10154 Turin, Italy,³ National Veterinary Research Institute (NVRI), Al. Partyzantow 57, 24-100 Pulawy, Poland,⁴ National Veterinary Institute (SVA), SE-751 89 Uppsala, Sweden,⁵ Friedrich-Loeffler-Institut, Boddenblick 5a, 17493 Greifswald-Insel Riems, Germany⁶

Received 22 January 2007/ Returned for modification 12 March 2007/ Accepted 6 April 2007

Transmissible spongiform encephalopathy strains can be differentiated by their behavior in bioassays and by molecular analyses of the disease-associated prion protein (PrP) in a posttranslationally transformed conformation (PrP^Sc). Until recently, isolates from cases of bovine spongiform encephalopathy (BSE) appeared to be very homogeneous. However, a limited number of atypical BSE isolates have recently been identified upon analyses of the disease-associated proteinase K (PK) resistance-associated moiety of PrP^Sc (PrP^res), suggesting the existence of at least two additional BSE PrP^res variants. These are defined here as the H type and the L type, according to the higher and lower positions of the nonglycosylated PrP^res band in Western blots, respectively, compared to the position of the band in classical BSE (C-type) isolates. These molecular PrP^res variants, which originated from six different European countries, were investigated together. In addition to the migration properties and glycosylation profiles (glycoprofiles), the H- and L-type isolates exhibited enhanced PK sensitivities at pH 8 compared to those of the C-type isolates. Moreover, H-type BSE isolates exhibited differences in the binding of antibodies specific for N- and more C-terminal PrP regions and principally contained two aglycosylated PrP^res moieties which can both be glycosylated and which is thus indicative of the existence of two PrP^res populations or intermediate cleavage sites. These properties appear to be consistent within each BSE type and independent of the geographical origin, suggesting the existence of different BSE strains in cattle. The choice of three antibodies and the application of two pHs during the digestion of brain homogenates provide practical and diverse tools for the discriminative detection of these three molecular BSE types and might assist with the recognition of other variants.

Supplemental material for this article may be found at http://jcm.asm.org.

Published ahead of print on 18 April 2007.

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