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. 2004 Jan;5(1):110-5.
doi: 10.1038/sj.embor.7400054.

Distinct molecular phenotypes in bovine prion diseases

Anne-Gaëlle Biacabe  1 , Jean-Louis Laplanche, Stephen Ryder, Thierry Baron
Affiliations

Distinct molecular phenotypes in bovine prion diseases

Anne-Gaëlle Biacabe et al. EMBO Rep. 2004 Jan.

Abstract

Bovine spongiform encephalopathy (BSE) in cattle, the most likely cause of variant Creutzfeldt-Jakob disease in humans, is thought to be caused by a unique infectious agent, with stable features, even when transmitted to other species. Here, we show the existence of an atypical molecular phenotype among cattle diagnosed with BSE in France. Following western blot analysis, three cases showed unusual features of the electrophoretic profiles of the protease-resistant prion protein (PrP(res)) accumulating in the brain. The PrP(res) patterns were similar in these three atypical cases, showing a higher molecular mass of unglycosylated PrP(res) and strong labelling by P4 monoclonal antibody compared to 55 typical BSE cases. This finding suggests either some phenotypic modifications of PrP(res) following infection by the BSE agent or the existence of alternative origins of such diseases in cattle.

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Figures

Figure 1
Figure 1
(A) Western blot detection of PrPres from proteinase K-treated and ultracentrifuged brain homogenates, using RB1 polyclonal antibody (105–120 bovine epitope). Atypical cattle-BSE cases (A1F and A2F) (lanes 3 and 5) show, as do scrapie experimentally infected cattle (CScr) (lane 1), a higher molecular mass of the unglycosylated bands (arrow), compared to typical cattle-BSE cases (TUK, lane 2; T1F, lane 4). Similar differences are also observed in sheep, between natural scrapie (SHNS) (lane 7) and experimental BSE (SHBSE) (lane 6). Brain equivalent quantities loaded per lane from lanes 1 to 7 are 2.4, 4.8, 38, 2.4, 38, 1.2 and 1.2 mg, respectively. (B) Mean molecular weights±standard deviations obtained for the di-, mono- and unglycosylated PrPres bands (A: atypical cattle BSE; T: typical cattle BSE; F: French isolate; UK: British isolate; SH: sheep).
Figure 2
Figure 2
Western blot detection of PrPres from proteinase K-treated and ultracentrifuged brain homogenates, using RB1 polyclonal antibody (105–120 bovine epitope) (A) or P4 monoclonal antibody (against the ovine PrP sequence that corresponds to the 97–112 amino acids in cattle) (B). Typical cattle-BSE cases from France (T1F, lane 2; T2F, lane 3) or the UK (TUK, lane 1) and atypical cattle-BSE cases (A1F, A2F, A3F: lanes 4, 5, 6, respectively); biotinylated marker (39.8, 29.0, 20.1 and 14.3 kDa bands) (lane 4). Note the position of the lower bands of PrPres detected with RB1 polyclonal antibody in atypical or typical BSE cases compared to the 20.1 kDa band of the biotinylated marker. Brain equivalent quantities loaded per lane are respectively 5.6, 22.4 and 2.8 mg from lanes 1–3 and 37, 56 and 56 mg from lanes 4–7.
Figure 3
Figure 3
Ratios of di- and monoglycocosylated PrPres detected by western blot with RB1 polyclonal antibody in atypical (A1F, A2F and A3F) and typical (T1F, T2F and TUK) cattle-BSE cases.
See this image and copyright information in PMC

References

    1. Asante EA, Linehan JM, Desbrulais M, Joiner S, Gowland I, Wood AL, Welch J, HIll AF, Wadsworth JDF, Collinge J (2002) BSE prions propagate as either variant CJD-like or sporadic CJD-like prion strains in transgenic mice expressing human prion protein. EMBO J 21: 6358–6366 - PMC - PubMed
    1. Baron T (2002) Identification of inter-species transmission of prion strains. J Neuropathol Exp Neurol 61: 377–383 - PubMed
    1. Baron TGM, Biacabe A-G (2001) Molecular analysis of the abnormal prion protein during coinfection of mice by the bovine spongiform encephalopathy agent. J Virol 75: 107–114 - PMC - PubMed
    1. Baron TGM, Betemps D, Groschup MH, Madec JY (1999a) Immunological characterisation of the sheep prion protein expressed as fusion proteins in Escherichia coli. FEMS Immunol Med Microbiol 25: 379–384 - PubMed
    1. Baron TGM, Madec J-Y, Calavas D (1999b) Similar signature of the prion protein in natural sheep scrapie and bovine spongiform encephalopathy-linked diseases. J Clin Microbiol 37: 3701–3704 - PMC - PubMed