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Brain Advance Access originally published online on June 23, 2003
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Brain, Vol. 126, No. 9, 2065-2073, September 2003
© 2003 Guarantors of Brain
doi: 10.1093/brain/awg205

Regional heterogeneity of cellular prion protein isoforms in the mouse brain

Vincent Beringue*,1,2, Gary Mallinson1,2, Maria Kaisar1,2, Mourad Tayebi1,2, Zahid Sattar1,2, Graham Jackson3, David Anstee4, John Collinge2,3 and Simon Hawke1,2

1 CNS Infection and Immunity Group and 2 Department of Neurogenetics, Imperial College, 3 MRC Prion Unit, Institute of Neurology, University College, London, and 4 IBGRL, National Blood Service, Bristol, UK

Correspondence to: Dr Simon Hawke, CNS Infection and Immunity Group, Department of Neurogenetics, Imperial College Faculty of Medicine, Norfolk Place, London W2 1PG, UK E-mail: s.hawke{at}imperial.ac.uk*Present address: Virologie et Immunologie Moléculaires, Institut National de la Recherche Agronomique, Jouy-en-Josas, France

Prion diseases are a group of invariably fatal neurodegenerative disorders that include Creutzfeldt–Jakob disease in humans, scrapie in sheep and goats, and bovine spongiform encephalopathy in cattle. The infectious agent or prion is largely composed of an abnormal isoform (PrPSc) of a host encoded normal cellular protein (PrPc). The conversion of PrPc to PrPSc is a dynamic process and, for reasons that are not clear, the distribution of spongiform change and PrPSc deposition varies among prion strains. An obvious explanation for this would be that the transformation efficiency in any given brain region depends on favourable interactions between conformations of PrPc and the prion strain being propagated within it. However, identification of specific PrPc conformations has until now been hampered by a lack of suitable panels of antibodies that discriminate PrPc subspecies under native conditions. In this study, we show that monoclonal antibodies raised against recombinant human prion protein folded into {alpha} or ß conformations exhibit striking heterogeneity in their specificity for truncations and glycoforms of mouse brain PrPc. We then show that some of these PrPc isoforms are expressed differentially in certain mouse brain regions. This suggests that variation in the expression of PrPc conformations in different brain regions may dictate the pattern of PrPSc deposition and vacuolation, characteristic for different prion strains.


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