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Application of an immunocapillary electrophoresis assay to the detection of abnormal prion protein in brain, spleen and blood specimens from patients with variant Creutzfeldt–Jakob disease

¹ National CJD Surveillance Unit, School of Molecular and Clinical Medicine, University of Edinburgh, Western General Hospital, Edinburgh EH4 2XU, UK
² Ames Laboratory, USDOE, Iowa State University, Ames, IA 500011, USA
³ SNBTS Products and Components R&D Group, National Science Laboratory, 21 Ellen's Glen Road, Edinburgh EH17 7QT, UK

Correspondence
Mark W. Head
m.w.head{at}ed.ac.uk

Sensitive and specific detection of abnormal prion protein in blood could provide a diagnostic test or screening assay for animal and human prion diseases. Here, the application of an immunocapillary electrophoresis (ICE) method developed for sheep scrapie to brain, spleen and blood from patients with Creutzfeldt–Jakob disease (CJD) is described. The assay involves organic-solvent extraction, a competitive immunoassay using fluorescently labelled synthetic prion protein peptides and polyclonal antibodies specific for those sequences, and analysis by capillary electrophoresis using laser-induced fluorescence detection. The test was evaluated by using clinical blood specimens from patients with variant (n=5) or sporadic (n=4) CJD and patients initially suspected of having CJD who were given an alternative diagnosis (n=6). In this context, the ICE assay was specific, but incompletely sensitive (55 %). The method was unable to detect abnormal prion protein in variant CJD brain or spleen reference materials due to its loss during the extraction process.

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