Abstract
Objective To study the distribution of disease-associated prion protein (PrP) in oral and dental tissues in variant CJD. Design Prospective single centre autopsy based study. Setting Within the National CJD Surveillance Unit, UK, 2000–2002. Materials and methods Patients with suspected variant CJD undergoing autopsy where permission to remove tissues for research purposes had been obtained from the relatives. Fixed and frozen autopsy tissues from the brain, trigeminal ganglion, alveolar nerve, dental pulp, gingiva, salivary gland, tongue and tonsils were studied by Western blot, PET blot and immunocytochemistry to detect disease-associated PrP. Results Disease-associated PrP was only detected in the brain, trigeminal ganglia and tonsils. Conclusions The failure to detect disease-associated PrP in most dental and oral tissues will help inform ongoing risk assessments for dental surgery in relation to the possible iatrogenic transmission of variant CJD via dental instruments.
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