Prevalence of lymphoreticular prion protein accumulation in UK tissue samples
Article first published online: 21 MAY 2004
Copyright © 2004 Pathological Society of Great Britain and Ireland. Published by John Wiley & Sons, Ltd.
The Journal of Pathology
Volume 203, Issue 3, pages 733–739, July 2004
How to Cite
Hilton, D. A., Ghani, A. C., Conyers, L., Edwards, P., McCardle, L., Ritchie, D., Penney, M., Hegazy, D. and Ironside, J. W. (2004), Prevalence of lymphoreticular prion protein accumulation in UK tissue samples. J. Pathol., 203: 733–739. doi: 10.1002/path.1580
- Issue published online: 21 JUN 2004
- Article first published online: 21 MAY 2004
- Manuscript Accepted: 22 MAR 2004
- Manuscript Revised: 15 MAR 2004
- Manuscript Received: 19 FEB 2004
- UK Department of Health. Grant Numbers: 1216963, 1216982
- Creutzfeldt-Jakob disease (CJD);
This study aims to provide an estimate of the number of individuals in the UK who may be incubating variant Creutzfeldt-Jakob disease and at risk of causing iatrogenic spread of the disease. Lymphoreticular accumulation of prion protein is a consistent feature of variant Creutzfeldt-Jakob at autopsy and has also been demonstrated in the pre-clinical phase. Immunohistochemical accumulation of prion protein in the lymphoreticular system remains the only technique that has been shown to predict neurological disease reliably in animal prion disorders. In this study, immunohistochemistry was used to demonstrate the presence of prion protein, with monoclonal antibodies KG9 and 3F4, in surgically removed tonsillectomy and appendicectomy specimens. The samples were collected from histopathology departments across the UK and anonymised prior to testing. Samples were tested from 16 703 patients (14 964 appendectomies, 1739 tonsillectomies), approximately 60% of whom were from the age group 20–29 years at operation. Twenty-five per cent of the samples were excluded from the final analyses because they contained inadequate amounts of lymphoid tissue. Three appendicectomy samples showed lymphoreticular accumulation of prion protein, giving an estimated prevalence of 3/12 674 or 237 per million (95% CI 49–692 per million). The pattern of lymphoreticular accumulation in two of these samples was dissimilar from that seen in known cases of variant Creutzfeldt-Jakob disease. Although it is uncertain whether immunohistochemical accumulation of prion protein in the lymphoreticular system is specific for variant Creutzfeldt-Jakob disease, it has not been described in any other disease, including other forms of human prion disease or a range of inflammatory and infective conditions. These findings reinforce the importance of measures taken by the UK Department of Health to reduce the risk of spread of variant Creutzfeldt-Jakob via blood products and surgical instruments, and of the urgency to proceed with large-scale screening of fresh tonsil specimens for the presence of prion protein. Copyright © 2004 Pathological Society of Great Britain and Ireland. Published by John Wiley & Sons, Ltd.