Prion infection is a worry with beef in the human food chain. This rather
esoteric paper is an important step in the detection of this threat to human
well being.,

Privat et al 2008 Human prion diseases: from antibody screening to a standardized
fast immunodiagnosis using automation. Modern Pathology vol 21, 140-149

Demopstration of pathological prion protein accumulation in the central nervous system is required to establish the diagnosis of transmissible subacute encephalopathies. In humans, this is frequently achieved using prion protein immunohistochemistry in paraffin -embedded tissue, a technique that requires multiple epitope retrieval and denaturing pretreatments. In addition to being time-consuming this procedure induces tissue alterations that preclude accurate morphological examination. The aim of the study described in this paper was to simplify prion protein immunohistochemistry procedure in human tissue, together with increased sensitivity and specificity. A panel of 50 monoclonal antibodies were produced using various immunugens ( human and ovine recombinant prion protein, prion protein peptides. denatured scrapie associated fibrils from 263K-infected Syrian hamsters) and directed against different epitopes along the human prion protein sequence. A panel of different forms of genetic, infectious and sporadic transmissible subacute encephalopathies was assessed. The monoclonal 12F10 antibody provided a high specificity and fast immunodiagnosis with very limited denaturing pretreatments. A standardized and reliable fast imnmnostaining procedure was established using an automated diagnostic system and allowed prion protein detection in the- central nervous system and in tonsil biopsies. It was evaluated in a series of 300 patients with a suspected d iagnosis of transmissible subacute transmissible encephalopaties and showed high sensitivity.

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