|Van Everbroeck, B. - UNIV OF ANTWERP,BELGIUM|
|Cras, P - UNIV OF ANTWERP,BELGIUM|
Submitted to: Eur J Histochem
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: January 19, 1999
Publication Date: April 1, 1999
Citation: Van Everbroeck, B., O'Rourke, K.I., Cras, P. 1999. Immunoreactivity of the monoclonal antibody F89/160.1.5 for the human prion protein. Eur. J. Histochem. 43(4):335-338. Interpretive Summary: Specialized, laboratory produced monoclonal antibodies are the reagent of choice for large scale surveillance for transmissible spongiform encephalopathies (prion diseases). In this study, the reactivity of two monoclonal antibodies for the marker protein PrP-Sc were analyzed. Reactivity to human TSE-positive tissues was equivalent. Mab F89/160.1.5 also reacts with TSE material from cattle, sheep, deer, and elk. The use of these commercially available antibodies in diagnostic and surveillance programs should increase the accuracy and reduce the cost of large scale programs.
Technical Abstract: Monoclonal antibodies (Mab) to the prion protein (PrP) are used for diagnosis and pathological characterization of the transmissible spongiform encephalopathies of humans and livestock. Although the target protein (PrP) is highly evolutionary conserved, sequence differences among the species may require different antibodies for diagnosis in different species. In this study, we analyzed monoclonal antibody F89/160.1.5 for reactivity with the human prion protein. This antibody binds an epitope conserved among humans, sheep, cattle, deer and elk. Immunohistochemical (IHC) analysis showed that this antibody is a highly sensitive (final concentration 55 ng/ml) and specific antibody for prion detection in humans and the reactivity did not different from that observed after staining with the well characterized antibody 3F4.