Immunoreactivity of the monoclonal antibody F89/160.1.5 for the human prion protein.
Monoclonal antibodies (Mab) to the prion protein (PrP) have been critical to the neuropathological characterisation of PrP-related diseases in human and animals. Although PrP is highly evolutionary conserved, there is some sequence divergence among species. We have analysed the F89/160.1.5 Mab raised against the bovine prion protein for immunoreactivity with the human prion protein. The antibody recognised the IHFG epitope of the prion protein. An analysis of the Swiss Prot database confirmed conservation of the epitope in humans. Further immunohistochemical (IHC) analysis showed a highly sensitive (final concentration 55 ng/ml) and specific antibody for prion detection in humans. The observed immunoreactivity of the prion protein did not differ from that observed after staining with the well-known 3F4 (Senetek) monoclonal antibody.
Van Everbroeck
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Laboratory of Neurobiology, Born Bunge Foundation, University of Antwerp, Wilrijk, Belgium.
O'Rourke
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Cras
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D000818:Animals; D000911:Antibodies, Monoclonal / Q000378:metabolism*; D000937:Antigen-Antibody Reactions; D002417:Cattle; D007562:Creutzfeldt-Jakob Syndrome / Q000276:immunology / Q000378:metabolism; D000939:Epitopes / Q000276:immunology; D006801:Humans; D007150:Immunohistochemistry; D011328:Prions / Q000276:immunology*; D013194:Staining and Labeling
D000911:Antibodies, Monoclonal; D000939:Epitopes; D011328:Prions