|Serban, Ana - UNIV CALIF SAN FRANCISCO|
|Safa, Jiri - UNIV CALIF SAN FRANCISCO|
|Prusiner, Stanley - UNIV CALIF SAN FRANCISCO|
Submitted to: Meeting Abstract
Publication Type: Abstract Only
Publication Acceptance Date: May 31, 2006
Publication Date: June 21, 2006
Citation: Stanker, L.H., Serban, A.V., Safa, J., Prusiner, S.B. 2006. Isolation and characterization of new anti-prp monoclonal antibodies. [Abstract]. ACS National Meeting and Exposition. Platform Presentation AGFD 199. Technical Abstract: The prion diseases (or transmissible spongiform encephalopathies) are fatal neurodegenerative illnesses caused by the accumulation of PrPSc, which is an alternatively folded isoform of the cellular prion protein (PrPC). These disorders are widespread and are found in humans (Creutzfeldt-Jakob disease), in sheep (scrapie), in elk and deer (chronic wasting disease), and in cattle (bovine spongiform encephalopathy) as well as in mink and cats. Detection of PrPSc commonly relies on immunochemical methods. In this study, we isolated antibodies that improved the performance of the conformation-dependent immunoassay (CDI) used to measure both the protease-resistant and -sensitive forms of PrPSc. Following immunization of Prnp-null mice, a multitiered screening strategy was developed and a panel of candidate antibodies identified. Monoclonal antibody binding to PrP from different species, to reduced versus non-reduced PrP, to synthetic peptides, and to denatured PrP suggest that antibodies with both continuous and discontinuous epitopes were isolated. At least one of the antibodies, F4-31, substantially improved performance of the CDI for detection of PrPSc in cattle.