Abstract: The present invention provides antibodies that specifically bind with a high degree of binding affinity to a native ungulate PrPC and/or a denatured ungulate PrPSc, but not to a native ungulate PrPSc. Preferred antibodies find native bovine PrPC and treated PrPSc but not native bovine PrPSc and can be used in an assay to determine if a sample is infected with infectious prions, i.e. PrPSc.

Abstract: An assay method is disclosed which isolates and detects the presence of a disease related conformation of a protein (e.g., PrPSc) present in a sample also containing the non-disease related conformation of the protein (e.g., PrPSc). The sample is treated (e.g., contacted with protease) in a manner which hydrolyzes the disease related conformation and not the non-disease related conformation. The treated sample is contacted with a binding partner (e.g., a labeled antibody which binds PrPSc) and the occurrence of binding provides and indication that PrPSc is present. Alternatively the PrPSc of the treated sample is denatured (e.g., contacted with guanadine) or unfolded. The unfolded PrPSc is contacted with a binding partner and the occurrence of binding indicates the presence of PrPSc in the sample.

Abstract: An assay method is disclosed which isolates and detects the presence of a disease related conformation of a protein (e.g., PrPSc) present in a sample also containing the non-disease related conformation of the protein (e.g., PrPC). The sample is treated (e.g., contacted with protease) in a manner which hydrolyzes the disease related conformation and not the non-disease related conformation. The treated sample is contacted with a binding partner (e.g., a labeled antibody which binds PrPSc) and the occurrence of binding provides and indication that PrPSc is present. Alternatively the PrPSc of the treated sample is denatured (e.g., contacted with guanadine) or unfolded. The unfolded PrPSc is contacted with a binding partner and the occurrence of binding indicates the presence of PrPSc in the sample.

Abstract: The present invention provides assays for identifying the levels of both protease sensitive and protease resistant conformers of PrPSc in a sample. In a preferred embodiment, the assay comprises determining levels of total PrPSc in a sample, subjecting the PrPSc fraction to treatment with a protease that selectively hydrolyzes the protease sensitive PrPSc (sPrPSc) conformers, and quantifying the levels of sPrPSc in the sample. The ability to detect sPrPSc allows early detection of prions, since the PrPSc in easily accessible biological samples such as blood is predominantly sPrPSc. The ratio of sPrPSc to rPrPSc also allows the identification of a particular prion strain in an infected sample.

Abstract: The present invention provides assays for identifying the levels of both protease sensitive and protease resistant conformers of PrPSc in a sample. In a preferred embodiment, the assay comprises determining levels of total PrPSc in a sample, subjecting the PrPSc fraction to treatment with a protease that selectively hydrolyzes the protease sensitive PrPSc (sPrPSc) conformers, and quantifying the levels of sPrPSc in the sample. The ability to detect sPrPSc allows early detection of prions, since the PrPSc in easily accessible biological samples such as blood is predominantly sPrPSc. The ratio of sPrPSc to rPrPSc also allows the identification of a particular prion strain in an infected sample.

Abstract: The present invention provides antibodies that specifically bind with a high degree of binding affinity to a native ungulate PrPC and/or a denatured ungulate PrPSc, but not to a native ungulate PrPSc. Preferred antibodies find native bovine PrPC and treated PrPSc but not native bovine PrPSc and can be used in an assay to determine if a sample is infected with infectious prions, i.e. PrPSc.