<span>Field of the invention: The present invention is directed to a method for identifying prion protein which is involved in various transmissible neurological disorders of the central nervous system (CNS) in both humans and animals. Specifically, the method is based on the use of hybridomas or monoclonal antibodies (Mabs) and/or epitope binding fragments thereof prepared against prion protein in order to detect the presence of prion diseases. These antibodies or fragments thereof are suitable for use in highly sensitive immuno-assays for demonstrating the presence of prion protein. Additionally, the invention is also directed to pharmaceutical compositions containing the antibodies or fragments thereof. Background of the invention: A prion is a small infectious protein. It is believed to be the cause of a number of degenerative neurological diseases. These prion caused diseases are collectively hereinafter referred to as "prion diseases".Prions were formerly called "slow viruses" but are now known to be devoid of nucleic acids and are, therefore, neither viruses nor viroids. The name prion is a contraction of the terms protein and infection. Prions are resistant to inactivation by procedures that modify nucleic acids. The membrane glycoprotein, now called prion protein (PrP), is involved in the pathogenesis of prion diseases. However, the normal function of PrP and its precise role in disease is not fully understood. It is believed that prion diseases are </span><span>associated with alterations in PrP. The PrP gene is generally expressed at high levels in neuronal cells of the brain and at lower levels in other tissue such as the heart, lung and spleen. Furthermore, studies indicate that prion diseases are associated with a build up of PrP in and around cells of the brain. Normal cellular prion protein is encoded by one single gene which can exist in multiple glycoforms with molecular masses existing between 27-40 K. Daltons. The glycoprotein is attached to the cell membrane of mammalian cells by a glycosyl phosphatidyl inositol (GPI) anchor. Prion caused diseases, or transmissible spongiform encephalopathies (TSE), are neurodegenerative disorders that affect both humans and animals. Prion diseases are referred to as sponiform encephalopathies due to the characteristic of forming holes or pores in cranial tissue. Development of prion disease may be the result of mutations in the PrP gene. Inherited prion diseases include; Creutzfeldt-Jakob disease (CJD), fatal familial insomnia (FFI) and Gerstmann-Straussler-Scheinker syndrome or disease (GSS) in humans. Prion diseases can also be contracted by an infectious mechanism. This group of diseases includes iatrogenic CJD and a new variant of CJD, which may be the result of transmission of bovine spongiform encephalopathy (BSE, also referred to as "Mad Cow" disease) from cattle to humans. The majority of the prion diseases are sporadic disorders.http://www.google.com/patents?vid=USPAT6528269</span>
