| abstract |
The present invention provides novel PrP proteins, and nucleic acids encoding the proteins, wherein the PrP proteins are 1) incomplete glycosylation relative to glycosylation of wild type PrP C and 2) suitable cell localization, ie transport to the cell surface. Is characterized in vivo. Unlike the normal cell counterparts of PrP, this novel low-glycosylated PrP can be converted to protease-resistant isoforms by incubation with infectious prions. Moreover, the present invention provides in vitro cell and animal systems for studying prion disorders and methods of using these systems, for example novel therapeutics for the study of mechanisms in prion-mediated disease progression or for the treatment of prion-mediated disorders. To provide a method of verification. In such a system, protease-resistant low-glycosylated PrP is newly generated and can be detected by standard immunoblot techniques. |