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This article describes a procedure which permits for the first time the isolation of the prion protein PrPc from the Syrian golden hamster in heterologous systems. Using a glutathione S-transferase (GST) fusion approach, milligram amounts of stable, soluble, and homogeneous GST::PrPc protein were obtained in Escherichia coli and with baculovirus-infected(More)
The crucial event in the development of transmissible spongiform encephalopathies (TSEs) is the conformational change of a host-encoded membrane protein - the cellular PrP(C) - into a disease associated, fibril-forming isoform PrP(Sc). This conformational transition from the alpha-helix-rich cellular form into the mainly beta-sheet containing counterpart(More)
Prion diseases are neurodegenerative disorders, affecting humans and animals. The human diseases include kuru, Creutzfeldt-Jakob disease (CJD), Gerstmann-Sträussler-Scheinker syndrome (GSS), and fatal familial insomnia (FFI). To generate monospecific antisera against human prion proteins we have immunized mice with DNA coding for different human prion(More)
The transmissible spongiform encephalopathies comprise a group of fatal neurodegenerative diseases that are characterized by the conversion of the normal host cellular prion protein (PrPC) to the abnormal protease-resistant isoform PrPSC. Distinct alterations of transcriptional regulation during disease progression could not be observed. The regulation of(More)
Erysipelothrix rhusiopathiae is a widely distributed mucosal commensal of the alimentary tracts of vertebrates. Antibodies to a 66-64 kDa protein released from the cell surface have been shown to be involved in protective immunity. Mice immunized with the purified 66-64 kDa protein from strain T28, serotype 2b were protected against challenge by the United(More)
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