Propagation of prions with artificial properties in transgenic mice expressingchimeric PrP genes
Article Abstract:
Transgenic mice with chimeric prior protein genes derived from Syrian hamster and mouse genes show, when constructed, that one Syrian hamster gene designated MH2M PrP contains five amino acid substitutions while another construct, designated MHM2 PrP, has possess two substitutions. Transgenic MH2M PrP mice were vulnerable to both Syrian hamster and mouse prions. Findings of the study support genetic evidence for homophilic intercourse between PrPSc in the inoculum and Prpc absorbed by the host.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1993
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Prion protein of 106 residues creates an artificial transmission barrier for prion replication in transgenic mice
Article Abstract:
A study was conducted to determine the minimal size and the number of N-terminal residues that can be deleted from transgenic mice's cellular prion proteins without inhibiting prion propagation. Results indicate that a redacted prion protein (PrP) of 106 amino acids with two deletions can still support prion propagation. Further studies revealed that removal of 50% of the residues of PrP will still allow prion propagation through its remaining polypeptides.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1999
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Prion propagation in mice expressing human and chimeric PrP transgenes implicates the interaction of cellular PrP with another protein
Article Abstract:
Prion formation involves a species-specific macromolecule, protein X. A region from codons 96 to 167 contains scrapie isoform prion protein bound to cellular prion protein. Residues near the C-terminus are involved in the binding of cellular prion protien to protein X. The role of molecular chaperon is probably played by protein X in the formation of scrapie isoform prion protein.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1995
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