Unique structural properties associated with mouse prion Δ105–125 protein

Abstract

Murine prion protein deleted for residues 105–125 is intrinsically neurotoxic and mediates a TSE-like phenotype in transgenic mice. Equivalent and overlapping deletions were expressed in E.coli, purified and analyzed. Among mutants spanning the region 95–135, a construct lacking solely residues 105–125 had distinct properties when compared with the full-length prion protein 23–231 or other deletions. This distinction was also apparent followed expression in eukaryotic cells. Unlike the full-length protein, all deletion mutants failed to bind to synthetic membranes in vitro. These data suggest a novel structure for the 105–125 deleted variant that may relate to its biological properties.

Keywords: :

• E.coli
• baculovirus
• deletion
• expression
• folding
• hydrophobic
• murine PrP^C
• toxicity

Disclosure of Potential Conflicts of Interest

No potential conflict of interest was disclosed.

Acknowledgments

A.P. was the grateful recipient of an MRC doctoral training award.