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. © 2013 Landes Bioscience.