A conformational transition at the N terminus of the prion protein features in formation of the scrapie isoform Article

Peretz, D, Williamson, RA, Matsunaga, Y et al. (1997). A conformational transition at the N terminus of the prion protein features in formation of the scrapie isoform . JOURNAL OF MOLECULAR BIOLOGY, 273(3), 614-622. 10.1006/jmbi.1997.1328

cited authors

  • Peretz, D; Williamson, RA; Matsunaga, Y; Serban, H; Pinilla, C; Bastidas, RB; Rozenshteyn, R; James, TL; Houghten, RA; Cohen, FE; Prusiner, SB; Burton, DR

authors

abstract

  • The scrapie prion protein (PrP(Sc)) is formed from the cellular isoform (PrP(C)) by a post-translational process that involves a profound conformational change. Linear epitopes for recombinant antibody Fab fragments (Fabs) on PrP(C) and on the protease-resistant core of PrP(Sc), designated PrP 27-30, were identified using ELISA and immunoprecipitation. An epitope region at the C terminus was accessible in both PrP(C) and PrP 27-30; in contrast, epitopes towards the N-terminal region (residues 90 to 120) were accessible in PrP(C) but largely cryptic in PrP 27-30. Denaturation of PrP 27-30 exposed the epitopes of the N-terminal domain. We argue from our findings that the major conformational change underlying PrP(Sc) formation occurs within the N-terminal segment of PrP 27-30.

publication date

  • October 31, 1997

published in

Digital Object Identifier (DOI)

start page

  • 614

end page

  • 622

volume

  • 273

issue

  • 3