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

The scrapie prion protein (PrPSc) is formed from the cellular isoform (PrPC) by a post-translational process that involves a profound conformational change. Linear epitopes for recombinant antibody Fab fragments (Fabs) on PrPC and on the protease-resistant core of PrPSc, designated PrP 27-30, were i...

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Published inJournal of molecular biology Vol. 273; no. 3; pp. 614 - 622
Main Authors Peretz, D, Williamson, R A, Matsunaga, Y, Serban, H, Pinilla, C, Bastidas, R B, Rozenshteyn, R, James, T L, Houghten, R A, Cohen, F E, Prusiner, S B, Burton, D R
Format Journal Article
LanguageEnglish
Published England 31.10.1997
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Summary:The scrapie prion protein (PrPSc) is formed from the cellular isoform (PrPC) by a post-translational process that involves a profound conformational change. Linear epitopes for recombinant antibody Fab fragments (Fabs) on PrPC and on the protease-resistant core of PrPSc, designated PrP 27-30, were identified using ELISA and immunoprecipitation. An epitope region at the C terminus was accessible in both PrPC and PrP 27-30; in contrast, epitopes towards the N-terminal region (residues 90 to 120) were accessible in PrPC 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 PrPSc formation occurs within the N-terminal segment of PrP 27-30.
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ISSN:0022-2836
DOI:10.1006/jmbi.1997.1328