Limited information is available about conformational differences between the abnormal isoform of prion protein (PrPSc) and cellular prion protein (PrPC) under native conditions. To clarify conformational differences between these two isoforms, PrP-deficient mice were immunized with brain homogenates of normal and scrapie-infected animals. All mice generated anti-PrP antibodies. Peptide array analysis of these serum samples revealed a distinctive epitope of PrPSc consisting of QGSPGGN (PrP41-47) at the N-terminus. This study demonstrated a conformational dissimilarity at the N-terminus between PrPSc and PrPC, a finding that may provide novel information about conformational features of PrPSc. © 2013 The Societies and Wiley Publishing Asia Pty Ltd 57 11 November 2013 10.1111/1348-0421.12105 Note Note Virology © 2013 The Societies and Wiley Publishing Asia Pty Ltd.
CITATION STYLE
Ushiki-Kaku, Y., Iwamaru, Y., Masujin, K., Imamura, M., Itohara, S., Ogawa-Goto, K., … Yokoyama, T. (2013, November). Different antigenicities of the N-terminal region of cellular and scrapie prion proteins. Microbiology and Immunology. https://doi.org/10.1111/1348-0421.12105
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