Different antigenicities of the N‐terminal region of cellular and scrapie prion proteins. (November 2013)

• Record Type: Journal Article
• Authors: Ushiki‐Kaku, Yuko; Iwamaru, Yoshifumi; Masujin, Kentaro; Imamura, Morikazu; Itohara, Shigeyoshi; Ogawa‐Goto, Kiyoko; Hattori, Shunji; Yokoyama, Takashi
• Is Part Of: Microbiology and immunology. Volume 57:Number 11(2013:Nov.)
• Page Start: 792
• Page End: 796
• Publication Date: 2013-11
• Subjects: Microbiology -- Periodicals; Immunology -- Periodicals; Allergy and Immunology -- Periodicals; Microbiology -- Periodicals; Microbiologie -- Périodiques; Immunologie -- Périodiques; 579
• DOI: 10.1111/1348-0421.12105
• Languages: English
• ISSNs: 0385-5600

Abstract

<abstract abstract-type="main" xml:lang="en"> <title>ABSTRACT</title> <sec id="mim12105-sec-0001" sec-type="section"> <p>Limited information is available about conformational differences between the abnormal isoform of prion protein (PrP^Sc) and cellular prion protein (PrP^C) 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 PrP^Sc consisting of QGSPGGN (PrP41–47) at the N‐terminus. This study demonstrated a conformational dissimilarity at the N‐terminus between PrP^Sc and PrP^C, a finding that may provide novel information about conformational features of PrP^Sc.</p> </sec> </abstract>