Literature DB >> 24117858

Different antigenicities of the N-terminal region of cellular and scrapie prion proteins.

Yuko Ushiki-Kaku1, Yoshifumi Iwamaru, Kentaro Masujin, Morikazu Imamura, Shigeyoshi Itohara, Kiyoko Ogawa-Goto, Shunji Hattori, Takashi Yokoyama.   

Abstract

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) .
© 2013 The Societies and Wiley Publishing Asia Pty Ltd.

Entities:  

Keywords:  N-terminal region; abnormal isoform of prion protein; antigenicity; prion

Mesh:

Substances:

Year:  2013        PMID: 24117858     DOI: 10.1111/1348-0421.12105

Source DB:  PubMed          Journal:  Microbiol Immunol        ISSN: 0385-5600            Impact factor:   1.955


  1 in total

1.  Accumulation of cellular prion protein within β-amyloid oligomer plaques in aged human brains.

Authors:  Reisuke H Takahashi; Mayumi Yokotsuka; Minoru Tobiume; Yuko Sato; Hideki Hasegawa; Toshitaka Nagao; Gunnar K Gouras
Journal:  Brain Pathol       Date:  2021-02-23       Impact factor: 6.508

  1 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.