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Different antigenicities of the N‐terminal region of cellular and scrapie prion proteins
Author(s) -
UshikiKaku Yuko,
Iwamaru Yoshifumi,
Masujin Kentaro,
Imamura Morikazu,
Itohara Shigeyoshi,
OgawaGoto Kiyoko,
Hattori Shunji,
Yokoyama Takashi
Publication year - 2013
Publication title -
microbiology and immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.664
H-Index - 70
eISSN - 1348-0421
pISSN - 0385-5600
DOI - 10.1111/1348-0421.12105
Subject(s) - scrapie , gene isoform , prion protein , epitope , biology , n terminus , c terminus , conformational epitope , peptide , antibody , microbiology and biotechnology , peptide sequence , virology , biochemistry , amino acid , immunology , gene , pathology , medicine , disease
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 .