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Binding of N‐ and C‐terminal anti‐prion protein antibodies generates distinct phenotypes of cellular prion proteins (PrP C ) obtained from human, sheep, cattle and mouse
Author(s) -
Kuczius Thorsten,
Grassi Jacques,
Karch Helge,
Groschup Martin H
Publication year - 2007
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/j.1742-4658.2007.05691.x
Subject(s) - scrapie , gene isoform , antibody , prion protein , bovine spongiform encephalopathy , biology , phenotype , microbiology and biotechnology , monoclonal antibody , virology , biochemistry , immunology , gene , disease , pathology , medicine
Prion diseases are neurodegenerative disorders which cause Creutzfeldt–Jakob disease in humans, scrapie in sheep and bovine spongiform encephalopathy in cattle. The infectious agent is a protease resistant isoform (PrP Sc ) of a host encoded prion protein (PrP C ). PrP Sc proteins are characterized according to size and glycoform pattern. We analyzed the glycoform patterns of PrP C obtained from humans, sheep, cattle and mice to find interspecies variability for distinct differentiation among species. To obtain reliable results, the imaging technique was used for measurement of the staining band intensities and reproducible profiles were achieved by many repeated immunoblot analysis. With a set of antibodies, we discovered two distinct patterns which were not species‐dependent. One pattern is characterized by high signal intensity for the di‐glycosylated isoform using antibodies that bind to the N‐terminal region, whereas the other exhibits high intensity for protein bands at the size of the nonglycosylated isoform using antibodies recognizing the C‐terminal region. This pattern is the result of an overlap of the nonglycosylated full‐length and the glycosylated N‐terminal truncated PrP C isoforms. Our data demonstrate the importance of antibody selection in characterization of PrP C .