NR AWZO
AU Kuczius,T.; Grassi,J.; Karch,H.; Groschup,M.H.
TI Binding of N- and C-terminal anti-prion protein antibodies generates distinct phenotypes of cellular prion proteins (PrPc) obtained from human, sheep, cattle and mouse
QU The FEBS Journal 2007 Mar; 274(6): 1492-502
PT journal article; research support, non-u.s. gov't
AB 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 (PrPsc) of a host encoded prion protein (PrPc). PrPsc proteins are characterized according to size and glycoform pattern. We analyzed the glycoform patterns of PrPc 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 PrPc isoforms. Our data demonstrate the importance of antibody selection in characterization of PrPc.
MH Amino Acid Sequence; Animals; Antibodies/*immunology; Blotting, Western; Cattle; Glycosylation; Humans; Mice; Molecular Sequence Data; Phenotype; PrPc Proteins/chemistry/*immunology; Sequence Homology, Amino Acid; Sheep
AD Institute for Hygiene, University Hospital Münster, Robert Koch Strasse 41, 48149 Münster, Germany. tkuczius@uni-muenster.de
SP englisch
PO England