Bovine prion protein as a modulator of protein kinase CK2

Abstract

On the basis of far-Western blot and plasmon resonance (BIAcore) experiments, we show here that recombinant bovine prion protein (bPrP) (25-242) strongly interacts with the catalytic α\αh subunits of protein kinase CK2 (also termed ' casein kinase 2 '). This association leads to increased phosphotransferase activity of CK2α, tested on calmodulin or specific peptides as substrate. We also show that bPrP counteracts the inhibition of calmodulin phosphorylation promoted by the regulatory β subunits of CK2. A truncated form of bPrP encompassing the Cterminal domain (residues 105-242) interacts with CK2 but does

Immunotherapeutic effect of anti-PrP monoclonal antibodies in transmissible spongiform encephalopathy mouse models: pharmacokinetic and pharmacodynamic analysis

“…dAntibodies of the Sha series were raised against PK-treated and non-denatured scrapie-associated fibrils from Syrian hamster-infected brain (263K). §Antibodies of the bS series were raised against a mutated form of murine PrP (23-231), obtained by heterologous expression in bacteria (Meggio et al, 2000). Far-UV circular dichroism analysis of this mutated protein (pH 7.0, no added denaturants) revealed an extensive b-sheet conformation, with little or no a-helix present.…”

Gerstmann-Sträussler-Scheinker Disease Amyloid Protein Polymerizes According to the “Dock-and-Lock” Model

“…Most of these studies, however, provided only a qualitative analysis of SPR data, whereas the binding constants were not determined because of the complex association and dissociation kinetics, not fitting the classic 1:1 interaction model. Complex binding kinetics were always found when PrP was used as the flowing analyte, suggesting oligomerization of PrP on the sensor chip (27,28,30,32).…”

Selective and Efficient Immunoprecipitation of the Disease-associated Form of the Prion Protein Can Be Mediated by Nonspecific Interactions between Monoclonal Antibodies and Scrapie-associated Fibrils

“…mAb SHA-31 was clearly identified as binding PrPc in Western blot and ELISA experiments, whereas SHA-9, SHA-29, and SHA-52 were shown to react only with SAFs when the SPIE-IA technique was used. Antibodies of the ␤S series were immunized with a mutated form of murine PrP (23-231), obtained by heterologous expression in bacteria (21). The far-ultraviolet CD analysis of the protein (pH7.0, no added denaturants) revealed an extensive ␤-sheet conformation, with little or no ␣ helix present.…”