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.
Transmissible spongiform encephalopathies are characterized by the accumulation in brain tissues of an abnormal isoform of the prion protein named PrPsc, which is the only direct marker known for transmissible spongiform encephalopathies. Here we show that PrPsc can be specifically immunoprecipitated by using several monoclonal antibodies (mAbs) of various specificities independently of the properties of their binding site (paratope). These results strongly suggest that a significant proportion of mAbs can interact with PrPsc aggregates through nonspecific paratope-independent interactions allowing selective immunoprecipitation of PrPsc when these mAbs are immobilized on a polydisperse solid phase like microbeads.
Morel
Nathalie
N
CEA, Service de Pharmacologie et d'Immunologie, CEA Saclay, 91191 Gif sur Yvette, France.
Simon
Stéphanie
S
Frobert
Yveline
Y
Volland
Hervé
H
Mourton-Gilles
Chantal
C
Negro
Alessandro
A
Sorgato
Maria Catia
MC
Créminon
Christophe
C
Grassi
Jacques
J
D000818:Animals; D000911:Antibodies, Monoclonal / Q000737:chemistry* / Q000378:metabolism; D001665:Binding Sites; D001667:Binding, Competitive; D015153:Blotting, Western; D001921:Brain / Q000378:metabolism; D018604:Epitope Mapping; D000939:Epitopes; D008280:Magnetics; D011233:Precipitin Tests; D011328:Prions / Q000737:chemistry*; D011485:Protein Binding; D012608:Scrapie / Q000378:metabolism; D012756:Sheep
D000911:Antibodies, Monoclonal; D000939:Epitopes; D011328:Prions