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 immunoprecipitate...

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Bibliographic Details
Published in:The Journal of biological chemistry 2004-07, Vol.279 (29), p.30143-30149
Main Authors: Morel, Nathalie, Simon, Stéphanie, Frobert, Yveline, Volland, Hervé, Mourton-Gilles, Chantal, Negro, Alessandro, Sorgato, Maria Catia, Créminon, Christophe, Grassi, Jacques
Format: Article
Language:English
Subjects:
Animals
Antibodies, Monoclonal - chemistry
Antibodies, Monoclonal - metabolism
Binding Sites
Binding, Competitive
Blotting, Western
Brain - metabolism
Epitope Mapping
Epitopes
Magnetics
Precipitin Tests
Prions - chemistry
Protein Binding
Scrapie - metabolism
Sheep
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Summary: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.
ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.M403896200