NR AQMY
AU Morel,N.; Simon,S.; Frobert,Y.; Volland,H.; Mourton-Gilles,C.; Negro,A.; Sorgato,M.C.; Creminon,C.; Grassi,J.
TI 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
QU The Journal of Biological Chemistry 2004 Jul 16; 279(29): 30143-9
PT journal article
AB 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.
IN Offenbar ist es möglich, spezifisch das PrPsc durch unspezifisch bindende monoklonale Antikörper zu immunopräzipitieren. Dies könnte helfen, BSE- oder Scrapie-Tests zu entwickeln, die auch bei Varianten funktionieren, bei denen das PrPsc nicht oder kaum resistent gegenüber der Protease K ist.
MH Animals; Antibodies, Monoclonal/*chemistry/metabolism; Binding Sites; Binding, Competitive; Blotting, Western; Brain/metabolism; Epitope Mapping; Epitopes; Magnetics; Precipitin Tests; Prions/*chemistry; Protein Binding; Scrapie/metabolism; Sheep; Support, Non-U.S. Gov't
AD CEA, Service de Pharmacologie et d'Immunologie, CEA Saclay, 91191 Gif sur Yvette, France.
SP englisch
PO USA
ZF Zusammenfassung des Abstracts von Roland Heynkes