In vitro neutralization of prions with PrP(Sc)-specific antibodies

Prion diseases reflect the misfolding of a self-protein (PrP(C)) into an infectious, pathological isomer (PrP(Sc)). By targeting epitopes uniquely exposed by misfolding, our group developed PrP(Sc)-specific vaccines to 3 disease specific epitopes (DSEs). Here, antibodies induced by individual DSE va...

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Bibliographic Details
Published in:Prion 2015, Vol.9 (4), p.292-303
Main Authors: Taschuk, Ryan, Van der Merwe, Jacques, Marciniuk, Kristen, Potter, Andrew, Cashman, Neil, Griebel, Philip, Napper, Scott
Format: Article
Language:English
Subjects:
Animals
Antibodies - immunology
Antibodies, Neutralizing - immunology
Humans
Prions - antagonists & inhibitors
Prions - immunology
PrPSc Proteins - immunology
Vaccines - immunology
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Summary:Prion diseases reflect the misfolding of a self-protein (PrP(C)) into an infectious, pathological isomer (PrP(Sc)). By targeting epitopes uniquely exposed by misfolding, our group developed PrP(Sc)-specific vaccines to 3 disease specific epitopes (DSEs). Here, antibodies induced by individual DSE vaccines are evaluated for their capacity to neutralize prions in vitro. For both purified antibodies and immunoreactive sera, the PrP(Sc)-specific antibodies were equally effective in neutralizing prions. Further, there was no significant increase in neutralizing activity when multiple DSEs were targeted within an assay. At a low antibody concentration, the PrP(Sc)-specific antibodies matched the neutralization achieved by an antibody that may act via both PrP(C) and PrP(Sc). At higher doses, however, this pan-specific antibody was more effective, potentially due to a combined deactivation of PrP(Sc) and depletion of PrP(C).
ISSN:1933-690X
DOI:10.1080/19336896.2015.1071761