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 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).
a School of Public Health ; University of Saskatchewan , Saskatoon , Saskatchewan , Canada.
Ryan
R
Taschuk
Jacques
J
Van der Merwe
Kristen
K
Marciniuk
Andrew
A
Potter
Neil
N
Cashman
Philip
P
Griebel
Scott
S
Napper
D000818:Animals; D000906:Antibodies / Q000276:immunology*; D057134:Antibodies, Neutralizing / Q000276:immunology; D006801:Humans; D018620:PrPSc Proteins / Q000276:immunology*; D011328:Prions / Q000037:antagonists & inhibitors* / Q000276:immunology*; D014612:Vaccines / Q000276:immunology
D000906:Antibodies; D057134:Antibodies, Neutralizing; D018620:PrPSc Proteins; D011328:Prions; D014612:Vaccines
antibodies; antibody neutralization; disease specific epitopes; prion; vaccine