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- W2126181567 abstract "Immunotherapy has become a strategy for treatment of Alzheimer's disease, by inducing antibody response to amyloid-ß peptide (AßP) or by passive administration of anti-AßP antibodies. Clearance of amyloid plaques involves interaction of immunoglobulin Fc receptor (FcR)-expressing microglia and antibodyopsonized Aß deposits, stimulating phagocytosis but may promote neuroinflammation. Carbohydrate moiety of Fc of the immunoglobulin G molecule plays a significant role in modulating binding to FcR and its effector functions. Here, we enzymatically removed Fc glycan from monoclonal antibody 196 raised against AßP. Antigen binding ability and in vitro stability of deglycosylated antibody were unaffected by deglycosylation. M oreover, the deglycosylated antibody exhibits low affinity to FcR on microglial BV-2 cells and has limited ability to mediate microglial chemotaxis and antibodydependent cytotoxicity compared to native antibody. These data suggest that deglycosylation of anti-Aß antibodies before in vivo administration might prevent microglial overactivation, thus reducing the risk of neuroinflammatory response during passive immunization." @default.
- W2126181567 created "2016-06-24" @default.
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- W2126181567 date "2005-09-01" @default.
- W2126181567 modified "2023-09-27" @default.
- W2126181567 title "Deglycosylation of anti-ß amyloid antibodies inhibits microglia activation in BV-2 cellular model" @default.
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- W2126181567 doi "https://doi.org/10.1177/153331750502000511" @default.
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