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Both studies showed dose- and time-dependent lowering of cerebral amyloid.
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In October 2019, Biogen announced that upon analysis of the full data set of all participants, aducanumab reached its primary endpoint of clinical benefit (CDR-SB) in a large Phase III clinical trial (EMERGE), and while not significant in another large Phase III (ENGAGE) study, post hoc analysis showed slowing of cognitive decline for those in the high dose treatment group (press release CTAD 2019, San Diego). Biogen halted all aducanumab clinical trials in March 2019 after an interim futility analysis of half of the participants predicted that there would be no clinical benefit in patients with prodromal or mild AD (press release MaAD/PD 2019, Lisbon). Similar to some other anti-amyloid antibodies, aducanumab treatment was accompanied by amyloid-related imaging abnormalities (ARIA), imaging abnormalities indicating mostly asymptomatic and transient side effects due to vascular edema. Following the initial failures of active and passive immunotherapies after the onset of clinical symptoms, a Phase 1b study of an anti-Aβ monoclonal antibody, aducanumab, provided promising results with regard to amyloid lowering and cognitive readouts. Peripherally administered anti-Aβ antibodies are able to access the CNS to reduce the extent of plaque deposition through Fc-mediated phagocytosis. On the basis of the amyloid hypothesis, removal of Aβ aggregates by immunotherapy has been suggested as a treatment option to slow or halt AD.
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Strong genetic and pathological evidence indicates the “amyloid hypothesis” as a central contributor of early AD pathogenesis.
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The pathological hallmarks of AD include amyloid-beta (Aβ) plaques and neurofibrillary tangles. Hence, the results provide implications for tailoring effector function of humanized antibodies for clinical development.Īlzheimer’s disease (AD) is the most common form of dementia, with global prevalence of this devastating disease estimated at 50 million people and predicted to triple by 2050. We present evidence that antibody engineering to reduce CDC-mediated complement binding facilitates phagocytosis of plaques without inducing neuroinflammation in vivo.
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Our results suggest that attenuation of behavioral deficits and clearance of amyloid is associated with strong effector function of the anti-pGlu-3 Aβ mAb in a therapeutic treatment paradigm. Longitudinal 18F-GE180 microPET imaging revealed different temporal patterns of microglial activation for 3A1, 07/1, and 07/2a mAbs and no difference between 07/2a-k and PBS-treated Tg mice. Treatment of APP SLxhQC mice with 07/2a and 07/2a-k mAbs in our second in vivo study showed significant plaque-lowering with both mAbs. Compared with 07/2a, 07/2a-k showed slightly reduced affinity to Fcγ receptors CD32 and CD64, although the two antibodies had similar binding affinities to pGlu-3 Aβ. All mAbs cleared plaques in an ex vivo assay, although 07/2a promoted the highest phagocytic activity. We demonstrated significant cognitive improvement, better plaque clearance, and more plaque-associated microglia in the absence of microhemorrhage in aged APP SWE/PS1ΔE9 Tg mice treated with 07/2a, but not 07/1 or 3A1, compared to PBS in our first in vivo study. We also compared the ability of these antibodies and a CDC-mutant form of 07/2a (07/2a-k), engineered to avoid complement activation, to clear Aβ in an ex vivo phagocytosis assay and following treatment in APP SLxhQC double Tg mice, and to activate microglia using longitudinal microPET imaging with TSPO-specific 18F-GE180 tracer following a single bolus antibody injection in young and old Tg mice. We compared two different immunoglobulin (Ig) isotypes of the same murine anti-pGlu-3 Aβ mAb (07/1 IgG1 and 07/2a IgG2a) and a general N-terminal Aβ mAb (3A1 IgG1) for their ability to clear Aβ and protect cognition in a therapeutic passive immunotherapy study in aged, plaque-rich APP SWE/PS1ΔE9 transgenic (Tg) mice. We address the question of how the effector function of an anti-pGlu-3 Aβ antibody influences the efficacy of immunotherapy in mouse models with AD-like pathology. Its increased peptide aggregation propensity and toxicity make it an attractive emerging treatment strategy for AD. Pyroglutamate-3 Aβ (pGlu-3 Aβ) is an N-terminally truncated and post-translationally modified Aβ species found in Alzheimer’s disease (AD) brain.