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Intracranial administration of deglycosylated C-terminal-specific anti-Aβ antibody efficiently clears amyloid plaques without activating microglia in amyloid-depositing transgenic mice

Bibliographic

Year of Publication:
2006
Contact PI Name:
David Morgan
Contact PI Affiliation:
Alzheimer's Research Laboratory University of South Florida Department of Molecular Pharmacology and Physiology, Tampa, Florida, USA
Co-Authors:
Niki C. Carty, Donna M. Wilcock, Arnon Rosenthal, Jan Grimm, Jaume Pons, Victoria Ronan, Paul E. Gottschall, Marcia N. Gordon
Primary Reference (PubMED ID):
Funding Source:
National Institute on Aging (NIA)
Study Goal and Principal Findings:

This study investigated effects of deglycosylated C-terminal-specific anti-Aβ antibody on amyloid plaque clearance and microglia activation in Tg2576 mice. Past studies have shown vaccinations with Aβ can prevent plaque formation, reduce pre-existing brain amyloid, and protect APP transgenic mice from developing memory impairments. These observations initiated clinical trials in which patients with mild to moderate AD were given an active immunization, but Phase IIa trials were interrupted due to the occurrence of meningoencephalitis in 6% of the patients. Consequently, passive immunization became considered as a possibly safer means of removing Aβ deposits from the brain. Immunization with anti- Aβ monoclonal antibodies has been demonstrated to be an effective means of clearing Aβ plaques and reversing cognitive deficits in Tg mice. However, recent studies have demonstrated potentially harmful aspects of Aβ passive immunotherapy, such as significant increases in cerebral hemorrhage and cerebral amyloid angiopathy in association with increases in vascular leakage. Microglial activation has been shown surrounding amyloid-containing blood vessels following systemic passive immunization and could potentially be one of the mechanisms that increase the likelihood of microhemorrhage. This study investigated the efficacy of a deglycosylated antibody with decreased affinity for the Fcγ receptor for its ability to eliminate Aβ from the brain without increasing microglial activation. Results show that deglycosylated 2H6 antibody had lower affinity for several murine Fcγ receptors and human complement than intact 2H6 without a change in affinity for Aß, with reductions in both diffuse and compact deposits and no increase in Fcγ-receptor II/III or the microglial activation marker CD45. These findings suggest that antibodies with reduced effector functions may clear amyloid without concomitant immune activation when tested as immunotherapy for Alzheimer's disease.

Therapeutic Agent

Therapeutic Information:
Therapy Type:
Biologic - Immunotherapy(passive)
Therapeutic Agent:
2H6 (anti-Abeta Mab)
Therapeutic Target:
beta Amyloid Peptide
Therapy Type:
Biologic - Immunotherapy(passive)
Therapeutic Agent:
Deglycosylated 2H6 (anti-Abeta Mab)
Therapeutic Target:
beta Amyloid Peptide

Animal Model

Model Information:
Species:
Mouse
Model Type:
APP
Strain/Genetic Background:
Not Reported

Experimental Design

Is the following information reported in the study?:
Power/Sample Size Calculation
Randomized into Groups
Blinded for Treatment
Blinded for Outcome Measures
Pharmacokinetic Measures
Pharmacodynamic Measures
Toxicology Measures
ADME Measures
Biomarkers
Dose
Formulation
Route of Delivery
Duration of Treatment
Frequency of Administration
Age of Animal at the Beginning of Treatment
Age of Animal at the End of Treatment
Sex as a Biological Variable
Study Balanced for Sex as a Biological Variable
Number of Premature Deaths
Number of Excluded Animals
Statistical Plan
Genetic Background
Inclusion/Exclusion Criteria Included
Conflict of Interest

Outcomes

Outcome Measured
Outcome Parameters
Histopathology
beta Amyloid Deposits
beta Amyloid Load
Activated Microglia
Dense-core/Compact Plaques
Immunochemistry
Fc gamma Receptor
CD45
Immunology
Antibody Target Specificity
Antibody Affinity