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Lecanemab, donanemab, and aducanumab bind amyloid-beta aggregates differently, but this study found no clear preference for specific forms that explains varying rates of amyloid-related imaging abnormalities (ARIA). These findings suggest antibody binding to cerebral amyloid angiopathy (CAA) Aβ does not solely determine ARIA risk.

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Area of Science:

  • Neuroscience
  • Immunology
  • Biochemistry

Background:

  • Lecanemab, donanemab, and aducanumab target amyloid-beta (Aβ) aggregates in Alzheimer's disease (AD) clinical trials.
  • These antibodies are proposed to bind distinct Aβ forms, potentially explaining varying rates of amyloid-related imaging abnormalities (ARIA).

Purpose of the Study:

  • To investigate the binding properties of lecanemab, donanemab, and aducanumab to different Aβ aggregates in human AD brain extracts.
  • To determine if antibody binding preferences correlate with ARIA rates observed in clinical trials.

Main Methods:

  • Developed an immunoprecipitation-ELISA to measure binding affinity (KD) and antigen availability (Bmax) to Aβ aggregates.
  • Analyzed aqueous and insoluble fractions from grey matter (plaque-enriched) and leptomeninges (CAA-enriched) AD brain.
  • Utilized linear mixed models to assess antibody binding, APOE genotype, and sex effects in 18 AD cases.

Main Results:

  • High correlation (r > 0.9) in Bmax was observed across all antibodies and Aβ aggregate extracts.
  • Lecanemab did not show a preference for aqueous Aβ (protofibrils) over aducanumab.
  • Aducanumab, associated with higher ARIA rates, did not consistently show greater preference for CAA Aβ compared to lecanemab or donanemab.

Conclusions:

  • No distinct Aβ aggregate populations were identified that were uniquely accessible to one antibody over the others in vitro.
  • Antibody preference for CAA Aβ over plaque Aβ does not appear to explain the observed differences in clinical trial ARIA rates.
  • Further research is needed to fully elucidate the mechanisms underlying ARIA development in response to amyloid-targeting therapies.