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Basic Science and Pathogenesis.

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Researchers developed a novel synaptic-chimeric antibody receptor (synCAR) to target pathogenic tau species in Alzheimer's disease (AD). This approach concentrates tau seeds at the synapse, potentially preventing disease spread and progression.

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Area of Science:

  • Neuroscience
  • Molecular Biology
  • Immunotherapy

Background:

  • Trans-synaptic tau transmission drives Alzheimer's disease (AD) pathology.
  • Current immunotherapies struggle to target tau species within the synaptic cleft.
  • Limitations include antibody selectivity, CNS availability, and synaptic access.

Purpose of the Study:

  • To develop a novel strategy for targeting pathogenic tau species at the synapse.
  • To overcome limitations of existing immunotherapies for AD.

Main Methods:

  • Purified synaptosomes from AD and control patients.
  • Utilized phospho-proteomics to identify tau epitopes in post-synaptic terminals.
  • Developed a synaptic-chimeric antibody receptor (synCAR) by fusing PHF1 scFv with neurolignin-1 (NLGN1) and delivered via AAV9.

Main Results:

  • Identified 17 phospho-tau epitopes enriched in AD post-synaptic fractions, including PHF1 (pS396/pS404).
  • PHF1 synCAR expressed effectively at the synaptic membrane in murine and hiPSC neuronal models without affecting viability.
  • PHF1 synCAR targeting of pathogenic tau increased tau aggregation in seeded neurons by ~73%, indicating capture and concentration of tau seeds.

Conclusions:

  • The study presents a novel mechanism for targeting proteins within the synaptic cleft or post-synaptic membrane.
  • PHF1 synCAR offers an effective approach for isolating and identifying propagating tau species.
  • This strategy holds potential for developing new AD therapeutics.