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Cell-based Assay to Study Antibody-mediated Tau Clearance by Microglia

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Fucoidans inhibited tau interaction and cellular uptake.

Weihua Jin¹, Chenghui Lu², Yanan Zhu³

¹College of Biotechnology and Bioengineering, Zhejiang University of Technology, Hangzhou 310014, China; Department of Chemical and Biological Engineering, Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, NY 12180, USA.

Carbohydrate Polymers

|March 6, 2023

Summary

Fucoidans, sulfated polysaccharides, may inhibit Alzheimer's disease tau spreading by competing with cell surface heparan sulfate binding. Specific fucoidan fractions demonstrated strong tau binding and reduced cellular uptake, offering potential therapeutic strategies.

Keywords:

Alzheimer's disease Fucoidans Heparin Sulfated glycan Tau protein

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Area of Science:

Neuroscience
Biochemistry
Pharmacology

Background:

Tau spreading is a key mechanism in Alzheimer's disease progression.
Cell surface heparan sulfate (HS) mediates tau binding and spreading.
The structural basis for fucoidan competition with HS for tau binding is unclear.

Purpose of the Study:

To investigate fucoidans as potential inhibitors of tau spreading.
To identify structural determinants of fucoidans that influence tau binding.
To evaluate the efficacy of fucoidans in preventing tau cellular uptake.

Main Methods:

Surface Plasmon Resonance (SPR) and AlphaLISA assays were used to assess fucoidan-tau binding.
Sixty diverse fucoidan/glycan structures were analyzed.
Cellular uptake assays in mouse lung endothelial cells were performed.
Nuclear Magnetic Resonance (NMR) titration was employed to map binding sites.

Main Results:

Two fucoidan fractions, sulfated galactofucan (SJ-I) and sulfated heteropolysaccharide (SJ-GX-3), showed strong binding to tau, outperforming heparin.
SJ-I and SJ-GX-3 significantly inhibited tau-cell interactions and tau cellular uptake.
NMR mapping identified specific fucoidan binding sites on tau.

Conclusions:

Fucoidans, particularly SJ-I and SJ-GX-3, are effective inhibitors of tau-cell interaction and uptake.
These fucoidans show promise as therapeutic candidates for mitigating tau spreading in Alzheimer's disease.
Understanding fucoidan structural determinants provides a basis for designing novel tau spreading inhibitors.