Novel antibody against low-n oligomers of tau protein promotes clearance of tau in cells via lysosomes.

ABSTRACT:

Introduction

Tau, a natively unfolded soluble protein, forms abnormal oligomers and insoluble filaments in several neurodegenerative diseases, including Alzheimer disease (AD). Tau-induced toxicity is mainly due to oligomers rather than monomers or fibrils.

Methods

We have developed monoclonal antibodies against purified low-n tau oligomers of the tau repeat domain as a tool to neutralize tau aggregation and toxicity. In vitro aggregation inhibition was tested by thioflavin S, dynamic light scattering (DLS), and atomic force microscopy (AFM). Using a split-luciferase complementation assay and fluorescence-activated cell sorting (FACS), the inhibition of aggregation was analyzed in an N2a cell model of tauopathy.

Results

Antibodies inhibited tau aggregation in vitro up

SUBMITTER: Chandupatla RR 

PROVIDER: S-EPMC7593557 | biostudies-literature | 2020

REPOSITORIES: biostudies-literature