Structural characterization of monoclonal antibodies targeting C-terminal Ser⁴⁰⁴ region of phosphorylated tau protein.

ABSTRACT: Targeting tau with immunotherapies is currently the most common approach taken in clinical trials of patients with Alzheimer's disease. The most prominent pathological feature of tau is its hyperphosphorylation, which may cause the protein to aggregate into toxic assemblies that collectively lead to neurodegeneration. Of the phospho-epitopes, the region around Ser³⁹⁶/Ser⁴⁰⁴ has received particular attention for therapeutic targeting because of its prominence and stability in diseased tissue. Herein, we present the antigen-binding fragment (Fab)/epitope complex structures of three different monoclonal antibodies (mAbs) that target the pSer⁴⁰⁴ tau epitope region. Most notably, these structures reveal an antigen conformation similar to a previously described p

SUBMITTER: Chukwu JE 

PROVIDER: S-EPMC6512906 | biostudies-literature | 2019 Apr

REPOSITORIES: biostudies-literature