Using tau protein extracts from Alzheimer's disease (AD) brain tissue, we generated a monoclonal antibody (mAb DC11) which decorated neurofibrillary pathology in brain derived from AD patients on immunohistochemistry, and which lacked reactivity with healthy brain tissue. The same pattern of DC11 specificity was observed on Western blot. The main constituent of structures decorated by DC11 is microtubule-associated protein tau. In Western blot, DC11 recognized neither native healthy tau nor its full length recombinant counterpart. However, the mAb showed strong immunoreactivity with truncated tau (residues tau151-421), thus indicating the requirement for a conformational epitope. Importantly, the DC11 epitope was phosphorylation independent. The immunochemical parameters of mAb show that DC11 could represent a novel structural probe with the specificity for conformation of pathological tau present in AD brains.
Copyright 2003 Lippincott Williams & Wilkins