Amyloid-â (Aâ) plaques and neurofibrillary tangles are the hallmark neuropathological lesions of Alzheimer's disease (AD). Using a triple transgenic model (3xTg-AD) that develops both lesions in AD-relevant brain regions, we determined the consequence of Aâ clearance on the development of tau pathology. Here we show that Aâ immunotherapy reduces not only extracellular Aâ plaques but also intracellular Aâ accumulation and most notably leads to the clearance of early tau pathology. We find that Aâ deposits are cleared first and subsequently reemerge prior to the tau pathology, indicative of a hierarchical and direct relationship between Aâ and tau. The clearance of the tau pathology is mediated by the proteasome and is dependent on the phosphorylation state of tau, as hyperphosphorylated tau aggregates are unaffected by the Aâ antibody treatment. These findings indicate that Aâ immunization may be useful for clearing both hallmark lesions of AD, provided that intervention occurs early in the disease course.