Alzheimer’s Disease:Intracellular Beta Amyloid Completes the Irreversible Pathway from Spirochetes to Biofilms to Beta Amyloid to Hyperphosphorylated Tau Protein

Abstract

In this histopathological study, we have identified beta amyloid (Aβ) intracellularly in hippocampal specimens of Alzheimer’s disease (AD) patients. This is a continuation of the same histopathological project in which we observed biofilms intracellularly in the same neuronal cells in the same brain samples. To demonstrate that these were intracellular biofilms, we utilized the same techniques that showed biofilms in senile plaques in AD, in occluded eccrine ducts in atopic dermatitis, and in tonsils of psoriasis patients. Lyme spirochetes have recently been cultured from AD brains, and those same cultivated organisms have been shown in vitro to make biofilms, beta amyloid precursor protein (AβPP), and Aβ. We believe these spirochetes (and others) make the in vivo biofilms, and we believe our finding of intracellular Aβ helps confirm the in vitro observations. The Aβ, in turn, has previously been shown to stimulate the production and accumulation of hyperphosphorylated tau protein which has been shown to result in axonal and dendritic disintegration. With neuronal cell deterioration, the biofilms, AβPP, Aβ, and neurofibrillary tangles that were once inside are now present outside the cells. Once in the tissue, biofilms lead to upregulation of Toll-like receptor 2 (TLR2) which by known pathways leads to further production of Aβ. Thus, the Aβ can be derived from two sources: one is the spirochetes themselves and the other is from the activation of the innate immune system. The two major components of AD (tau protein and Aβ) have consequently been shown to be created by the pathogenic spirochetes. The spirochetes themselves have been shown to be of Lyme disease and dental origin.