We recently have demonstrated pathologically that biofilms are present in the brains of Alzheimer’s disease (AD) patients. The biofilms were undoubtedly created by the dental and Lyme spirochetes which have previously been shown to be present there consequently, these biofilms would represent a chronic infection We also provided immunopathological evidence that the innate immune system reactant, Toll-like receptor 2 (TLR 2), was upregulated in that same tissue. We postulated that TLR 2, while trying to destroy the spirochetes, could not penetrate the biofilm and attacked the surrounding tissue instead. We also alluded to the recent work showing how the adaptive immune system became involved after traumatic brain injury and very rapidly created much more devastating damage than the innate immune system.
Our other observation, which combined pathology and immunopathology was demonstrating the co-localization of beta amyloid (Aβ) and biofilm. The significance of the finding represented by that photomicrograph was not alluded to. We present herein observations and marshal the evidence that gives substantiation to the significance of that finding.
Aβ has been shown, in a 3-dimensional pathology (side-by-side) presentation, to lay on top of the biofilms. This finding, plus the aforementioned co-localization, positions the Aβ in direct contiguity with the biofilms (which actually form the pathological plaques of AD).
An issue that remains is: how does the Aβ become positioned there, and what is its potential purpose?
We believe it may be related to the presence of TLR 2. This innate immune system molecule kills by activating the MyD88 pathway which leads to NFκB and ultimately to TNFα. It is the TNFα that is the “killing” agent for TLR 2.. It is capable of destroying planktonic gram positive organisms, yeasts, and spirochetes.
TNFα has been shown to be cleaved by TNFα converting enzyme (TACE) which has been shown to be dramatically upregulated in AD. TACE is localized in the neuronal membranes where it is in direct proximity to the spirochetal derived biofilms and where it acts to upregulate alpha secretase. Beta secretase, and gamma secretase are upregulated by NFκB. NFκB then links with BACE (beta amyloid converting enzyme) that cleaves the amyloid precursor protein (APP) that changes the precursor molecule to Aβ. The γ- secretase has been linked to the genetic form of the disease.
Aβ has been shown to be antimicrobial. It seems that is its purpose for which it is generated. However, and this is most important, it is not able to penetrate the biofilm either (just as TNFα cannot).
Thus, the body in trying to rid itself of the spirochetal parasites in one case (TNFα) most assuredly contributes to the disease. In the other case, while also trying to act anti-microbially, the innate immune system creates a substance (Aβ) that further damages the tissue and the neuronal circuits.
As has been said previously, it is most important to treat these microbes before they get to the brain or before the do damage (make biofilms).
All that is necessary is an antibiotic that is bactericidal and crosses the blood brain barrier. If necessary, a biofilm dispersing agent that also crosses the blood-brain barrier, such as a furan, a pyrrole, a piperidine, or a thiophene or other could also be added to the regimen (All these pharmaceuticals cross the blood brain barrier). The spirochetes, biofilm, immune system, and Aβ are capable of marked neuronal damage which is non-reversible. This makes treatment and potential prevention both urgent and compelling.