Parasitic Nematode Worms containing Borrelia Endosymbionts in Alzheimer’s Disease

Alz Dis Case 8104 TRichrome stain-16-06-12-16-05-08
Parasitic nematode in autopsy Alzheimer’s brain tissue. Copyright Alan MacDonald MD

In June 2016, Dr. Alan B. MacDonald, president of the Dr. Paul Duray Research Fellowship Endowment and patron of the Spirochaetal Alzheimer’s Association, became the first scientist to demonstrate the presence of parasitic nematode worms containing endosymbiont Borrelia bacteria in autopsy Alzheimer’s brain tissue.

Below Dr. MacDonald explains his findings, and hypothesises on the ramifications of what he has found. The results of his study are illustrated in a series of posters to be published here.

“Nematode worms, (for example C. elegans), manufacture their very own proteins. One example of these is LEA proteins (Late Embryogenesis-Abundant proteins)

The LEA proteins, by sheer serendipity, show striking three dimensional stereo-similarities with the alpha-helical domains of mammalian alpha-synuclein proteins.

The bad news is this:

Worm-manufactured proteins cross-react antigenically with alpha-synuclein proteins.

Worm proteins, because of their stereo-morphologies, and accidental cross-reactivities with benign human alpha-synucleins, are incorporated by synaptic re-uptake from the presynaptic bouton of the human neuron and enter its cytoplasm.

Once inside the human neuron, the worm LEA proteins produce toxic effects, and eventually form Lewy neurites, and in  further retrograde  migration/passage backwards towards the nucleus of the neuron,  eventually  reach the soma regions of the human neuron, where they “round up” to form the rounded Lewy bodies.  The Lewy bodies are dumped into the brain after the neuron dies.

It is well established that by injection studies of animal brains with  huge excesses of healthy labelled alpha-synuclein proteins, that there is a nerve-to-nerve transmission of these proteins throughout neural networks  and that synaptic re-uptake of extra-cellular alpha-synuclein is a reality.

We have already proven that nematode worms and their borrelia endosymbionts collectively manufacture proteins which cross-react with rabbit antibodies to benign human alpha-synucleins.

The extension of the Lewy body pathobiology ( worms, LEA proteins, Borrelia endosymbionts, dementia, LBD) to Alzheimer’s disease pathobiology is completely logical, given that 30% of Alzheimer’s disease contains a population of Lewy bodies.

I hypothesise that Parkinson’s and its Lewy bodies (worm endosymbiont Borrelia), Multiple System Atrophy, ALS (with its round bodies inside of wounded neurons), Cortico-basal degeneration, Progressive Supranuclear Palsy, and Fronto-Temporal Dementias including Pick’s Disease, as well as all of the less well known neurodegenerative disorders involving round bodies in neurons will show the same pathology.

That is to say that worms, in partnership with their endosymbiont microbes, destroy human higher cortical functions and produce movement disorders.”


Click here to view micrographs of parasitic nematodes and/or nematode debris in Alzheimer’s Disease, including inside the amyloid plaques.