Dr James Schaller
tick infection pearls chat free books testimonials main page books and articles schaller health creed free consult testimonies search
menu main page what's new second opinion new patient meet doctor schaller location, travel

More Evidence of Lyme Biotoxins

In a book in Press I discuss about 15 reasons why Lyme disease treatment fails. Many reasons exist for patient residual suffering. One reason is that Lyme has biotoxins and when it dies there is more then mere debris, but also chemicals which cause serious damage to many human chemical systems. Here is a sample of just one Lyme biotoxin.

A Novel Toxin (Bb Tox 1) of Borrelia burgdorferi [Lyme disease]

Mark J. Cartwright, Ph.D.*, Suzanne E. Martin, Ph.D. and Sam T. Donta, M.D.

The mechanisms responsible for many of the symptoms of Lyme disease remain to be delineated. Because many of the symptoms involve the nervous system, we postulated that the Lyme spirochetes produce a toxin that interferes with normal neurophysiological function. We have identified and cloned a gene of B. burgdorferi which encodes a protein that is a neurotoxin.

Initially, degenerate primers were designed to highly conserved regions within various toxin groups. These primers were used for amplification of DNA extracted from B. burgdorferi strain 2591 to identify genes that express proteins analogous to existing toxins. Degenerate primers designed to the highly conserved catalytic domains of diphtheria and pertussis toxins yielded an amplification product. The product was cloned, sequenced, and subsequently identified in The Institute of Genomic Research (TIGR) database as BB0755, a 37 kD protein of unknown function. The full length gene for BB0755 was cloned, expressed and purified using epitope tags in the pET30a expression system, and the resultant recombinant protein renamed Bbtox1. Using the synthetic target agmantine, Bbtox1 exhibited ADP-ribosyltransferase activity. No ADP-ribosyltransferase activity was detected using elongation factor 2 as the target. In tissue culture, Bbtox1 affected the morphology (rounding) of Y1 mouse adrenal cells and C6 rat glial cells. Bbtox1 induced cell death in both Y1 and C6 cells. C6 glial cells responded to Bbtox1 in a dose and time dependent manner. Brefeldin A, an inhibitor of the trans-golgi network, accelerated the onset of action of Bbtox1 an Y1 adrenal cells.

The effects of Bbtox1 are consistent with a mechanism of action similar to that of botulinum C2 and other cytoskeletal toxins. Studies are underway to identify the cellular target of Bbtox1 and its role in Lyme Disease. In addition, a homologous gene in Treponema pallidum of undefined function is being analyzed to determine if it codes for a toxin similar to Bbtox1.

[Bolding and underlining done by Dr. Schaller]

Mark J. Cartwright, Ph.D.
Boston University Medical Center
Boston VA Medical Center
88 East Newton Street, E-639
Boston, MA 02118

Bank Towers, Tamiami Trail, Naples, FL
disclaimer privacy