Lyme disease, potential plague of the 21st century detection problems resolved by imaging with the Bradford Variable Projection High Resolution Microscope

Townsend Letter for Doctors and Patients, Jan, 2005 by Robert W. Bradford, Henry W. Allen

Therapy for Lyme Disease

Antibiotics

When conditions become adverse for its survival, Bb produces cysts containing the DNA defining the organism intended for future generations but surviving in a metabolically inactive state. In this state there is no cell wall generation and no way an antibiotic can damage the organism. (9)

It has been found that tetracycline can inhibit cyst formation and damage the envelope of cysts. It is also believed that bismuth compounds can enter cysts through the cyst wall. In addition, the prolonged replication rate, mentioned previously, protects the organism from cell wall damage by most antibiotics. (10) See Chart 7.

Oral Salt Therapy

Certain white blood cells (WBC) display several distinct mechanisms that may be employed for the purpose of killing invading microorganisms. One of these deserves particular attention in relation to killing the causative agent of Lyme disease, namely, the spirochete Borrelia burgdorferi.

Neutrophils (a class of WBC) contain two essentially different types of storage granules, peroxidase-positive granules and peroxidase-negative granules. Peroxidase-positive granules contain myeloperoxidase, an enzyme that uses hypochlorous acid (HOCI) in conjunction with hydrogen peroxide, providing a source of nascent (atomic) oxygen for the purpose of killing invading microorganisms. (11)

Peroxidase-negative granules contain a family of large polypeptides (11 to 19 kDa) (Dalton, the unit of molecular weight) known as the cathelicidins or, in humans, hCAP-18. A segment of this larger or precursor protein (also known as a Bacteriacidal Permeability-Increasing (BPI) protein) is proteolytically removed by the enzyme elastase found in peroxidase-positive granules. The better-known substrate of elastase is the elastic protein elastin, found in skin and other tissues requiring elasticity. By incorporating elastase inhibitors into skin creams, attempts are made to inhibit the activity of this enzyme, thereby decreasing the ageing of skin. In Lyme therapy there is an advantage (described below) to increasing the activity of this enzyme, thereby stimulating the natural antimicrobial system. These short peptides, ranging from 12 to 100 amino acids, have the ability to assemble into larger units that form pores in the membrane surrounding microorganisms, thereby increasing the permeability of those membranes. In humans, one of these antimicrobial peptides has been dubbed LL-37. (11) See Photo 10, courtesy of Blood 96 (8) 2000.

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Both of these proteins, the cathelicidin and elastase, meet in the phagocytic vacuole, the cytoplasmic chamber in which resides the phagocytized microorganism. Within this chamber, elastase removes a short peptide capable of forming a molecular pore in the surface membrane of the microorganism. The pore formed from a group of the cathelicidins allows the efflux of potassium ions from the organism, resulting in swelling and eventual lysis. (12)

Research has shown that, of all the proteins in neutrophil granules, the only protein capable of releasing the cathelicidin active peptide is elastase. (13) It has been demonstrated that the activity of elastase is enhanced by an increased salt concentration. (14) Through oral salt (12 g per day, see Chart 12), combined with large doses of vitamin C, the indirect killing ability of elastase is dramatically increased. (15)