Chronic Lyme disease and the Yasko treatment program

[Guest guest]

Hi, all.

Here's a repost from the Experimental list. Maybe it will be of

interest to some people here:

I've been doing some more study of chronic Lyme disease and have

been thinking about why the Yasko treatment program might be helpful

to someone with this disorder.

As we know, Sue T. has been reporting considerable improvement on

the Yasko treatment program, and as we also know, she has tested

positively for Lyme disease in the past and has been ill for a long

time. So what's going on here?

As some of you may recall, I posted some information about Lyme

disease and glutathione depletion back in January. I've pasted it at

the end of this message for those who would like to review it.

In that earlier post, I reviewed published literature showing that

Borrelia burgdorferi (the bacteria responsible for Lyme disease)

depletes glutathione in the host, and it appears to suppress the

activity of glutathione peroxidase over the longer term, even after

antibiotic treatment.

With glutathione peroxidase suppressed, we can expect that the

levels of hydrogen peroxide would be higher in the host, because the

job of glutathione peroxidase is to eliminate hydrogen peroxide.

O.K., here's something I just found out: Borrelia burgdorferi is

encouraged to assume its cystic form when hydrogen peroxide is

elevated, and when the cystic forms are placed back in a medium with

low hydrogen peroxide, they revert back to the spirochete form. (R.

Murgia and M. Cinco, 2004, PMID: 14961976).

Now, I think this is really interesting. I think it suggests that

the reason Borrelia burgdorferi is able to hang on in a person's

body and produce chronic Lyme disease is that it suppresses the

activity of glutathione peroxidase, which allows hydrogen peroxide

to build up, and then the hydrogen peroxide signals the bacteria to

assume the cystic form. This protects it from the immune system

and, to a large extent, from antibiotics as well, and that's why

chronic Lyme is such a difficult disease to knock out.

As I said in my earlier post (below), I don't know how Bb suppresses

glutathione peroxidase, but I suspect that it might do it by

hoarding selenium, as Prof. Harry has theorized as the

pathogenesis mechanism for some viruses, including HIV. Of course,

as we know, the buildup of mercury, as occurs when glutathione is

depleted and a person is exposed to mercury from amalgams, fish, or

other sources, will tie up selenium as well. This may be part of

the synergism that Dr. Yasko has found between pathogens and heavy

metals.

In any case, it seems to me that the key to knocking out chronic

Lyme disease might be to lower the levels of hydrogen peroxide, so

that Bb will revert to the spirochete form and can be attacked by

the immune system and by antibiotics. To do this, both the activity

of glutathione peroxidase and the level of glutathione must be

brought up to normal. How do we do this?

I think supplementation with selenium would be a good thing to try

for restoring the activity of glutathione peroxidase.

What about glutathione? Well, in the case of many of the people

with chronic Lyme disease, I suspect that we are dealing with a set

of polymorphisms in the enzymes impacting the methylation cycle that

enable the development of a vicious circle mechanism when the

glutathione level drops low enough, i.e. the same mechanism that

occurs in many cases of autism and chronic fatigue syndrome. (This

certainly seems to have been true in the case of Sue T.) If this is

true, then it will be necessary to deal directly to bypass these

polymorphisms, such as is done in the Yasko treatment program.

What I'm suggesting then, is that the people with chronic Lyme

disease might also be brought under the " Yasko tent. " This might be

the key to making the Borrelia more vulnerable to the immune system

and to the antibiotics, so that this disease can be knocked out more

effectively.

I would appreciate comments on this hypothesis.

Rich

Here is my earlier post from last January:

Hi, Nelly, Sue, Sheila and the group.

Thanks very much for posting this. It has really stimulated my

thinking about why Lyme disease is symptomatologically so similar to

CFS.

First, some review. As we all know, it has been terribly difficult

to do the differential diagnosis between Lyme disease and CFS. The

symptoms overlap considerably, and even the best of the lab tests do

not have the sensitivity and selectivity we would all like to see.

Symptoms are manifestations of the pathophysiology of a disease,

i.e. how the functioning of the body of the sick person is abnormal

as a result of the disease. Therefore, if we see that the symptoms

of two diseases are very similar, we should suspect that they must

have some aspects of pathophysiology in common.

Pathophysiology is intimately involved with abnnormal gene

expression in the cells of the sick person, because gene expression

is a reflection of how the cell is conducting its business, and the

misconduct of the business of the cell is pathophysiology.

Because of this, I was quite struck some time ago when Sheila

reported that Dr. Gow said in a recent talk that he had found that

the gene expression pattern in peripheral blood mononuclear cells

(monocytes and lymphocytes) is " identical " in CFS and Lyme disease.

This implies that the pathophysiology of these two disorders in

these cell types is the same. (Note that we can't say anything

about what's going on in other cell types in the body in these two

disorders from this work. There are no doubt different things that

happen in other cell types between Lyme and CFS, and so this is not

saying that the two are identical in every way. But in these

mononuclear cells, this is saying that the pathophysiology of the

two is the same.)

As you know, I am of the firm view that in at least a large subset

of CFS there is glutathione depletion. In another subset, it looks

as though there are genetic variations in the enzymes that make use

of glutathione (glutathione transferases and glutathione

peroxidases), and the results in terms of pathophysiology are much

the same, even though the first group has low glutathione, and the

second group may have elevated glutathione. In either subset, the

people do not have normal glutathione function.

As you also know, based on the work by the DAN! project in autism, I

now believe that the basic abnormalities in the biochemistry in

autism and CFS are the same or similar. The glutathione depletion

brings down the methylation cycle, and a vicious circle develops

that produces a host of problems because of the depletion of SAMe

(the main methylator in the body), cysteine, glutathione, taurine

and sulfate.

So, if the pathophysiology of CFS involves the inability to use

glutathione effectively, whether because glutathione itself is

depleted or because the enzymes that use it have below-normal

activity, and if the pathophysiology of CFS and Lyme are indeed

identical, then it follows that there must be a problem with the

glutathione system in Lyme disease as well.

With that introduction, let me now review some things I found in the

literature, including the paper to which you (Nelly) drew my

attention. I will give the PubMed ID numbers for the references

that support these statements.

(PMID 1477785) First, in in vitro experiments it has been found

that the growth of Borrelia burgdorferi (Bb), the bacterium that

causes Lyme disease, is decreased by 80% if cysteine is not present

in the culture medium.

(PMID 147785) It has been found that cysteine diffuses passively

into Bb, i.e. there is no active transporter protein that pumps it

into the bacterium.

(PMID 1477785) It has been found that Bb incorporates cysteine in

three of its proteins. One has a mass of 22 kilodaltons. The

others have been identified as outer surface protein A (Osp A), with

a mass of 30 kilodaltons, and outer surface protein B (Osp , with

a mass of 34 kilodaltons.

(PMID 1639493) Bb produces a water-soluble hemolysin. This is a

substance that is able to break down red blood cells and release

their hemoglobin. It is likely that this substance incorporates a

cysteine residue, and this cysteine must be in its reduced state in

order for the hemolysin to break down red blood cells.

(PMID 16390443) Bb does not produce glutathione, which is the

principal non-protein thiol (substance containing an S-H or

sulfhydryl group) in human cells. Instead, Bb cells have a high

concentration (about 1 millimolar) of reduced coenzyme A (CoASH).

Bb also produces a CoA disulfide reductase enzyme that has the

responsibility to keep CoASH in its chemically reduced form, so it

can function. This enzyme is in turn reduced by NADH (reduced

nicotinamide adenine dinucleotide), which is reduced by metabolism

of Bb's fuel. (This is analogous to glutathione reductase in human

cells, which requires NADPH, which in turn is reduced by the pentose

phosphate shunt on glycolysis, which metabolizes glucose as fuel.)

In Bb, CoASH is able to reduce hydrogen peroxide, as glutathione

peroxidase, together with glutathione, do in human cells.

(PMID 11687735) It has been found that when people were infected

with Bb and had the characteristic erythema migrans (bulls-eye

rash), the total thiol and glutathione in blood analysis were found

to be significantly decreased. The activity of glutathione

peroxidase was also significantly decreased. Malondialdehyde, a

marker for lipid peroxidation, was significantly elevated. After

antibiotic treatment with amoxycillin, which eliminated the acute

symptoms of Lyme disease, both the total thiol and the glutathione

levels recovered to normal. However, the glutathione peroxidase

activity was still significantly below normal, and the

malondialdehyde remained significantly elevated. This suggested

that Bb lowers the thiol and glutathione levels in its host, and

inhibits the activity of glutathione peroxidase.

I think this also suggests that while antibiotic therapy eliminates

acute Lyme symptoms and brings recovery of glutathione levels, the

Bb infection may still be suppressing the activity of glutathione

peroxidase, and this may be a mechanism involved in long-term (or

chronic or post-) Lyme disease.

One way in which a pathogen can inhibit its host's glutathione

peroxidase activity is to hoard selenium, because this is a cofactor

for that enzyme. You may recall that that is the mechanism that

Prof. Harry has hypothesized for HIV and AIDS

(http://www.hdfoster.com). I could not find any reference in the

literature connecting Bb and selenium, and I don't know whether

anyone has looked at that. Have any of you who are positive for

Lyme had your selenium level measured?

It seems pretty clear that Bb uses cysteine and that it depletes

glutathione and total thiol (which includes cysteine and protein

thiols as well as glutathione) in its host, at least in the acute

phase. It also suppresses the activity of glutathione peroxidase,

but I'm not sure whether it does it by lowering the host's selenium

level, or by some other means. This suppression appears as though

it could be chronic. I think there is a good chance that this

lowering of glutathione and/or suppressing of the activity of

glutathione peroxidase could very well be the explanation for the

similarities in symptomatology and the " identical " gene expression

in the peripheral blood mononuclear cells in CFS and Lyme disease.

It may also be that a host whose glutathione has been depleted by

other factors may be more vulnerable to developing Lyme disease,

once inoculated with Bb. I am speculating a little here, but this

is exciting!

If this is true, what are the consequences for treatment of long-

term Lyme disease, the subject that Sue raised? I think this

remains to be seen, but it does suggest that the DAN! autism

treatments may have a contribution to make in the treatment of long-

term Lyme disease as I've suggested that they also do in the

treatment of CFS. Before we can reach such a conclusion, though, I

think it behooves us to get more data on glutathione levels,

selenium levels, and glutathione peroxidase activity in people with

positive tests for long-term Lyme disease, as well as some

experience trying these treatments as part of the treatment of long-

term Lyme disease. I'm not suggesting that they would replace other

treatments for Lyme disease, such as antibiotic therapy, detoxing of

neurotoxins, or other approaches to deal with the bacteria

themselves or to deal with particular characteristics of Lyme

disease that are not found in autism or CFS. Nevertheless, these

treatments might make a significant impact. Time will tell. Thanks

for rattling my cage about this, Sheila, Sue and Nelly.

Rich