Re: AUTOIMMUNE DISEASES CAUSED BY AN AMOEBA INFECTION?
Hi,
I woke up this morning thinking about the lectin - virus -amoeba sequence.
It is sort of matter (lectin) - information (virus) - microorganism (amoeba).
As the next study show, they are interconnected when acting in the organism (please bear with me, I'm not a microbiologist...)
_http://www.ncbi.nlm.nih.gov/books/NBK1907/
quote:
This chapter describes examples of proteins on the surface of microorganisms (adhesins or hemagglutinins), secreted proteins (heat-labile toxins), thei rglycan partners on mammalian cell surfaces (receptors), and insights into the molecular interactions that take place.
Viruses, bacteria, and protozoa express an enormous number of glycan-binding proteins or lectins. Many of these microbial lectins were originally detected based on their ability to aggregate red blood cells (i.e., to inducehemagglutination). The first microbial hemagglutinin identified was in the influenza virus, and it was shown by Alfred Gottschalk in the early 1950s to bind to erythrocytes and other cells though sialic acid residues of cell-surface glycoconjugates.
Many adhesins contain carbohydrate-recognition domains (CRDs) that bind to the same carbohydrates as endogenous mammalian lectins (see Chapter 26).
Like animal cell lectins, some microbial adhesins bind to terminal sugar residues, whereas others bind to internal sequences found in linear or branched oligosaccharide chains. Detailed studies of the specificity of microbial lectins have led to the identification and synthesis of powerful inhibitors of adhesion that may form the basis for therapeutic agents for treating infection (see Chapter 51).
….
VIRAL GLYCAN-BINDING PROTEINS
By far, the best-studied example of a viral glycan-binding protein is the influenza virus hemagglutinin, which binds to sialic acid–containing glycans. The affinity of this interaction is relatively low, like that of other glycan-binding proteinswith their glycan ligands, but the avidity for cell membranes increases because of oligomerization of the hemagglutinin into trimers and the high density of glycan receptors present on the host cell (see Chapter 27). Binding is a prerequisite for fusion of the viral envelope with the plasma membrane and for uptake of the virus into cells. The specificity of the interaction of the hemagglutinin with host glycans varies considerably for different subtypes of the virus.
…
BACTERIAL ADHESION TO GLYCANS
Bacterial lectins occur commonly in the form of elongated, submicroscopic, multisubunit protein appendages, known asfimbriae (hairs) or pili (threads), which interact with glycoprotein and glycolipid receptors on host cells.
…
Other binding specificities have been described as well (Table 34.2). The specificity of binding can explain the tissue tropism of the organism. The columnar epithelium that lines the large intestine expresses Galα1–4Gal-Cer, whereas the cells lining the small intestine do not. Thus, Bacterioides, Clostridium, E. coli, and Lactobacillus only colonize the large intestine under normal conditions.
…
TOXINS THAT BIND GLYCANS
A number of secreted bacterial toxins also bind to glycans (Table 34.3). The best-studied example is the toxin fromVibrio cholera (cholera toxin), which consists of A and B sub-units in the ratio AB5. Its crystal structure shows that the B subunits bind to the Galβ1–3GalNAc moiety of GM1 ganglioside receptors through CRDs located on the base of the subunits (Figure 34.6). The A subunit is loosely held above the plane of the B subunits, with a single α-helix penetrating through a central core created by the pentameric B subunits. Upon binding to membrane glycolipids through the B subunits, the A subunit is delivered to the interior of the cell by an unknown mechanism. In cholera toxin, the affinity of the B subunit for its glycan ligand (GM1) is unusually high compared to the binding of related AB5 toxins from Shigella dysenteria, Bordetella pertussis, and E. coli to their glycan receptors (Kd in the nanomolar range for cholera toxin B subunit vs. millimolar range for Shiga toxin B subunit binding to Pk determinants). In both examples, the formation of the pentameric complex greatly increases the avidity of the interaction. This phenomenon is being exploited to make oligovalent glycan ligands as protective agents against the toxin.
………
PARASITE LECTINS
In addition to viruses and bacteria,
a number of parasites also utilize glycans as receptors for adhesion (Table 34.4).Entamoeba histolytica expresses a 260-kD heterodimeric lectin that
binds to terminal galactose/N-acetylgalactosamine residues on glycoproteins and glycolipids. Binding may have a role in attachment, invasion, and cytolysis of intestinal epithelium,
and it may function in binding the amoeba to bacteria as a food source. The lectin is heterodimeric, with a transmembrane subunit of 170 kD and a glycosylphosphatidylinositol (GPI)-anchored subunit of 35 kD. The glycan-binding site is located in a cysteine-rich domain. The importance of this receptor in virulence has been established by antisense silencing of the adhesin and
by expression of a dominant-negative form of the light subunit. Thus, the adhesin is a potential target to manage E. histolytica infection (see Chapter 40).
end guote
Well, as we can see, these critters use one another and the environment to proliferate in the body.
But more important is to understand the mechanism of diseases in order to:
- prevent weakening of the immune system
- reduce toxic load of whatever origin, be it received from exterior or generated internally by those microorganisms
- use the microorganisms' own metabolism characteristics to prevent their proliferation.
I think that the most important steps are
- paleo/keto diet, as all this critters prime necessity is to adhere to the host cells, and preferred are tissues with high carbohydrate content
- I would also suggest that weekly whole body baths with salt, sodium bicarbonate, borax, magnesium sulfate would help strengthen the immune system, detoxify, reduce overall body acidity/inflammation, also kill germs. Nora Gedgaudas said that transdermal administration is 80% more efficient than assimilation via guts.
- She also, emphasize the role of L-glucosamine in enhancing the secretory IgA response of our endothelium, and tissue repair, which is the body's first line defense. Other similar substances are featured in the above article.
The last sequence quoted contain a rather puzzling remark (at least for me, but I might be mistaken).
quoted again:
PARASITE LECTINS
In addition to viruses and bacteria,
a number of parasites also utilize glycans as receptors for adhesion (Table 34.4).Entamoeba histolytica expresses a 260-kD heterodimeric lectin that
binds to terminal galactose/N-acetylgalactosamine residues on glycoproteins and glycolipids. Binding may have a role in attachment, invasion, and cytolysis of intestinal epithelium,
and it may function in binding the amoeba to bacteria as a food source. The lectin is heterodimeric, with a transmembrane subunit of 170 kD and a glycosylphosphatidylinositol (GPI)-anchored subunit of 35 kD. The glycan-binding site is located in a cysteine-rich domain. The importance of this receptor in virulence has been established by antisense silencing of the adhesin and
by expression of a dominant-negative form of the light subunit. Thus, the adhesin is a potential target to manage E. histolytica infection (see Chapter 40).
It just remembered me something about light-interference to modify DNA, from session of 26 November 1994
A: Light wave alteration.
Q: (L) And light waves, actual light waves, affect DNA?
A: Yes.
Q: (T) What was the origin of the light waves?
A: Our center.
Q: (L) What is your center?
A: Our realm. STO.
Q: (L) So, how did the Lizzies use the light from the Service to Others realm...
A: They used sophisticated technology to interrupt light frequency waves.
..................
A: Are you ready? DNA core is as yet undiscovered enzyme relating to carbon. Light waves were used to cancel the first ten factors of DNA by burning them off. At that point, a number of physical changes took place including knot at top of spine. Each equally reflected in the ethereal.
Maybe, just maybe, this could be also the way we get sick, in order to contact "needed diseases" which will help learn and evolve? Too many people can't learn from it, just stay ill.
It's such a complex situation.
I could use some help to connect the dots here, if any.
FWIW
Joy
