We’ve been looking into how wheat can cause autoimmune diseases other than the “classic” wheat-associated diseases, celiac disease and Hashimoto’s thyroiditis.
The first post in the series discussed how wheat can cause a leaky, permeable gut that lets toxins and bacteria into the body. The second post discussed how wheat can itself generate a variety of auto-antibodies that attack nerves, brain, connective tissue and joints.
Now, we want to look at how wheat can create diseases by binding to other molecules and causing the body to form antibodies to them. Wheat can thereby cause allergies against foods as well as autoimmune attacks on self molecules.
Adjuvant Activity of Wheat Germ Agglutinin
Immunologically speaking, an “adjuvant” is a molecule that when bound to another molecule makes it much more immunogenic. Adjuvants such as aluminum salts are used in vaccines to make the immune system produce antibodies more readily against the target protein. This lowers the vaccine dose needed for immunity.
Wheat germ agglutinin (WGA) is a wheat lectin. (It is not part of gluten.) WGA can act as an adjuvant, causing the body to generate antibodies against proteins that, in isolation, the body would not form antibodies against.
For instance, antibodies against the egg protein ovalbumin are not generated if it enters the body alone, but are generated if it is accompanied by WGA. [1]
So don’t eat toast with your eggs! If you have a leaky gut, the wheat might give you an egg allergy.
Haptenization Activity of Wheat Gliadin
A similar process that helps create auto-antibodies is “haptenization.” The immune system forms antibodies more readily against large molecules than small ones. (This helps avoid autoimmunity, since small molecules are more likely to have similar human peers.)
When two small molecules bind together, so they look like one big one, the immune system is more likely to form antibodies against the large complex. These antibodies may then react against one of the molecules individually, even if it is not paired up. If the targeted molecule is human, then the antibody is an auto-antibody.
One reason wheat gliadin is so disruptive to the body is that it binds strongly to sugars. The average molecule of wheat gliadin is bound to 1 to 2 molecules of glucose and 2 molecules of sialic acid, another sugar. [2] Since a lot of human molecules have sialic acid residues, gliadin can bind to them.
One of the sialic acid-containing molecules gliadin binds to is called GM1 ganglioside. This molecule is found on the intestinal brush border, but it is also found in nerves. When wheat binds to GM1 ganglioside on the intestinal surface, it induces the formation of auto-antibodies that attack the ganglioside in nerves. In 65% of patients with gluten sensitivity and peripheral nerve damage, anti-ganglioside antibodies are found. [2]
Conclusion
Wheat could be a concealed cause of many food allergies, through WGA’s adjuvant activity. If so, then many food allergies may gradually disappear after wheat is given up.
Wheat proteins can also bind to an extraordinarily large number of human proteins, in part by binding to sialic acid or other carbohydrate residues of glycoproteins or glycolipids, and has a chance to induce antibody formation against many of those proteins.
The bewildering array of ways in which wheat can trigger attacks on human tissue makes it impossible to identify all the wheat-caused diseases. The only thing we can say for sure is that if you have a disease, it’s a good idea to give up wheat. You may give up your illness at the same time.
Related Posts
Other posts in this series:
- Wheat Is A Cause of Many Diseases, I: Leaky Gut Oct 26, 2010.
- Why Wheat Is A Concealed Cause of Many Diseases, II: Auto-Antibody Generation Oct 28, 2010.
References
[1] Lavelle EC et al. The identification of plant lectins with mucosal adjuvant activity. Immunology. 2001 Jan;102(1):77-86. http://pmid.us/11168640
[2] Alaedini A, Latov N. Transglutaminase-independent binding of gliadin to intestinal brush border membrane and GM1 ganglioside. J Neuroimmunol. 2006 Aug;177(1-2):167-72. http://pmid.us/16766047.
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