Subscribe to our feed!

Articles of Interest

Ji DarkSideWheat.GreenMedInfo.Store




~ A Critical Appraisal of the Role of Wheat in Human Disease ~

Foreword by Dr. Ron Hoggan, author of Dangerous Grains

Having studied gluten grains and their impact on human health for almost 20 years now, the surprises caused by new insights are more and more rare. Nonetheless, when I read about Sayer Ji's startling perception of wheat germ agglutinin (WGA), and the several pathways by which it can impact our mental and physical health, partly due to its ability to cross protective barriers of the gut and the brain, I was, at first, very skeptical. Further investigation revealed that he really was onto something new. And the implications of this new understanding are, to say the least, dramatic. His work raises legitimate questions about one facet of gluten grains that has largely been ignored by the gastrointestinal research community. It opens windows of understanding. And it provides a different vantage point on these perplexing problems. Here is my promise to you, dear reader: There is a whole new world revealed through Sayer Ji's work. Read on. Enjoy. Puzzle it out. And by the end of your reading, you will wonder how your prior view could have been so simplistic and, perhaps, misguided.

Sir Isaac Newton's famous metaphor (perhaps quoting others) said something to the effect that we see further, not because of any special endowment of our own, but because we are standing on the shoulders of giants. After reading Sayer's work on WGA, I felt as if I had just been boosted to a higher plane from which I could see and understand much, much more. Sayer's insights continue to shape and inform much of my effort to understand the various impacts of grains on human health.

Dr. Ron Hoggan, Ed. D.
Co-author: Dangerous Grains and Cereal Killers
Author: The Iron Edge
Editor: The Journal of Gluten Sensitivity



Part I: New Perspectives On Celiac Disease & Wheat
By Sayer Ji, founder of
The globe-spanning presence of wheat and its exalted status among secular and sacred institutions alike differentiates this food from all others presently enjoyed by humans. Yet, the unparalleled rise of wheat as the very catalyst for the emergence of ancient civilization, has not occurred without a great price. While wheat was the engine of civilization’s expansion and was glorified as a "necessary food," both in the physical (staff of life) and spiritual sense (the body of Christ), those suffering from celiac disease are living testimony to the lesser known dark side of wheat. A study of celiac disease (CD) may help unlock the mystery of why modern man, who dines daily at the table of wheat, is the sickest animal yet to have arisen on this strange planet of ours.


CD was once considered an extremely rare affliction, limited to individuals of European descent. Today, however, a growing number of studies indicate that CD is found throughout the world at a rate of up to one in every 100 persons, which is several orders of magnitude higher than previously estimated.

These findings have led researchers to visualize CD as an iceberg. The tip of the iceberg represents the relatively small number of the world’s population whose gross presentation of clinical symptoms often leads to the diagnosis of CD. This is the classical case of CD characterized by gastrointestinal symptoms, malabsorption and malnourishment. It is confirmed with the "gold standard" of an intestinal biopsy. The submerged middle portion of the iceberg is largely invisible to classical clinical diagnosis, but not to modern serological screening methods in the form of antibody testing. This middle portion is composed of asymptomatic and latent celiac disease, as well as ‘out of the intestine’ varieties of wheat intolerance. Finally, at the base of this massive iceberg, sits approximately 20-30% of the world’s population – those who have been found to carry the HLA-DQ locus of genetic susceptibility to celiac disease on chromosome

The "Celiac Iceberg" may not simply illustrate the problems and issues associated with diagnosis and disease prevalence, but may represent the need for a paradigm shift in how we view both CD and wheat consumption among non-CD populations.

First, let us address the traditional view of CD as a rare, but clinically distinct species of genetically-determined disease, which I believe is now running itself aground upon the emerging, post-genomic perspective, whose implications for understanding and treating disease are Titanic in proportion.


Despite common misconceptions, monogenic diseases, or diseases that result from errors in the nucleotide sequence of a single gene are exceedingly rare. Perhaps only 1% of all diseases fall within this category, and CS is not one of them. In fact, following the completion of the Human Genome Project (HGP) in 2003, it is no longer accurate to say that our genes alone "cause" disease, any more than it is accurate to say that DNA is alone sufficient to account for all the proteins in our body. Despite initial expectations, the HGP revealed that there are only 20,000-
23,000 genes in human DNA (genome), rather than the 100,000+ believed necessary to encode the 100,000+ proteins found in the human body (proteome).

The "blueprint" model of genetics: one gene > one protein > one cellular behavior, which was once the holy grail of biology, has now been supplanted by a model of the cell where epigenetic factors (literally: "above the control of the gene") are primary in determining how DNA will be interpreted, translated and expressed. A single gene can be used by the cell to express a multitude of proteins and it is not the DNA itself that determines how or what genes will be
expressed. Rather, we must look to the epigenetic factors to understand what makes a liver cell different from a skin cell or brain cell. All of these cells share the exact same three billion base
pairs that make up our DNA code, but it is the epigenetic factors, e.g. regulatory proteins such as miRNA and post-translational modifications, that make the determination as to which genes to turn on and which to silence, resulting in each cell’s unique phenotype. Moreover, epigenetic factors are directly and indirectly influenced by the presence or absence of key nutrients in the diet, as well as exposures to chemicals, pathogens and other environmental influences.
In a nutshell, what we eat and what we are exposed to in our environment directly affect our
DNA and its expression.

Within the scope of this new perspective, even classical monogenic diseases like cystic fibrosis (CF) can be viewed in a new, more promising light. In CF, many of the adverse changes that result from the defective expression of the Cystic Fibrosis Transmembrane Conductance Regulator (CFTR) gene may be preventable or reversible, owing to the fact that the misfolding of the CFTR gene product has been shown to undergo partial or full correction (in the rodent
model) when exposed to phytochemicals found in turmeric (curcumin), cayenne (capsiacan), and soybean (genistein). Moreover, nutritional deficiencies of seleniun, zinc, riboflavin, vitamin E, etc. in the womb or early in life, may "trigger" the faulty expression or folding patterns of the CFTR gene in CF which might otherwise have avoided epigenetic activation. This would explain why it is possible to live into one’s late seventies with this condition, as was the case for Katherine Shores (1925-2004). The implications of these findings are rather extraordinary: epigenetic and not genetic factors are primary in determining disease outcome. Even if we exclude the possibility of reversing certain monogenic diseases, the basic lesson from the post- Genomic era is that we can’t blame our DNA for causing disease. Rather, it may have more to do with what we choose to expose our DNA to.


What all of this means for CD is that the genetic susceptibility locus, HLA DQ, does not determine the exact clinical outcome of the disease. Instead of being the cause, the HLA genes may be activated as consequence of the disease process. Thus, we may need to shift our epidemiological focus from viewing this as a classical "disease" involving a passive subject controlled by aberrant genes, to viewing it as an expression of a natural, protective response to the ingestion of something that the human body was not designed to consume.

If we view CD not as an unhealthy response to a healthy food, but as a healthy response to an unhealthy food, classical CD symptoms like diarrhea may make more sense.  Diarrhea can be the body’s way of reducing the duration of toxic or pathogenic exposure, and villous atrophy the body’s way of preventing the absorption.  Therefore, these symptoms might be considered the systemic effects of chronic exposure to wheat.

I believe we would be better served by viewing the symptoms of CD as expressions of bodily intelligence rather than deviance. We must shift the focus back to the disease trigger, which is wheat itself.

People with CD may actually have an advantage over the apparently unafflicted. Those who are "non-symptomatic" and whose wheat intolerance goes undiagnosed or misdiagnosed because they lack the classical symptoms may suffer in ways that are equally or more damaging, but expressed more subtly, or in distant organs.  Given the nature of these more “mysterious” atypical symptoms, a situation may be created that sends the person suffering along a potentially frustrating path to reach a solid diagnosis.  Within this view, CD would be redefined as a protective (healthy?) response to exposure to an inappropriate substance, whereas “asymptomatic” ingestion of the grain with its concomitant “out of the intestine” and mostly silent symptoms, would be considered the unhealthy response insofar as it does not signal, in an obvious and acute manner, that there is a problem with consuming wheat.

It is possible that CD represents both an extreme reaction to a global, human species-specific intolerance to wheat that we all share in to varying degrees. CD symptoms may reflect the body’s innate intelligence when faced with the consumption of a substance that is inherently toxic. Let me illustrate this point using the lectin wheat germ agglutinin (WGA) as an example.
WGA is classified as a lectin and is known to play a key role in kidney pathologies, such as IgA nephropathy. In the article: "Do dietary lectins cause disease?" the allergist David L. J. Freed points out that WGA binds to "glomerular capillary walls, mesangial cells and tubules of human kidney and (in rodents) binds IgA and induces IgA mesangial deposits," indicating that wheat consumption may lead to kidney damage in susceptible individuals. This is not the only study linking wheat to kidney disease. For instance, a study from the Mario Negri Institute for Pharmacological Research in Milan, Italy, published in 2007 in the International Journal of Cancer, looked at bread consumption and the risk of kidney cancer. They found that those who consumed the most bread had a 94% higher risk of developing kidney cancer compared to those who consumed the least bread.

Given the inherently toxic effect that WGA may have on kidney function, it is possible that in certain genetically predisposed individuals (e.g. HLA-DQ2/DQ8), the body – in its innate intelligence – makes an executive decision: either continue to allow damage to the kidneys (or possibly to other organs) until kidney failure and rapid death result, or launch an autoimmune attack on the villi to prevent the absorption of the offending substance which results in a prolonged though relatively malnourished life. This is the explanation typically given for the body’s reflexive formation of mucous following exposure to certain highly allergenic or potentially toxic foods, e.g. dairy products, sugar, etc.? The mucous coats the offending substance, preventing its absorption and facilitating safe elimination via the gastrointestinal tract.  From this perspective, the HLA-DQ locus of disease susceptibility in the celiac is not simply activated, but utilized as a defensive adaptation to continual exposure to a harmful substance. In those who do not have the HLA-DQ locus, an autoimmune destruction of the villi will not occur as rapidly, and exposure to the universally toxic effects of WGA will likely go unabated until silent damage to distant organs leads to the diagnosis of a disease that is apparently unrelated to wheat consumption.

Loss of kidney function, therefore, may only be the "tip of the iceberg" when it comes to the possible adverse effects that wheat proteins and wheat lectin can generate in the body. If kidney cancer is a likely possibility, then other cancers may eventually be linked to wheat consumption as well. This correlation would fly in the face of globally sanctioned and reified assumptions about the inherent benefits of wheat consumption. It would require that we suspend cultural, socio-economic, political and even religious assumptions about its inherent benefits. In many
ways, the reassessment of the value of wheat as a food requires a William Boroughs-like moment of shocking clarity when we perceive "in a frozen moment….what is on the end of every
fork." Let’s take a closer look at what is on the end of our forks.


In a previous article, I discussed the role that wheat plays as an industrial adhesive (e.g. paints, paper mache’, and book binding glue) in order to illustrate the point that it may not be such a good thing for us to eat. The problem is implicit in the word gluten, which literally means "glue" in Latin and in words like pastry and pasta, which derives from wheatpaste, the original concoction of wheat flour and water which made such good plaster in ancient times. What gives gluten its adhesive and difficult-to-digest qualities are the high levels of disulfide bonds it contains. These same sulfur-to-sulfur bonds are found in hair and vulcanized rubber products, which we all know are difficult to decompose and are responsible for the sulfurous odor they give off when burned.

Each year approximately 700 million metric tons of wheat are produced around the arable surface of the globe, making it the primary cereal of temperate regions and third most prolific cereal grass on the planet. This global dominance of wheat is signified by the Food & Agricultural Organization’s (FAO) (the United Nation’s international agency for defeating hunger) use of a head of wheat as its official symbol, with the motto “Fiat Panis,” literally, “let there be bread.” Any effort to indict the credibility of this "king of grains" will prove challenging. As Rudolf Hauschka once remarked, wheat is "a kind of earth-spanning organism." It has vast socio-economic, political, and cultural significance.   For example, in the Catholic Church, a wafer made of wheat was long considered irreplaceable as the embodiment of Christ.
Our dependence on monocultured wheat is matched only by its dependence on us. As Europeans have spread one-culture (monoculture) across the planet, so has this grain. We have assumed total responsibility for all phases of the wheat life cycle: from fending off its pests; to providing its ideal growing conditions; to facilitating reproduction and expansion into new territories. We have become so inextricably interdependent that neither species is perceived as sustainable at current population levels without this symbiotic relationship.

It is this codependence that may explain why our culture has, for so long, consistently confined wheat intolerance to categorically distinct, "genetically-based" diseases like "celiac." These categorizations may protect us from the realization that wheat exerts a vast number of deleterious effects on human health in the same way that "lactose intolerance" distracts attention from the deeper problems associated with the casein protein found in cow’s milk. [For additional evidence of this view the over 200 adverse health effects linked to wheat consumption on the GreenMedInfo wheat toxicity database]. Rather than see wheat for what it very well may be: a biologically inappropriate food source, we "blame the victim," and look for genetic explanations for what’s wrong with small subgroups of our population who have the most obvious forms of intolerance to wheat consumption, e.g. celiac disease, dermatitis herpetiformis, etc.   The medical justification for these classifications may be secondary to economic and cultural imperatives that require the inherent problems associated with wheat consumption to be minimized or occluded.

In all probability, the celiac genotype represents a surviving vestigial branch of a once universal genotype, which, through accident or intention, have resulted in, through successive generations, only limited exposure to wheat. The celiac genotype, no doubt, survived through numerous bottlenecks or "die offs" represented by a dramatic shift from hunted and foraged/gathered foods to gluten-grain consumption and, for whatever reason, simply did not have adequate time to adapt or remove the gluten-grain incompatible genes. The celiac response may indeed reflect a prior, species-wide intolerance to a novel food source: the seed storage form of the monocotyledonous cereal grasses which our species only began consuming 1-500 generations ago at the advent of the Neolithic transition (10-12,000 BC). Let us return to the image of the celiac iceberg for greater clarification.


The iceberg metaphor is an excellent way to expand our understanding of what was once considered to be an extraordinarily rare disease into one that has statistical relevance for us all, but it has a few limitations. For one, it reiterates the commonly held view that celiac disease is a numerically distinct disease entity or "disease island," floating alongside other numerically distinct disease "ice cubes" in the vast sea of normal health. Though accurate in describing the sense of social and psychological isolation many of the afflicted feel, the celiac iceberg/condition may not be a distinct disease entity at all.

Although the HLA-DQ locus of disease susceptibility on chromosome 6 offers us a place to project blame, I believe we need to shift the emphasis of responsibility for the condition back to the disease "trigger" itself: namely, wheat and other prolamine-rich grains, e.g. barley, rye, spelt, and oats. Without these grains, the typical afflictions we call celiac disease would not exist. Within the scope of this view, the “celiac iceberg” is not actually free-floating, but an outcropping from an entire submerged subcontinent, representing our long-forgotten (cultural time), but relatively recent metabolic prehistory as hunters-and-gatherers (biological time),
where grain consumption was, in all likelihood, non-existent, except in instances of near- starvation.  The pressure on the celiac to be viewed as an exceptional case or deviation may have everything to do with our preconscious belief that wheat, and grains as a whole, are the "health foods," and very little to do with a rigorous investigation of the facts.

Grains have been heralded since time immemorial as the "staff of life," when in fact, they are more accurately described as a cane, precariously propping up a body starved of the nutrient- dense, low-starch vegetables, fruits, edible seeds and meats, they have so thoroughly supplanted (c.f. Paleolithic Diet). Most of the diseases of affluence, e.g. type 2 diabetes, coronary heart disease, cancer, etc. can be linked to a grain-based diet, including secondary "hidden sources" of grain consumption in grain-fed fish, poultry, meat and milk products.

Our modern belief that grains make for good food, is simply not supported by the facts. The cereal grasses are within an entirely different super family: monocotyledonous (one-leafed embryo) than that from which our body sustained itself for millions of years: dicotyledonous (two-leafed embyro). The preponderance of scientific evidence points to a human origin in the tropical rainforests of Africa where dicotyledonous fruits would have been available for year- round consumption. It would not have been monocotyledonous plants, but the flesh of hunted animals that would have allowed for the migration from Africa 60,000 years ago into the northern latitudes where vegetation would have been sparse or non-existent during winter months. Collecting and cooking grains would have been improbable given the low  nutrient and caloric content of grains, inadequate development of pyrotechnology (“cooking”) and associated cooking utensils necessary to efficiently consume them. It was not until the end of the last Ice Age, 20,000 years ago that our human ancestors would have slowly transitioned to a cereal
grass-based diet that evolved with emergence of civilization.  20,000 years is probably not enough time to fully adapt to the consumption of grains. Even animals like cows with a head start of thousands of years, evolved to graze on monocotyledons, equipped as ruminants with their four-chambered fore-stomach enabling the breakdown of cellulose and anti-nutrient rich plants, are not designed to consume grains. Cows are designed to consume the sprouted mature form of the grasses and not their seed storage form. Grains are so acidic/toxic in reaction that exclusively grain-fed cattle are prone to developing severe acidosis and subsequent liver abscesses and infections, etc. Feeding wheat to cattle provides an even greater challenge:

"Beef:  Feeding wheat to ruminants requires some caution as it tends to be more apt than other cereal grains to cause acute indigestion in animals which are unadapted to it. The primary problem appears to be the high gluten content of which wheat in the rumen can result in a "pasty" consistency to the rumen contents and reduced rumen motility."
(source: Ontario Ministry of Agriculture, Food & Rural Affairs)

Seeds, after all, are the "babies" of these plants, and are invested with not only the entire hope for continuance of their species, but contain a vast armory of anti-nutrients to help them accomplish this task: toxic lectins, phytates and oxalates, alpha-amalyase and trypsin inhibitors, and endocrine disrupters. These not so appetizing phytochemicals enable plants to resist predation of their seeds, or at least, prevent them from "going out without a punch."


Wheat presents a special case insofar as wild and selective breeding has produced variations which include up to six sets of chromosomes (3x the human genome worth!), capable of generating a massive number of proteins each with a distinct potentiality for antigenicity. Common bread wheat (Triticum aestivum), for instance, has over 23,788 proteins cataloged thus far. In fact, the genome for common bread wheat is actually 6.5 times larger than that of the human genome!

With up to a 50% increase in gluten content of some varieties of wheat versus their ancient predecessors, it is amazing that we continue to consider "glue-eating" a normal behavior; whereas wheat avoidance is left to the "celiac", still perceived by most health care practitioners as exhibiting a "freak" reaction to the consumption of something intrinsically wholesome.

Thankfully, we don’t need to rely on our intuition, or even (not so) common sense to draw conclusions about the inherently unhealthy nature of wheat. A wide range of investigation has occurred over the past decade revealing the problem with the alcohol-soluble protein component of wheat known as gliadin; the glycoprotein known as lectin (wheat germ agglutinin (WGA)); the opioid-like peptides known as gluten exorphins and gliadomorphin, and the excitotoxic potentials of high levels of aspartic and glutamic acid found in wheat. Add to these, the anti- nutrients found in grains such as phytates, enzyme inhibitors, etc. and you have a substance which we may more appropriately consider the farthest thing from wholesome.
The remainder of this article will demonstrate the following adverse effects of wheat on both celiac and non-celiac populations: 1) wheat causes damage to the intestines 2) wheat causes intestinal permeability 3) wheat has pharmacologically active properties 4) wheat causes damage that is "out of the intestine", affecting distant organs 5) wheat induces molecular mimicry 6) wheat contains high concentrations of excitoxins.


Gliadin is classified as a prolamin, which is a wheat storage protein high in the amino acids proline and glutamine and soluble in strong alcohol solutions. Gliadin, once deamidated by the enzyme tissue transglutaminase, is considered the primary epitope for T-cell activation and subsequent autoimmune destruction of intestinal villi. Yet, gliadin does not need to activate an autoimmune response, e.g. celiac disease, in order to have a deleterious effect on intestinal tissue.

In a study published in GUT in 2007, a group of researchers asked the question: "Is gliadin really safe for non-coeliac individuals?"   In order to test the hypothesis that an innate immune response to gliadin is common in patients with celiac disease and without celiac disease, intestinal biopsy cultures were taken from both groups and challenged with crude gliadin, the gliadin synthetic 19-mer (19 amino acid long gliadin peptide) and 33-mer deamidated peptides. Results showed that all patients with or without celiac disease, when challenged with the various forms of gliadin, produced an interleukin-15-mediated response. The researchers concluded:
"The data obtained in this pilot study supports the hypothesis that gluten elicits its harmful effect, throughout an IL15 innate immune response, on all individuals [my italics]."

The primary difference between the two groups is that the celiac disease (CD) patients experienced both an innate and an adaptive immune response to the gliadin, whereas the non- celiacs experienced only the innate response.   The researchers hypothesized that the difference between the two groups may be attributable to greater genetic susceptibility at the HLA-DQ locus for triggering an adaptive immune response, higher levels of immune mediators or receptors, or perhaps greater permeability in the celiac intestine. It is possible that over and
above the possibility of greater genetic susceptibility, most of the differences are from epigenetic factors that are influenced by the presence or absence of certain nutrients in the diet. Other
factors such as exposure to NSAIDs like naproxen or aspirin can profoundly increase intestinal permeability in the non-celiac, rendering them susceptible to gliadin’s potential for activating secondary adaptive immune responses. This may explain why, in up to 5% of all cases of classically defined celiac disease, the typical HLA-DQ haplotypes are not found. However, determining the factors associated with greater or lesser degrees of susceptibility to gliadin’s intrinsically toxic effect should be secondary to the fact that it has been demonstrated to be toxic to both non-celiacs and celiacs.

Gliadin upregulates the production of a protein known as zonulin, which modulates intestinal
permeability. Over-expression of zonulin is involved in a number of autoimmune disorders,
including CD and type 1 diabetes. Researchers have studied the effect of gliadin on increased
zonulin production and subsequent gut permeability in both celiac and non-celiac intestines, and
have found that "gliadin activates zonulin signaling irrespective of the genetic expression of
autoimmunity, leading to increased intestinal permeability to macromolecules."10     These results indicate, once again, that a pathological response to wheat gluten is a normal or human, species- specific response, and is not based entirely on genetic susceptibilities. Since intestinal permeability is associated with a wide range of disease states, including cardiovascular illness, liver disease and many autoimmune disorders, I believe this research indicates that gliadin (and therefore, wheat) should be avoided as a matter of principle.

Gliadin can be broken down into various amino acid lengths or peptides. Gliadorphin is a 7
amino acid long peptide: Tyr-Pro-Gln-Pro-Gln-Pro-Phe which forms when the gastrointestinal
system is compromised. When digestive enzymes are insufficient to break gliadorphin down into
2-3 amino acid lengths and a compromised intestinal wall allows for the leakage of the entire 7
amino acid long fragment into the blood, glaidorphin can pass through to the brain through circumventricular organs and activate opioid receptors resulting in disrupted brain function.

There have been a number of gluten exorphins identified: gluten exorphin A4, A5, B4, B5 and C, and many of them have been hypothesized to play a role in autism, schizophrenia, ADHD and related neurological conditions.   In the same way that the celiac iceberg illustrated the illusion that intolerance to wheat is rare, it is possible, even probable, that wheat exerts pharmacological influences on everyone. What distinguishes the schizophrenic or autistic individual from the functional wheat consumer is the degree to which they are affected.

Below the tip of the “Gluten Iceberg,” we might find that these opiate-like peptides are responsible for bread’s general popularity as a "comfort food", and our use of phrases like "I love bread," or "this bread is to die for" to be indicative of wheat’s narcotic properties. I believe a strong argument can be made that the agricultural revolution that occurred approximately 10-
12,000 years ago as we shifted from the Paleolithic into the Neolithic era, was precipitated as much by environmental necessities and human ingenuity, as it was by the addictive qualities of psychoactive peptides in the grains themselves.

The world-historical reorganization of society, culture and consciousness accomplished through the symbiotic relationship with cereal grasses, may have had as much to do with our ability to master agriculture, as to be mastered by it.   The presence of pharmacologically active peptides would have further sweetened the deal, making it hard to distance ourselves from what became a global fascination with wheat.

An interesting example of wheat’s addictive potential pertains to the Roman army. The Roman
Empire was once known as the "Wheat Empire," with soldiers being paid in wheat
rations. Rome’s entire war machine, and its vast expansion, was predicated on the availability of
wheat. Forts were actually granaries, holding up to a year’s worth of grain in order to endure
sieges from their enemies. Historians describe soldiers’ punishment included being deprived of
wheat rations and being given barley instead.  An entire political strategy was developed called
“Bread and Circuses,” based on both entertaining (Coloseum) and feeding (free bread) the
masses into submission.The Roman Empire went on to facilitate the global dissemination of
wheat cultivation which fostered a form of imperialism with biological as well as cultural roots.

The Roman appreciation for wheat, like our own, may have had less to do with its nutritional value as "health food" than its ability to generate a unique narcotic reaction. It may fulfill our hunger while generating a repetitive, ceaseless cycle of craving more of the same, and by doing so, enabling the surreptitious control of human behavior. Other researchers have come to similar conclusions. According to the biologists Greg Wadley & Angus Martin:

“Cereals have important qualities that differentiate them from most other drugs. They are a food source as well as a drug, and can be stored and transported easily. They are ingested in frequent small doses (not occasional large ones), and do not impede work performance in most people. A desire for the drug, even cravings or withdrawal, can be confused with hunger. These features make cereals the ideal facilitator of civilization (and may also have contributed to the long delay in recognizing their pharmacological properties).”

Wheat contains a lectin known as wheat germ agglutinin (WGA) which is responsible for
causing direct, non-immune mediated damage to our intestines, and subsequent to entry into the
bloodstream, results in damage to distant organs in our body.

Lectins are sugar-binding proteins which are highly selective for their sugar moieties. It is believed that wheat lectin, which binds to the monosaccharide N-acetyl glucosamine (NAG), provides defense against predation from bacteria, insects and animals. Bacteria have NAG in their cell wall, insects have an exoskeleton composed of polymers of NAG called chitin, and the epithelial tissue of mammals, e.g. gastrointestinal tract, have a "sugar coat" called the glycocalyx which is composed, in part, of NAG. The glycocalyx can be found on the outer surface (apical portion) of the microvilli within the small intestine.
There is evidence that WGA may cause increased shedding of the intestinal brush border membrane, reduction in surface area, acceleration of cell losses and shortening of villi, via binding to the surface of the villi. WGA can mimic the effects of epidermal growth factor (EGF) at the cellular level, indicating that the crypt hyperplasia seen in CD may be due to a mitogenic reponse induced by WGA. WGA has been implicated in obesity and "leptin resistance" by blocking the receptor in the hypothalamus for the appetite-satiating hormone leptin. WGA has also been shown to have an insulin-mimetic action, potentially contributing to weight gain and insulin resistance.15     And, as discussed earlier, wheat lectin has been shown to induce IgA mediated damage to the kidney, indicating that nephropathy and kidney cancer may be
associated with wheat consumption.

Gliadorphin and gluten exporphins exhibit a form of molecular mimicry that affects the nervous
system, but other wheat proteins affect different organ systems. The digestion of gliadin
produces a peptide that is 33 amino acids long and is known as 33-mer which has a remarkable
homology to the internal sequence of pertactin, the immunodominant sequence in the Bordetella
pertussis bacteria (whooping cough). Pertactin is considered a highly immunogenic virulence
factor and is used in vaccines to amplify the adaptive immune response. It is possible that the
immune system may confuse this 33-mer with a pathogen resulting in either a cell-mediated
and/or adaptive immune response against self.

John B. Symes, D.V.M. is responsible for drawing attention to the potential excitotoxicity of
wheat, dairy, and soy, due to their exceptionally high levels of the non-essential, glutamic and
aspartic amino acids. Excitotoxicity is a pathological process where glutamic and aspartic acids
cause an over-activation of the nerve cell receptors (e.g. NMDA and AMPA receptors) leading to
calcium-induced nerve and brain injury.   Of all cereal grasses commonly consumed, wheat
contains the highest levels of glutamic acid and aspartic acid. Glutamic acid is largely
responsible for wheat’s exceptional taste. The Japanese coined the word umami to describe the
extraordinary "yummy" effect that glutamic acid exerts on the tongue and palate and invented
monosodium glutamate (MSG) to amplify this sensation. Though the Japanese first synthesized
MSG from kelp, wheat can also be used due to its high glutamic acid content.   It is likely that
wheat’s popularity, alongside its opiate-like activity, has everything to do with the natural flavor-
enhancers already contained within it. These amino acids may contribute to neurodegenerative
conditions such as multiple sclerosis, Alzheimer’s disease, Huntington’s disease, and other
nervous disorders such as epilepsy, attention deficit disorder and migraines.

In this article, I have proposed that celiac disease be viewed not as a rare "genetically-
determined" disorder, but as an extreme example of our body’s communicating to us a once
universal, species-specific affliction: severe intolerance to wheat. Celiac disease reflects how
profoundly our diet has diverged from what was, until only recently, a grain-free diet and even
more recently, a wheat-free one. We are so profoundly distanced from that dramatic Neolithic
transition in cultural time that "missing is any sense that anything is missing." The body, on the
other hand, cannot help but remember a time when cereal grains were alien to the diet because in
biological time, it was only moments ago.

Eliminating wheat, if not all of the members of the cereal grass family and returning to dicotyledons or pseudo-grains like quinoa, buckwheat and amaranth, may help us roll back the hands of biological and cultural time, to a time of clarity, health and vitality that many of us have never known before. When one eliminates wheat and fills the void left by its absence with fruits, vegetables, high-quality meats and foods consistent with our biological needs, we may begin to feel a sense of vitality that many would find hard to imagine. If wheat really is more like a drug than a food, anesthetizing us to its ill effects on our body, it will be difficult for us to understand its grasp upon us unless and until we eliminate it from our diet. I encourage everyone to see
celiac disease not as a condition alien to our own. Rather, the celiac disease condition gives us a glimpse of how profoundly wheat may distort and disfigure our health if we continue to expose
ourselves to its ill effects. I hope this article will provide inspiration for non-celiacs to try a wheat free diet and judge for themselves if it is really worth eliminating.




* Genome screening of coeliac disease [7]

[1]       Lebenthal, Emanuel, David Branski, “Celiac Disease: An Emerging Global Problem”, Journal of Pediatric Gastroenterology & Nutrition, Philadelphia: Lippincott Williams & Wilkins, 2002, Disease: An Emerging Global Problem.4.aspx, accessed April 2008.

[2]       Richard Logan is responsible for first introducing the "Celiac  Iceberg" metaphor in 1991

[3]       Antibody testing for gliadin, tissue transglutaminase and endomysium indicates that "silent" or "latent" celiac disease is up to 100 times more frequent than represented by the classical form.

[4]       Fasano, A., R. Troncone, D. Branski, Frontiers in Celiac Disease,  Canton Basel: Karger Publishers, 2008,, accessed February 2008.

[5]       See: [10] for      Medline citations.

[6]       Wallach, J.D., B. Germaise, Cystic Fibrosis: A Perinatal Manifestation of Selenium Deficiency, Columbia: University of Missouri       Press, 1979.      6736(85)90761-5/fulltext, accessed March 2008.

[7]       Mustalahti, K., P. Holopainen, K. Karell, M. Maki, J. Partanen,           “Genetic Dissection Between Silent and Clinically Diagnosed Symptomatic Forms of Coeliac Disease in Multiplex Families”, Digestive and Liver Disease,  Amsterdam: Elsevier BV,  2002,, accessed December  2007.

[8]       Diosdado, Begona, Erica van Oort, Cisca Wijmenga, “’Coelionomics’: Towards Understanding the Molecular Pathology of Coeliac Disease”, Clinical  Chemistry and Laboratory Medicine,  Boston and Berlin: Walter de Gruyter, Inc. Publishers,
2005, l, accessed March 2008.

[9]       Bernardo, D., J. A. Garrote, L. Fernandez-Salazar, S. Riestra, E. Arranz, “Is Gliadin Really Safe for Non-coeliac Individuals?  Production of Interleukin 15 in Biopsy Culture from Non-coeliac Individuals Challenged with  Gliadin Peptides”, GUT, London:  Gut Pathogens, 2007,,  accessed January       2008.
[10]    Freed, David L. J., “Do Dietary Lectins Cause Disease?”, BMJ, London: BMJ Group,1999,,      accessed February 2008.

[11]     Bravi, F., C. Bosetti, L. Scotti, R. Talamini, M. Montella, V. Ramazzotti,        E.
Negri, S. Franceschi, C. LaVecchia, “Food Groups and Renal Cell Carcinoma: a
Case-Control Study from Italy.”,  International Journal of Cancer, Hoboken: Wiley-
Blackwell, 2007,, accessed January

[12]     Ji, Sayer, “Unglued: The Sticky Truth About Wheat, Dairy, Corn and Soy”,, Santa Rosa: Scott Adams, 2008, Corn-and-Soy/Page1.html, accessed March 2008.

[13]     Vandepoele, Klaas, Yvew Van de Peer, “Exploring the Plant     Transcriptome Through Phylogenetic Profiling”, Plant Physiology,  Rockville: American Society of Plant Biologists, 2005,, accessed December 2007.

[14]     Nicholl, Desmond S. T., An Introduction to Genetic Engineering, New   York: Cambridge University Press, 2002, Engineering-Desmond-Nicholl/dp/0521615216, accessed March 2008.

[15]     Mustalahti, K., P. Holopainen, K. Karell, M. Maki, J. Partanen, “Genetic Dissection Between Silent and Clinically Diagnosed Symptomatic Forms of Coeliac Disease in Multiplex Families”, Digestive and Liver Disease.

[16]     Drago, S., R. El Asmar, M. DiPierro, Clemente M. Grazia, A. Tripathi, A. Sapone, M. Thakar, G. Iacono, A. Carroccio, C. D’Agate, T. Not, L.Zampini, C. Catassi, A. Fassano, “Gliadin, Zonulin and Gut Permeability: Effects on Celiac and  Non-celiac Intestinal Mucosa and Intestinal Cell Lines”, Scandinavian Journal of Gastroenterology, London:  Informa Healthcare, 2006,, accessed February 2008.

[17]     Wadley, Greg and Angus Martin, “The Origins of Agriculture: a Biological Perspective and a New Hypothesis”, Australian Biologist, Milton: Australian Institute of Biology, Inc., 1993,, accessed February 2008.

[18]     Lorenzsonn, V., W.A. Olsen, “In Vivo Responses of Rat Intestinal Epithelium to Intraluminal Dietary Lectins”,  Gastroenterology,  Amsterdam: Elsevier B.V., 1982,, accessed March 2008.

[19]     Faith-Magnusson, K., K.E. Magnusson, “Elevated Levels of Serum      Antibodies to the Lectin Wheat Germ Agglutinin in Celiac Children Lend      Support to the Gluten-lectin Theory of Celiac Disease”, Pediatric Allergy and   Immunology,  New Rochelle: Mary Ann Liebert, Inc., publishers, 1995,, accessed February 2008.
[20]     Jonsson, T., S. Olsson, B. Ahren, T.C. Bog-Hansen, A. Dole, S. Lindeberg, “Agrarian Diet and Diseases of Affluence—Do evolutionary Novel Dietary Lectins Cause Leptin Resistance?”, BMC Endocrine Disorders, London: BioMed Central, Ltd., 2005,, accessed January 2008.

[21]     Messina, J. L., Manlin, J., J. Larner, “Insulin-mimetic Actions of Wheat Germ Agglutinin and Concanavalin A on Specific mRNA Levels”, Archives of Biochemistry and Biophysics,  Amsterdam: Elsevier B.V., 1987,, accessed November 2007.


Part II: Opening Pandora’s Bread Box: The Critical Role of Wheat Lectin in Human Disease
By Sayer Ji, founder of

Now that celiac disease has been allowed official entry into the annals of established medical conditions, and gluten intolerance is no longer entirely a fringe medical concept, the time has come to draw attention to the powerful little chemical in wheat known as 'wheat germ agglutinin' (WGA) which is largely responsible for many of wheat's pervasive, and difficult-to-diagnose, ill effects. Not only does WGA throw a monkey wrench into our assumptions about the primary causes of wheat intolerance, it also pulls the rug out from under one of the health food industry's favorite poster children since high concentrations of WGA is found in "whole wheat," including its supposedly superior sprouted form.  Below the radar of conventional serological testing for antibodies against various gluten proteins and genetic testing for disease susceptibility, the WGA "lectin problem" remains almost entirely obscured. Lectins, though found in all grains, seeds, legumes, dairy and our beloved nightshades: the tomato and potato, are rarely connected with health or illness, even when their consumption may greatly reduce both the quality and length of our lives.

Although significant progress has been made in exposing the dark side of wheat over the past decade, gluten receives a disproportionate share of the attention. Given that modern bread wheat (Triticum aestivum) is an allohexaploid species containing six distinct sets of chromosomes capable of producing well over 23,000 unique proteins, it is not surprising that we are only now beginning to unravel the complexities of this plant’s many secrets. [1] What is unique about WGA is that it can do direct damage to the majority of tissues in the human body without requiring a specific set of genetic susceptibilities and/or immune-mediated articulations. This may explain why chronic inflammatory and degenerative conditions are endemic to wheat- consuming populations even when overt allergies or intolerances to wheat gluten appear exceedingly rare. The future fate of wheat consumption and, by implication, our health, may depend largely on whether or not the toxic qualities of WGA come to light within the general population.

Nature engineers, within all species, a set of defenses against predation, though not all are as obvious as the thorns on a rose or the horns on a rhinoceros. Plants do not have the cell-mediated immunity of higher life forms, like ants, nor do they have the antibody-driven, secondary
immune systems of vertebrates with jaws. Therefore, they must rely on a much simpler, innate immunity. It is for this reason that seeds of the grass family, e.g. rice, wheat, spelt, rye, have exceptionally high levels of defensive sugar-binding proteins known as lectins, which function much like "invisible thorns." Cooking, sprouting, fermentation and digestion are the traditional
ways in which people, for instance, deal with the various anti-nutrients found within this family of plants, However, lectins are, by design, particularly resistant to degradation through a wide range of pH and temperatures.

WGA lectin is an exceptionally tough adversary as it is formed by the same disulfide bonds that make vulcanized rubber and human hair so strong, flexible and durable. Like synthetic pesticides, lectins are extremely small, resistant to decomposition by living systems, and tend to accumulate and incorporate into tissues where they interfere with normal biological processes. Indeed, WGA lectin is so powerful as an insecticide that biotech firms have used recombinant DNA technology to create genetically modified WGA-enhanced plants. We can only hope that these virtually unregulated biotech companies, in the business of playing God with the genetic infrastructure of life, will realize the potential harm to humans that such genetic modifications can cause.

Lectins are sugar-binding proteins and, through thousands of years of selectively breeding wheat for increasingly larger quantities of protein, the concentration of WGA lectin has increased proportionately. This, no doubt, has contributed to wheat’s global dominance as one of the world’s favored monocultures, offering additional "built-in" pest resistance. The word lectin comes from the same etymological root as the word select, and literally means "to choose." Lectins are designed "to choose" specific carbohydrates that project from and attach to the
surface of cells. In the case of WGA, the two glycoproteins it selects, in order of greatest affinity, are N-Acetyl Glucosamine and N-Acetylneuraminic acid (sialic acid).

WGA is nature's ingenious solution for protecting the wheat plant from the entire gamut of its natural enemies. Fungi have cell walls composed of a polymer of N-Acetylglucosamine. The cellular walls of bacteria are made from a layered structure called the peptidoglycan, a biopolymer of N-Acetylglucosamine. N-Acetylglucosamine is the basic unit of the biopolymer chitin, which forms the outer coverings of insects and crustaceans (shrimp, crab, etc.). All animals, including worms, fish, birds and humans, use N-Acetyglucosamine as a foundational substance for building the various tissues in their bodies, including the bones. The production of cartilage, tendons, and joints depends on the structural integrity of N-Acetylglucosamine. The mucous known as the glycocalyx, or literally, "sugar coat" is secreted in humans by the epithelial cells which line all the mucous membranes, from nasal cavities at the top to the alimentary tube
at the bottom, as well as the protective and slippery lining of our blood vessels. The glycocalyx
is composed largely of N-Acetylglucosamine and N-Acetylneuraminic acid (also known as sialic
acid), with carbohydrate end of N-Acetylneuraminic acid of this protective glycoprotein forming
the terminal sugar that is exposed to the contents of both the gut and the arterial lumen (opening).
WGA's unique binding specificity to these exact two glycoproteins is not accidental. Nature has
perfectly designed WGA to attach to, disrupt, and gain entry through these mucosal surfaces.

It may strike some readers as highly suspect that wheat - the "staff of life" - which has garnered a reputation for "wholesome goodness" the world over, could contain a powerful health-disrupting anti-nutrient, which is only now coming to public attention. WGA has been overshadowed by the other proteins in wheat. Humans – not nature – have spent thousands of years cultivating and selecting for larger and larger quantities of these proteins. These pharmacologically active,
opiate-like proteins in gluten are known as gluten exorphins (A5, B4, B5, C) and gliadorphins. In the short term, they may effectively anesthetize us to the long-term, adverse effects of WGA. Gluten also contains exceptionally high levels of the excitotoxic l-aspartic and l-glutamic amino acids, which can also be highly addictive, not unlike their synthetic shadow molecules aspartame and monosodium glutamate. No doubt the narcotic properties of wheat is the primary reason why suspicions about its toxicity have remained merely speculative for thousands upon thousands of years.

WGA is most concentrated in the seed of the wheat plant, likely due to the fact that the seeds are the "babies" of these plants and are invested with the entire hope for continuance of their species. Protecting the seed against predation is necessarily a first priority. WGA is an exceedingly small glycoprotein (36 kilodaltons) and is concentrated deep within the embryo of the wheat berry (approximately 1 microgram per grain). WGA migrates during germination to the roots and tips of leaves, as the developing plant begins to project itself into the world and outside the safety of
its seed. In its quest for nourishment from the soil, its roots are challenged with fungi and bacteria that seek to invade the plant. In its quest for sunlight and other nourishment from the heavens, the plant’s leaves become prey to insects, birds, mammals, etc. Even after the plant has developed beyond the germination and sprouting stages, it retains almost 50% of the levels of lectin found in the dry seeds. Approximately one third of this WGA is in the roots and two thirds is in the shoot, for at least 34 days [3]

Each grain contains approximately one microgram of WGA. That seems hardly enough to do any harm to animals our size. Lectins, however, are notoriously dangerous even in minute doses and can be fatal when inhaled or injected directly into the bloodstream. According to the Centers for Disease Control and Prevention, it takes only 500 micrograms (about half a grain of sand) of
ricin (a lectin extracted from castor bean casings) to kill a human. A single, one ounce slice of wheat bread contains approximately 500 micrograms of WGA, which, if it were refined to its purest form and injected directly into the blood, could, in theory, have platelet-aggregating and erythrocyte-agglutinizing effects strong enough to create an obstructive clot such as that occuring in myocardial infarction and stroke. This, however, is not a likely route of exposure and, in reality, the immediate pathologies associated with lectins like ricin and WGA are largely restricted to the gastrointestinal tract where they can cause mucosal injuries. The point is that WGA, even in small quantities, could have profoundly adverse effects, given suitable conditions. Ironically, WGA is exceptionally small, at 36 kilodaltons (approximately the mass of 36,000 hydrogen atoms) and it can pass through the cell membranes of the intestine with ease. The intestines will allow passage of molecules up to 1,000 kilodaltons in size. Moreover, one wheat kernel contains 16.7 trillion individual molecules of WGA, with each molecule of WGA having four N-Acetylglucosamine binding sites. The disruptive and damaging effects of whole wheat bread consumption are formidable in someone whose protective mucosal barrier has been compromised by something as simple as nonsteroidal anti-inflammatory drug (NSAID) use, or a recent viral or bacterial infection. The common consumption of both wheat and NSAIDs may suggest the frequency of the WGA vicious cycle. Anti-inflammatory medications, such as ibuprofen and aspirin, increase intestinal permeabilty and may cause absorption of even larger- than-normal quantities of pro-inflammatory WGA. Conversely, the inflammation caused by the absorption of WGA lectin is the very reason there is a great need for the inflammation-reducing effects of NSAIDs.

One way to gauge just how pervasive the adverse effects of WGA are among wheat-consuming populations is the popularity of the dietary supplement glucosamine.In the USA, a quarter-billion dollars’ worth of glucosamine is sold annually.The main source of glucosamine on the market is from the N-Acetylglucosamine-rich chitin exoskelotons of crustaceans like shrimp and crab. Glucosamine is used for reducing pain and inflammation. We do not have a dietary deficiency of the pulverized shells of dead sea critters, just as our use of NSAIDs is not caused by a deficiency of these synthetic chemicals in our diet. When we consume glucosamine supplements, the WGA, instead of binding to our tissues, binds to the pulverized chitin in the glucosamine supplements, sparing us from the full impact of WGA. Many millions of Americans who have greatly reduced their pain and suffering by ingesting glucosamine and NSAIDs may be better served by
removing wheat, the underlying cause of their malaise, from their diets. This would result in
even greater relief from pain and inflammation along with far less dependency on both palliative
supplements and medicines.

To further underscore this point, the following are several ways that WGA depletes our health while glucosamine works against it:

WGA may be Pro-inflammatory

At exceedingly small (nanomolar) concentrations, WGA stimulates the synthesis of pro- inflammatory chemical messengers (cytokines) including Interleukin 1, Interleukin 6 and Interleukin 8 in intestinal and immune cells.[4] WGA has been shown to induce NADPH- Oxidase in human neutrophils associated with the "respiratory burst" that results in the release of inflammatory free radicals called reactive oxygen species[5] WGA has been shown to play a causative role in patients with chronic thin gut inflammation.[6]

WGA may be Immunotoxic

WGA induces thymus atrophy in rats[7] and may directly bind to, and activate, leukocytes [8]. Anti-WGA antibodies in human sera have been shown to cross-react with other proteins, indicating that they may contribute to autoimmunity [9]. Indeed, WGA appears to play a role in the pathogenesis of celiac disease (CD) that is entirely distinct from that of gluten, due to significantly higher levels of the immunoglobulins IgG and IgA antibodies against WGA found in patients with CD, when compared with patients with other intestinal disorders. These antibodies have also shown not to cross-react with gluten antigens[10] [11]

WGA May be Neurotoxic

WGA can pass through the blood brain barrier (BBB) through a process called "adsorptive endocytosis"[12] and is able to travel freely among the tissues of the brain which is why it is used as a marker for tracing neural circuits[13]. WGA’s ability to pass through the BBB, pulling bound substances with it, has piqued the interest of pharmaceutical developers who are looking to find ways of delivering drugs to the brain. WGA has a unique binding affinity for N- Acetylneuraminic acid, a crucial component of neuronal membranes found in the brain, such as gangliosides which have diverse roles such as cell-to-cell contact; ion conductance, as receptors, and whose dysfunction has been implicated in neurodegenerative disorders. WGA may attach to the protective coating on the nerves known as the myelin sheath[14] and is capable of inhibiting nerve growth factor [15] which is important for the growth, maintenance, and survival of certain target neurons. WGA binds to N-Acetylglucosamine which is believed to function as an atypical neurotransmitter functioning in nocioceptive (pain) pathways.

WGA May be Cytotoxic

WGA has been demonstrated to be cytotoxic to both normal and cancerous cell lines, capable of inducing either cell cycle arrest or programmed cell death (apoptosis).[16]

WGA May Interfere with Gene Expression

WGA demonstrates both mitogenic and anti-mitogenic[17] activities. WGA may prevent DNA replication[18] WGA binds to polysialic acid (involved in post-translational modifications) and blocks chick tail bud development in embryogenesis, indicating that it may influence both genetic and epigenetic factors.

WGA May Disrupt Endocrine Function

WGA has also been shown to have an insulin-mimetic action, potentially contributing to weight gain and insulin resistance [19]. WGA has been implicated in obesity and "leptin resistance" by blocking the receptor in the hypothalamus for the appetite satiating hormone leptin. WGA stimulates epidermal growth factor which, when upregulated, is associated with increased risk of cancer. WGA has a particular affinity for thyroid tissue and has been shown to bind to both benign and malignant thyroid nodules[20] WGA interferes with the production of secretin from the pancreas, which can inhibit with digestion and  cause pancreatic hypertrophy. WGA attaches to sperm and ovary cells, indicating it may adversely influence fertility.

WGA May be Cardiotoxic

WGA induces platelet activation and aggregration [21]. WGA has a potent, disruptive effect on platelet endothelial cell adhesion molecule-1, which plays a key role in tissue regeneration and safely removes neutrophils from our blood vessels.[22]

WGA May Adversely Effect Gastrointestinal Function

WGA causes increased shedding of the intestinal brush border membrane, reduction in surface area, acceleration of cell losses and shortening of villi, via binding to the surface of the villi.
WGA can mimic the effects of epidermal growth factor (EGF) at the cellular level, indicating that the crypt hyperplasia seen in celiac disease may be due to the growth-promoting effects of WGA. WGA causes cytoskeletal degradation in intestinal cells, contributing to cell death and increased turnover. WGA decreases levels of heat shock proteins in gut epithelial cells leaving these cells less well protected against the potentially harmful content of the gut lumen.[23]

WGA May Share Similarities with Certain Viruses

There are a number of interesting similarities between WGA lectin and viruses.  Both viral particles and WGA lectin are several orders of magnitude smaller than the cells they enter, and subsequent to their attachment to the cell membrane, are taken into the cell through a process of endocytosis. Both influenza and WGA gain entry through the sialic acid coatings of our mucous membranes (glycocalyx) each with a sialic acid-specific substance: the neuraminidase enzyme for viruses and the sialic acid binding sites on the WGA lectin.Once the influenza virus and WGA lectin have made their way into wider circulation in the host body, they are both capable of blurring the line in the host between self and non-self.  Influenza accomplishes this by incorporating itself into the genetic material of our cells and taking over the protein production machinery to replicate itself, with the result that our immune system must attack its own virally transformed cell, to clear the infection.  Studies done with herpes simplex virus have shown that WGA has the capacity to block viral infectivity through competitively binding to the same cell
surface receptors, indicating that they may effect cells through very similar pathways.  WGA has the capability of influencing the gene expression of certain cells, e.g. mitogenic/anti-mitogenic action, and like other lectins associated with autoimmunity, e.g. soy lectin, and viruses like Epstein-Barr virus, WGA may be capable of causing certain cells to exhibit class 2 human leukocyte antigens (HLA-II), which mark them for autoimmune destruction by white blood cells. Since human antibodies to WGA have been shown to cross-react with other proteins, even if WGA does not directly transform the phenotype of our cells into "other," the resulting cross- reactivity of antibodies to WGA with our own cells would nonetheless result in autoimmunity.

Given the multitude of ways in which WGA may disrupt our health, gain easy entry through our intestine into systemic circulation, and remain refractory to traditional antibody-based clinical diagnoses, it is altogether possible that the consumption of wheat is detracting from the general health of the wheat-consuming world and that we have been, for all these years, "digging our graves with our teeth." This perspective may come as a great surprise  to the health food industry whose particular love affair for whole wheat products has begun to go mass market. The increasingly hyped-up marketing of "whole wheat," "sprouted grain," and "wheat germ" enriched products, all of which may have considerably higher levels of WGA than their processed, fractionized, non-germinated and supposedly "less healthy" equivalents, may contribute to making us all significantly less healthy.

It is my belief that a careful study of the wheat plant will reveal that, despite claims to the contrary, man does not have dominion over nature. All that he deems fit for his consumption may not be his inborn right. Though the wheat plant’s apparently defenseless disposition would seem to make it suitable for mass human consumption, it has been imbued with a multitude of invisible "thorns," with WGA being its smallest and perhaps most potent defense against predation. While WGA may be an uninvited guest at our table, wheat is equally inhospitable to us. Perhaps the courteous thing to do, having realized our mistaken intrusion, is to lick our wounds and simply go our separate ways. Perhaps, as we separate from our infatuation with wheat, we will grow more sensitive to our bodies’ true needs and discover far more suitable forms of nourishment that nature has not impregnated with such high levels of addictive  and potentially debilitating proteins.




[1]       Desmond, S. T. Nicholl.  An Introduction to Genetic Engineering 3rd Ed.  Cambridge: Cambridge University Press, 1994-2008,, accessed October 2012.

[2]       Ji, Sayer. “The Dark Side of Wheat: New Perspectives on Celiac Disease & Wheat Intolerance.” Journal of Gluten Sensitivity. Santa Rosa:, 2008. wheat-intolerance-sayer-ji, accessed October 2012.

[3]       Mishkind, Michael, Kenneth Keegstra,  Barry A. Palevitz.  “Distribution of Wheat Germ Agglutinin in Young Wheat Plants.” Plant Physiology.  Rockville:  American Society of Plant Biologists, 1980., accessed December 2012.

[4]       Pellegrina, Chiara Dalla, Omar Perbellini, Maria Teresa Scupoli, Carlo Tomelleri, Chiara Zanetti, Gianni Zoccatelli, Marina Fusi, Angelo Peruffo, Corrado Rizzi, Roberto Chignola. “Effects of Wheat Germ Agglutinin on Human Gastrointestinal Epithelium: Insights From an Experimental Model of Immune/epithelial Cell Interaction.” Toxicology and Applied Pharmacology.  Amsterdam: Elsevier B.V..,
2009. gastrointestinal-epithelium-DDDhjGaQzd/1, accessed January 2013.

[5]       Karlsson, A. “Wheat Germ Agglutinin Induces NADPH-oxidase Activity in Human Neutrophils by Interaction with Mobilizable Receptors.”  Infection and Immunity. Washington, DC: The American Society for Microbiology, 1999., accessed December 2012.

[6]       Guzyeyeva, Gloria V.  “Lectin Glycosylation as a Marker of Thin Gut Inflammation”, The FASEB Journal, Bethesda: Federation of American Societies For Experimental Biology, 2008., accessed October 2012.

[7]       Pusztai, A., S.W.B. Ewen, G. Grant, D.S. Brown, J.C. Stewart, W.J. Peumans, E.J.M Van Damme, S. Bardocz.  “Antinutritive Effects of Wheat-germ Agglutinin and Other N-Acetylglucosamine-specific Lectins.” The British Journal of Nutrition. Cambridge: Cambridge University Press,  1993.
593001254a.pdf&code=ad7ed0ca7f0f2f23215d621ee092fd 38, accessed September

[8]       Tyrrell, Gregory J., Mark S. Peppler, Robert A. Bonnah, Clifford  G. Clark, Pele Chong, Glen D. Armstrong.  “Lectinlike Properties of Pertussis Toxin”. Infection and Immunity. Washington, D.C.: The American Society for Microbiology, 1989., accessed November 2012.

[9]       Tchernychev, B., M. Wilchek.  “Natural Human Antibodies to Dietary Lectins.” FEBS Letters.  Amsterdam:  Elsevier BV, 1996., accessed January 2013.

[10]     Sollid, L.M., J. Kolberg, H. Scott, J. Ek, O. Fausa, P. Brandtzaeg. “Antibodies to Wheat Germ Agglutinin in Coeliac Disease.” Clinical & Experimental Immunology Hoboken:  Wiley-Blackwell Publishing 1986., accessed November 2012.
[11]     Faith-Magnusson, K., KE. Magnussen.  “Elevated Levels of  Serum Antibodies to the Lectin Wheat Germ Agglutinin in Celiac Children  Lend Support to the Gluten- lectin Theory of Celiac Disease.”  Pediatrid Allergy & Immunology.  Hoboken:
Wiley-Blackwell Publishing. 1995., accessed September 2012.

[12]     Broadwell, R.D., B. J. Balin, M. Salcman.  “Transcytotic Pathway for Blood-borne Protein Through the Blood-brain Barrier.”  Proceedings of the National Academy of Sciences of the United States of America.  Washington, DC: National Academy of Sciences.  1988., accessed December 2012.

[13]     Damak, S., B. Mosinger, RF Margolskee.  “Transsynaptic Transport of Wheat Germ Agglutinin Expressed in a Subset of Type II Taste Cells of Transgenic Mice.” BMC Neuroscience.  London:  BioMed Central, Ltd. 2008., accessed December 2012.

[14]     Dolapchieva, S..  “Distribution of Concanavalin A and Wheat Germ Agglutinin Binding Sites in the Rat Peripheral Nerve Fibres Revealed by Lectin/glycoprotein- gold Histochemistry”.  The Histochemical Journal.  London:  Chapman & Hall,
1996., accessed January 2013).

[15]     Hashimoto, S., A. Hagino.  “Wheat germ agglutinin, concanavalin A, and lens culinalis agglutinin block the inhibitory effect of nerve growth factor on cell-free phosphorylation of Nsp100 in PC12h cells.”  Cell Structure and Function Journal. Kyoto:  Nihon Saibo Seibutsu Gakkai. 1989., accessed September 2012.

[16]     Liu, W.K., S.C. Sze, J.C. Ho, B.P. Liu, M.C. Yu.  “Wheat Germ Lectin Induces G2/M Arrest in Mouse L929 Fibroblasts.”  Journal of Cellular Biochemistry. Hoboken:  Wiley-Blackwell Publishing.  2004. es_G2/M_arrest_in_mouse_L929_fibroblasts, accessed November 2012.

[17]     Kaplowitz, Paul B. “Wheat germ agglutinin and concanavalin A inhibit the response of human fibroblasts to peptide growth factors by a post-receptor mechanism. Journal of Cellular Physiology.  Hoboken:  Wiley-Blackwell Publishing.  1985., accessed October
[18]     Cox, Lynne S.  “DNA Replication in Cell-free Extracts from Xenopus Eggs is Prevented by Disrupting Nuclear Envelope Function”.  Journal of Cell Science. Cambridge: The Company of Biologists. 1992,, accessed October 2012).

[19]     Yevdokimova, N.Y., A.S. Yefimov.  “Effects of Wheat Germ Agglutinin and Concanavalin A on the Accumulation of Glycosaminoglycans in Pericellular Matrix of Human Dermal Fibroblasts. A Comparison with Insulin”.  Acta Biochimica Polonica.    Warsaw:  The Polish Biochemical Society and the Committee of Chemistry and Biophysics. 2001., accessed November 2012.

[20]     Sasano, H., M. Rojas, S.G. Silverberg.  “Analysis of Lectin Binding in Benign and Malignant Thyroid Nodules.”  Pathology & Laboratory Medicine.  Northfield:  The College of American Pathologists.  1989.;jsessionid=KYN2j0u7h2Zg8CT6
OZ2D.2, accessed January 2013.

[21]     Lebret, M., F. Rendu.  “Further Characterization of Wheat Germ Agglutinin Interaction with Human Platelets: Exposure of Fibrinogen Receptors.”  Journal of Thrombosis and Haemostasis.  UK:  Blackwell Publishing. 1986., accessed September 2012.

[22]     Ohmori, T., Y. Yatomi, Y. Wu, M. Osada, K. Satoh, Y. Ozaki.  “Wheat Germ Agglutinin-induced Platelet Activation via Platelet Endothelial Cell Adhesion Molecule-1: Involvement of Rapid Phospholipase C Gamma 2 Activation by Src Family Kinases.”  Biochemistry.  New York:  Bedford, Freeman & Worth.  2001., accessed November 2012).

[23]     Ovelgonne, J.H., J.F.J.G. Koninkx, A. Pusztai, S. Bardocz, W. Kok, S.W.B. Ewen, H.G.C.J.M. Hendriks, J.E. van Dijk.  “Decreased Levels of Heat Shock Proteins in Gut Epithelial Cells After Exposure to Plant Lectins.”  Gut.   London:  BMJ Group.
2000., accessed September 2012).