Dietary management of autoimmune diabetes includes low glycemic foods classified from the glycemic index, but it does not consider the role that immunoreactive foods may play with the immunological etiology of the disease. We measured the reactivity of either monoclonal or polyclonal affinity-purified antibodies to insulin, insulin receptor alpha, insulin receptor beta, zinc transporter 8 (ZnT8), tyrosine phosphatase-based islet antigen 2 (IA2), and glutamic acid decarboxylase (GAD) 65 and 67 against 204 dietary proteins that are commonly consumed. Dietary protein determinants included unmodified (raw) and modified (cooked and roasted) foods, herbs, spices, food gums, brewed beverages, and additives. There was no immune reactivity between insulin or insulin receptor beta and dietary proteins. However, we identified strong to moderate immunological reactivity with antibodies against insulin receptor alpha, ZnT8, IA2, GAD-65, and GAD-67 with several dietary proteins. We also identified 49 dietary proteins found in foods classified as low glycemic foods with immune reactivity to autoimmune target sites. Laboratory analysis of immunological cross-reactivity between pancreas target sites and dietary proteins is the initial step necessary in determining whether dietary proteins may play a potential immunoreactive role in autoimmune diabetes.
Diabetes mellitus, commonly called diabetes, is a group of metabolic diseases in which the body experiences unusually high blood sugar levels over an extended period of time. Diabetes is a leading cause of death and disability in the United States and affects more than 9.3% of the population [ Type 1 diabetes (T1D) is a result of the pancreas’ failure to produce sufficient insulin. The pancreas is a glandular organ that not only secretes digestive enzymes but also produces important hormones. These hormones are produced inside the pancreas by clumps of cells called islet cells. Of the five kinds of islet cells, alpha, beta, delta, gamma (PP), and epsilon, only beta islet cells produce the hormone insulin, which regulates blood sugar levels. In an autoimmune condition, the body’s own immune system can mistakenly attack and damage or destroy beta islet cells, leading to a reduction of the insulin needed to regulate the body’s blood sugar levels [ Type 2 diabetes is a condition in which the cells of the body fail to respond to insulin properly, usually caused by excessive body weight and lack of exercise. Lack of insulin may also develop as the disease progresses [ Gestational diabetes occurs when pregnant women without a previous history of diabetes develop high blood sugar levels [ Other specific types are a collection of a few dozen different causes [
Many new cases of diabetes are due to an overlooked autoimmune etiology called latent autoimmune diabetes of adulthood (LADA), which is often misdiagnosed as type 2 diabetes [
LADA and juvenile type 1 diabetes are characterized by autoimmune destruction hyperglycemia. The pathogenic model in which antigens initiate and drive the process is currently under investigation [
Dietary protein cross-reactivity research has received limited attention in type 1 diabetes. Current research has mostly been limited to gluten and milk proteins as potential sources of pancreatic islet cell destruction. Cow’s milk albumin has also been suggested in the etiology of type 1 diabetes due to milk peptide antibody (bovine serum albumin antibodies) binding to beta-cell-specific surface protein and promoting islet cell destruction [
It is possible that other food proteins play a role in pancreatic cell cross-reactivity leading to islet cell destruction. In this study, we evaluated the potential for dietary protein cross-reactivity with insulin and pancreatic target sites by evaluating immune reactivity between target-specific antibodies and purified dietary proteins shown in Table
Dietary proteins screened for immune reaction.
|
Flax seed | Seaweed | Imitation crab |
Alpha-casein & beta-casein | Hazelnut, raw + roasted | Spinach + Aquaporin | Clam, boiled |
Cow’s milk | Macadamia nut, raw + roasted | Tomato + Aquaporin | Oyster, boiled |
Chocolate milk | Mustard seed | Tomato paste | Scallops, seared |
Egg white, boiled | Pecan, raw + roasted | Yam + Sweet potato, baked | Squid (Calamari), seared |
Egg yolk, boiled | Peanut, roasted | Zucchini, boiled | Shrimp, seared |
Goat’s milk | Peanut butter |
|
Shrimp tropomyosin |
Milk butyrophilin | Peanut agglutinin | Apple | Parvalbumin |
Soft cheese + Hard cheese | Peanut oleosin | Apple cider |
|
Whey protein | Pistachio, raw + roasted | Apricot | Beef, boiled medium |
Yogurt | Pumpkin seeds, roasted | Avocado | Chicken, boiled |
|
Sesame albumin | Banana | Lamb, baked |
Amaranth | Sesame oleosin | Banana, boiled | Pork, baked |
Buckwheat | Sunflower seeds, roasted | Latex hevein | Turkey, baked |
Casomorphin | Walnut | Blueberry | Gelatin |
Oats |
|
Cantaloupe + Honeydew melon | Meat glue |
Quinoa | Artichoke, boiled | Cherry |
|
Rice | Asparagus | Coconut, meat + milk | Basil |
Rice, white + brown, boiled | Asparagus, boiled | Cranberry | Cilantro |
Rice cake | Beet, boiled | Date | Cumin |
Rice protein | Bell pepper | Fig | Dill |
Rice endochitinase | Broccoli | Grape, red + green | Ginger |
Rye, barley, spelt, polish wheat | Broccoli, boiled | Red wine | Oregano |
Sesame | Brussels Sprouts, boiled | White wine | Parsley |
Sorghum | Cabbage, red + green | Grapefruit | Rosemary |
Tapioca | Cabbage, boiled | Kiwi | Thyme |
Teff | Canola oleosin | Lemon + Lime |
|
Wild rice, boiled | Carrot | Mango | Cinnamon |
Wheat + Alpha-gliadins | Carrot, boiled | Orange | Clove |
Yeast miller | Cauliflower, boiled | Orange juice | Mint |
Hemp | Celery | Papaya | Nutmeg |
|
Chili pepper | Peach + Nectarine | Paprika |
Black bean, boiled | Corn + Aquaporin, boiled | Pear | Turmeric (Curcumin) |
Bean agglutinins | Popped corn | Pineapple | Vanilla |
Dark chocolate + Cocoa | Corn oleosin | Pineapple bromelain |
|
Fava bean, boiled | Cucumber, pickled | Plum | Carrageenan |
Garbanzo bean, boiled | Eggplant, boiled | Pomegranate | Gum guar |
Kidney bean, boiled | Garlic | Strawberry | Gum tragacanth |
Lentil, boiled | Garlic, boiled | Watermelon | Locust bean gum |
Lentil lectin | Green Bean, boiled |
|
Mastic gum + Gum arabic |
Lima bean, boiled | Lettuce | Cod, baked | Xanthan gum |
Pinto bean, boiled | Mushroom, raw + boiled | Halibut, baked |
|
Soybean agglutinin | Okra, boiled | Mackerel, baked | Coffee bean protein, brewed |
Soybean oleosin + Aquaporin | Olive, green + black, pickled | Red Snapper, baked | Instant coffee |
Soy Sauce, gluten-free | Onion + Scallion | Salmon | Black tea, brewed |
Tofu | Onion + Scallion, boiled | Salmon, baked | Green tea, brewed |
|
Pea, boiled | Sardine + Anchovy, cooked | Honey, raw + processed |
Almond | Pea protein | Sea bass, seared | Beta-glucan |
Almond, roasted | Pea lectin | Tilapia, baked | Food coloring |
Brazil nut, raw + roasted | Potato, white, baked | Trout, baked | |
Cashew | Potato, white, fried | Tuna | |
Cashew, roasted | Pumpkin + Squash, boiled | Tuna, seared | |
Cashew vicilin | Radish | Whitefish, baked | |
Chia seed | Safflower + Sunflower oleosin | Crab + Lobster, boiled |
The determination of food proteins that cross-react with islet cell antigens may identify dietary proteins that are potential triggers for a subset of individuals with autoimmune diabetes.
Mouse monoclonal anti-insulin antibodies, affinity-purified rabbit polyclonal insulin receptor alpha (IR-A) antibodies, mouse monoclonal insulin receptor beta (IR-B) antibodies, affinity-purified rabbit polyclonal GAD-65 antibodies, and affinity-purified rabbit polyclonal GAD-67 antibodies were purchased from Abcam (Cambridge, MA, USA). Mouse monoclonal ZnT8 antibodies were purchased from Santa Cruz Biotechnology, Inc. (Dallas, TX, USA), and mouse monoclonal IA2 antibodies were purchased from ThermoFisher Scientific (Rockford, IL, USA).
Food antigens were prepared from products purchased from the supermarket in either raw, roasted, or cooked form. Cooked food proteins have different structural epitopes, and dietary protein preparation was conducted to reflect dietary proteins in either cooked or raw form as represented in typical human diets. For that preparation, 10 g of food product was put in a food processor using 0.1 M of phosphate buffer saline (PBS) at pH 7.4. The mixer was turned on and off for 1 hour and then kept on the stirrer overnight at 4°C. The food processor was decontaminated after each food product. After centrifugation at 20,000
To purify the oleosin from peanuts, corn, safflower, sunflower, and soybean, the foods were prepared according to the method described above. A total of 100 mL of chloroform/methanol (2/1,
Mastic gum, carrageenan, xanthan gum, guar gum, gum tragacanth, locust bean gum, and
Antigens and peptides were dissolved in PBS or methanol at a concentration of 1.0 mg/mL, then diluted 1 : 100 in 0.1 M carbonate-bicarbonate buffer (pH of 9.5). One hundred microliters was added to each well of the polystyrene flat-bottom ELISA plate. Plates were incubated overnight at 4 degrees Celsius and then washed three times with 200
Plates were washed, and then enzyme-labeled anti-mouse or anti-rabbit IgG antibodies were added to each well; plates were incubated for an additional 1 hour at room temperature. They were then washed five times with TBS-Tween buffer. The enzyme reaction was started by adding 100
Two hundred and four proteins were tested for seven target tissue antibodies in duplicate, leading to 2856 antigen-antibody OD measurements. The results of each duplicate OD were averaged together for one OD value. Of the 2856 OD measurements, the mean OD measurement was 0.25 with a standard deviation (SD) of 0.14. The OD of 0.53 represented two SD from the mean, the OD of 0.67 represented three SD from the mean, and an OD of 0.81 represented four SD from the mean. OD values below two SD or less than 0.52 were labeled nonsignificant. OD values above two SD but below three SD at OD values of 0.53–0.66 were categorized as 1+ reaction. OD values above three SD but less than four SD at OD values of 0.67–0.90 were categorized as 2+ reactions. OD values of 0.91–1.50 were categorized as 3+ reactions. OD values of 1.51–2.0 were categorized as 4+ reactions, and OD values >2.0 were categorized as 5+ reactions. The ODs of control wells coated only with BSA to which all other reagents were added were less than 0.15.
Our investigation found no specific immune reactivity with anti-insulin antibody and any of the 204 food antigens.
Our investigation identified eight dietary proteins that exhibited immune reactivity with specific IR-A antibody: milk butyrophilin (5+), potato (3+), amaranth (3+), quinoa (2+), tapioca (2+), buckwheat (1+), hemp (1+), and kamut (1+) (see Figure
Reaction of polyclonal IR-A, GAD-65, and GAD-67 antibodies with different dietary proteins.
Our investigation identified 9 dietary proteins that directly exhibited immune reactivity with specific targeted GAD-65 polyclonal antibody: of these, buckwheat (3+) was the most reactive, followed by amaranth (3+), rice (3+), corn (3+), and yeast (3+), potato (2+), quinoa (2+), and oats (2+), then tapioca (1+) (see Figure
Our investigation found 27 dietary proteins that exhibited immune reactivity with specific target IA2 monoclonal antibody. Of these immune reactive proteins, seaweed (5+), guar gum (5+), and apricot (5+) were the most reactive, followed by pea lectin (3+), spinach (3+), cooked white and brown rice (3+), cooked garlic (3+), zucchini (3+), and mackerel (3+), egg yolk (2+), garbanzo bean (2+), carrageenan (2+), soy bean agglutinin (2+), bell pepper (2+), and mint (2+), then cooked lima bean (1+), gluten-free soy sauce (1+), tofu (1+), and mustard seed (1+). Rice apple, melon, watermelon, clam, cooked cod, cooked halibut, and cilantro had reactions that were insignificant (see Figure
Reaction of monoclonal IA2 antibodies with different dietary proteins. The antigens in blue also reacted with ZnT8 antibodies.
The ZnT8 antibody reacted with 30 dietary proteins. The most reactive were seaweed (5+), cooked lentil (5+), and pea protein (5+), followed by guar gum (4+), wheat (4+), peanut oleosin (4+), and cooked pea (4+), garbanzo bean (3+), soy bean oleosin (3+), roasted peanut (3+), and cooked tilapia (3+), egg yolk (2+), cooked lima bean (2+), mustard seed (2+), clam (2+), goat’s milk (2+), roasted almond (2+), cashew vicilin (2+), tomato (2+), cooked yam and sweet potato (2+), banana (2+), and kiwi (2+), then gluten-free soy sauce (1+), tofu (1+), pea lectin (1+), spinach (1+), carrageenan (1+), macadamia nut (1+), cherry (1+), and salmon (1+) (see Figure
Reaction of monoclonal ZnT8 antibodies with different dietary proteins. The antigens in blue also reacted with IA2 antibodies.
In addition, 10 dietary proteins that directly exhibited immune reactivity with specific targeted GAD-67 polyclonal antibody: buckwheat (4+) was the most reactive, followed by cow’s milk (3+); milk chocolate (3+) were the most reactive, followed by raw and roasted pecan (2+), alpha and beta casein (2+), and rice cake (2+), then coconut (1+), cranberry (1+), orange juice 1+), and roasted hazelnut (1+) (see Figure
There is some evidence showing that pancreatic beta islet cell antibodies in children are predictive for determining progression to diabetes using proportional hazards analysis [
The focus of our laboratory research was to identify food proteins that have the potential to cross-react with pancreatic islet cells by evaluating immune reactivity between antibodies made against target tissue antigens involved in diabetes and various dietary proteins. The foods found to be immune reactive to pancreas target sites included the main food groups of gluten proteins, nongluten grains, and dairy proteins. Food groups tend to have homologous amino acid sequences. Reactivity to one food may also lead to immune reactivity with other dietary proteins in that food group. For example, several papers demonstrate that an isolated allergy to a single fish species leads to immune reactivity to other fish species due to amino acid structural similarity [
In this current study, we examined possible cross-reactivity between islet cell antigens and different food proteins by measuring the reactivity of highly specific antibodies made against islet cell antigens with a variety of food antigens.
With IR-A, the strongest reaction was with milk butyrophilin, while with GAD-65, the strongest reactions were with buckwheat, amaranth, rice, corn, and yeast. With GAD-67, the strongest reactions were with buckwheat, cow’s milk, and milk chocolate (see Figure
With IA2 antibody, the strongest reactions were with seaweed, guar gum, and apricot, then pea lectin, spinach, cooked white, and brown rice, cooked garlic, zucchini, and mackerel (see Figure
With ZnT8 antibody, the strongest reactions were with seaweed, cooked lentil, and pea protein, followed by guar gum, wheat, peanut oleosin, and cooked pea, then garbanzo bean, soy bean oleosin, roasted peanut, and cooked tilapia (see Figure
Overall, we found that IA2 antibody reacted with 27 food proteins, ZnT8 antibody reacted with 30 food proteins, and GAD-65 reacted with 9 food proteins. Out of these foods, the same 12 foods reacted with both IA2 and ZnT8 antibodies. These 12 foods were egg yolk, garbanzo bean, cooked lima bean, gluten-free soy sauce, tofu, mustard seed, pea lectin, seaweed, spinach, clam, carrageenan, and guar gum. The detection of these dietary proteins cross-reactive with these major islet cell antigens, IA2, ZnT8, and GAD-65, especially the 12 foods that are dually reactive to both IA2 and ZnT8, warrants further investigation, because on the occasion of oral tolerance failure, if these foods manage to penetrate the epithelial barriers, the production of cross-reactive antibodies may contribute towards the destruction of islet cells.
Both IA2 and ZnT8 were also shown to be reactive to pea lectin (3+ and 1+, resp.). Lectins stimulate class II human leukocyte antigens (HLAs) of islet cells, which normally do not display them. Islet cells carry a very specific disaccharide determinant called N-acetyllactosamine, to which wheat, peanuts, soy, potato, and tomato lectins love to bind. This binding can result in islet cells expressing the class II HLAs and foreign antigens together, making the individual susceptible to autoimmune attack.
The ZnT8 antibody reacted not only with roasted peanut (3+) but also with peanut oleosin (4+) and soy bean oleosin (3+). Oleosins are relatively small (15 to 25 kDa) oil proteins that provide energy for plant seed cells. To a sensitive person, the ingestion of even a small amount can provoke severe reactions. Refined vegetable oils are used in a wide variety of food products, but oils from plants such as peanuts and soybeans have been recognized as potent antigens and allergens [
Both IA2 and ZnT8 reacted very strongly to guar gum (5+ and 4+, resp.). Both also reacted to a lesser extent to carrageenan (2+ and 1+, resp.). Like oil, gums have an extremely broad range of commercial and industrial use, in not just food but including pharmaceuticals, printing, and other applications. Even though gums are generally recognized as safe by the FDA, gums do have a history of association with sensitivities or allergic reactions [
Aquaporin 4 (AQP4) is a class of water channels found in many cells of the body including the stomach, brain, lung, and skeletal muscle. Aquaporin is also found in many plants, and a recent study showed a significant similarity between the amino acid sequences of soy, spinach, corn, tomato, and tobacco with human aquaporin epitope 207–232 to elicit concerns about cross-reactivity. IA2 and ZnT8 had reactions in varying degrees with spinach, tomato, and different soy antigens (see Figure
Wheat has long been confirmed to be associated with a broad spectrum of autoimmune disorders, including T1D [
The role of milk proteins and their involvement with autoimmune diabetes due to mimicry epitopes has previously been reported from epidemiological studies and from animal models that found that milk proteins play a diabetogenic role [
Although many researchers have previously investigated the potential role of gluten and autoimmune diabetes, our largest immune reactive category was to nongluten grains, which has been less studied. These foods accounted for 4.4% of the screened dietary proteins and included rice, quinoa, hemp, yeast, oats, buckwheat, amaranth, and tapioca. This nongluten grain category was highly reactive to GAD-65 and insulin receptor alpha (see Figure
Reactivity of antibodies against pancreatic islet cell antigens with food proteins.
Food protein | Reactivity |
---|---|
|
|
Wheat | ZnT8 (4+) |
Kamut | IR-A (1+) |
|
|
|
|
Buckwheat | GAD-65 (4+), GAD-67 (3+), IR-A (1+) |
Amaranth | GAD-65 (3+), IR-A (3+) |
Quinoa | GAD-65 (2+), IR-A (2+) |
Tapioca | IR-A (2+), GAD-65 (1+) |
Oats | GAD-65 (2+) |
Rice/rice cake | GAD-65 (3+), IA2 (3+), GAD-67 (2+) |
Hemp | IR-A (1+) |
Corn | GAD-65 (3+) |
|
|
|
|
Lentil | ZnT8 (5+) |
Pea protein | ZnT8 (5+) |
Pea cooked | ZnT8 (4+) |
Pea lectin | IA2 (3+) |
Garbanzo bean | ZnT8 (3+), IA2 (2+) |
Lima bean | ZnT8 (2+), IA2 (1+) |
Soy sauce gluten free | ZnT8 (1+), IA2 (1+) |
Tofu | ZnT8 (1+), IA2 (1+) |
Soy bean agglutinin | IA2 (2+) |
Soy bean oleosin | ZnT8 (3+) |
|
|
|
|
Clam | ZnT8 (2+) |
Mackerel | IA2 (3+) |
Salmon | ZnT8 (1+) |
Tilapia | ZnT8 (3+) |
|
|
|
|
Seaweed | ZnT8 (5+), IA2 (5+) |
Egg yolk | ZnT8 (2+), IA2 (2+) |
Yeast | GAD-65 (3+) |
Mustard seed | ZnT8 (3+), IA2 (1+) |
|
|
|
|
Goat’s milk | ZnT8 (2+) |
Cow’s milk | GAD-67 (3+) |
Milk chocolate | GAD-67 (3+) |
Milk butyrophilin | IR-A (5+) |
|
GAD-67 (2+) |
|
|
|
|
Hazelnut | GAD-67 (1+) |
Pecan | GAD-67 (2+) |
Almond roasted | ZnT8 (2+) |
Cashew vicilin | ZnT8 (2+) |
Macadamia | ZnT8 (1+) |
Peanut roasted | ZnT8 (3+) |
Peanut oleosin | ZnT8 (4+) |
|
|
|
|
Guar gum | IA2 (5+), ZnT8 (4+) |
Carrageenan | IA2 (2+), ZnT8 (1+) |
|
|
|
|
Apricot | IA2 (5+) |
Banana | ZnT8 (2+) |
Cherry | ZnT8 (1+) |
Kiwi | ZnT8 (2+) |
Coconut | GAD-67 (1+) |
Cranberry | GAD-67 (1+) |
Orange juice | GAD-67 (1+) |
|
|
|
|
Bell pepper | IA2 (2+) |
Garlic Ck | IA2 (2+) |
Tomato | ZnT8 (2+) |
Potato | IR-A (3+), GAD-65 (2+) |
Yam + Sw Potato | ZnT8 (2+) |
Zucchini | IA2 (3+) |
|
|
|
|
Dill | IA2 (1+) |
Mint | IA2 (2+) |
The second largest reactive food category we identified was bean proteins. Beans (including black, white, navy, lima, pinto, garbanzo, soy, and kidney) are a winning combination of high-quality carbohydrates, lean protein, and soluble fiber that helps stabilize your body’s blood-sugar levels and keeps hunger in check. Unfortunately, although they are generally considered a low glycemic index food, in our study, the islet cell antigens reacted with garbanzo bean, lima bean, gluten-free soy sauce, soy bean oleosin, soy bean agglutinin, tofu, pea lectin, pea protein, cooked pea, and cooked lentil.
Our investigation identified 49 dietary proteins (24% of the 204 proteins) that are classified as low glycemic foods (glycemic index <55) to be reactive to antibodies made against pancreatic autoimmune target sites (see Table
Low glycemic index foods reactive with pancreatic islet cell antibodies.
Milk butyrophilin | Nuts | Corn |
Cow’s milk | Oats | Coconut |
|
Quinoa | Cranberry |
Goat’s milk | Rice | Hazelnut |
Milk chocolate | Hemp | Pecan |
Guar gum | Seaweed | Vegetables |
Carrageenan | Beans & Legumes | Seafood |
Glycemic index <55.
We must not forget that immune or sensitive reactions to food can also depend on whether the food is raw or cooked. A food in its natural state can be vastly different from the same food that has been cooked, processed, or modified. The food can react with sugar, lipids can be oxidized, peptide chains can be broken, and neoantigens can be formed. Thus, an individual that can eat a raw food safely may be highly reactive to the same food if cooked, or vice versa. It is not surprising then that in our tests, IA2 reacted strongly with cooked garlic (3+) but less with raw garlic (insignificant), strongly with pea lectin (4+) but not as much with pea protein (insignificant), and moderately with apple (2+) but less with apple cider (1+). In a similar fashion, ZnT8 reacted moderately with raw banana (2+) but less with cooked banana (insignificant), stronger against raw salmon (3+) but not as much with cooked salmon (1+), and very strongly with pea protein (5+) but less with pea lectin (3+).
It is important to note that cross-reactivity alone is not likely to initiate the pathogenesis of autoimmunity. However, the potential exists to upregulate subclinical or preexisting autoimmune conditions, and we suggest that immune reactivity is likely to promote the autoreactive process in susceptible subgroups if exposed to the specific antigens [
These underlying mechanisms that may coexist with autoimmune diabetes and, in combination with immune reactive foods that share amino acid sequence homology, may lead to dietary proteins that can be diabetogenic in a subset of individuals. Further research to investigate the pathogenic role of these dietary proteins is necessary but must include confounding variables such as humoral and cellular immunity factors, intestinal permeability, mucosal regulatory mechanisms, and other factors that can determine whether exposure to dietary proteins is antigenic or immunologically benign; protein sequence similarity alone would not account for a pathogenic role. It is unlikely that the consumption of these dietary proteins alone would be diabetogenic in nonsusceptible populations. However, the immunoreactive dietary proteins we identified may act as cross-reactive food antigens for subsets of individuals who produce these antibodies due to loss of immunological tolerance.
The results of our study identified immune reactivity between antibodies to insulin, insulin receptors, islet cell antigens, and food antigens. Potential tissue antibody binding with various food antigens or food antibody binding to specific pancreatic sites can lead to the possibilities that some dietary proteins may play an antigenic role with autoimmune diabetes.
Even though many of the individual proteins in these groups may be considered safe or of low glycemic index, the consumption of these foods by a sensitive or predisposed individual may trigger immune reactions or autoimmunities.
Further research should be conducted to evaluate the specific epitope for each of the dietary proteins that react with these tissue-specific antibodies. It is necessary to determine the exact amino acid sequence homology, the immunological factors that convert dietary proteins from benign to pathogenic, and the clinical role that these dietary proteins play in autoimmune diabetes. However, the results of our research provide a first step in narrowing down a list of specific dietary proteins that, due to cross-reactivity, may potentially have an impact on autoimmune diabetes.
Dr. Aristo Vojdani is CEO of Immunosciences Lab, Inc. Dr. Datis Kharrazian and Dr. Martha Herbert have nothing to disclose.
The authors do not have any conflicts of interest.