• -Almond, Apple, Apricot, Asparagus, Avocado, Bakers Yeast, Banana, Barley, Beef, Beet, Blueberry, Brewer's Yeast, Broccoli, Buckwheat, Succinic, Cabbage, Candida albicans,Cane Sugar, Carrot, Cashews, Casein, Celery, Cheese, Chicken, Cocoa, Coconut, Cod Fish, Coffee, Corn, Crab, Cranberry, Eggplant, Egg White, Egg Yolk, Flax, Garbanzo Beans, Garlic, Gliadin, Goats Milk Cheese, Grape, Grapefruit, Green Beans, Green Pepper, Halibut, Hazelnut, Honey, Kidney Beans, Lamb, Lemon, Lentil, Lettuce, Lima Beans, Lobster, Milk, Millet, Orotic, Oat, Onion, Orange, Papaya, Pea's, Peach, Peanut, Pear, Pecan, Pineapple, Pinto Beans, Pistachio, Plum(Prune), Pork, Potato, Pumpkin, Radish, Rice, Rye, Salmon, Sardine, Sesame, Shrimp, Sorghum, Soybean, Spinach, Strawberry, Sunflower, Sweet Potato, Tomato, Tuna, Turkey, Wheat Gluten, Walnut, Watermelon, Wheat, Whey, and Yogurt.

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Immunoglobulin G (IgG) is classified into several subclasses termed 1, 2, 3, and 4. IgGs are composed of two heavy chain–light chain pairs (half-molecules), which are connected via inter–heavy chain disulfide bonds situated in the hinge region (Figure 1). IgG4 antibodies usually represent less than 6% of the total IgG antibodies. IgG4 antibodies differ functionally from other IgG subclasses in their lack of inflammatory activity, which includes a poor ability to induce complement and immune cell activation because of low affinity for C1q (the q fragment of the first component of complement). Consequently, IgG4 has become the preferred subclass for immunotherapy, in which IgG4 antibodies to antigens are increased to reduce severe antigen reactions mediated by IgE. If antigens preferentially react with IgG4 antibodies, the antigens cannot react with IgE antibodies that might cause anaphylaxis or other severe reactions. Thus, IgG4 antibodies are often termed blocking antibodies. Another property of blood-derived IgG4 is its inability to cross-link identical antigens, which is referred to as "functional monovalency". IgG4 antibodies are dynamic molecules that exchange half of the antibody molecule specific for one antigen with a heavy-light chain pair from another molecule specific for a different antigen, resulting in bi-specific antibodies that are unable to form large cross-linked antibodies that bind complement and thus cause subsequent inflammation(16). In specific immunotherapy with allergen in allergic rhinitis, for example, increases in allergen-specific IgG4 levels indeed correlate with improved clinical responses. IgG4 antibodies not only block IgE mediated food allergies but also block the reactions of food antigens with other IgG subclasses, reducing inflammatory reactions caused by the other IgG subclasses of antibodies to food antigens.

In IgG mediated food allergy testing, the goal is to identify foods that are capable of causing inflammation that can trigger a large number of adverse reactions. IgG1, IgG2, and IgG3 all are capable of causing inflammation because these antibodies do not exchange heavy and light chains with other antibodies to form bispecific antibodies. Thus, IgG1, IgG2, and IgG3 antibodies to food antigens can and do form large immune complexes or lattices that fix complement and increase inflammation. The presence of IgG4 antibodies to food antigens indicates the presence of antibodies to foods that will not usually cause inflammation even though high amounts of these antibodies do indicate the presence of immune reactions against food antigens. Testing only for IgG4 antibodies in foods limits the ability of the clinician to determine those foods that are causing significant clinical reactions that are affecting their patients. The importance of measuring other subtypes of IgG antibodies is highlighted in an article by Kemeny et al. (17). They found that IgG1 antibodies to gluten were elevated in all 20 patients with celiac disease but none of the patients had elevated IgG4 antibodies to gluten.


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