Further Reading

Maize, Corn g202

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Code: f8
Latin name: Zea mays
Source material: Untreated planting seeds
Family: Poaceae (Gramineae)
Common names: Maize, Corn, Sweet Corn, Indian Corn, Field Corn
Cultivars within the genus may be divided into 6 general types: Popcorn (everta), Flint corn (indurata), Dent corn (indenta), Flour corn (amylacea), Sweet corn (saccharata) and Pod corn (tunicata).

There are, however, only 2 basic types: "Sweet corn" is distinguished from "Field corn" by the high sugar content of the kernels at the early "dough" stage and by wrinkled, translucent kernels when dry

Allergen Exposure

Geographical distribution
Maize kernels grow on long "ears" at the leaf axils of this unusual plant. The original habitat was probably South America or Mexico, where Maize was the staple diet of the American Indian. Maize is now grown almost anywhere summers are reasonably warm, although approximately 50% of the world's Maize is produced in the USA. It is a staple cereal of the human diet in Central and South America and in many parts of Africa. It is extremely important in livestock rearing, food processing and other commercial activities in developed countries. Few plants are grown more extensively or put to more diversified uses than Maize.

In the US and Europe, Maize is used almost entirely for animal feeding, as grain or fodder. But it is important as a vegetable, and as the snack popcorn. Kernels may be eaten straight from the cooked cob or cut off and used in succotash, custards, fritters, soups and chowders. Kernels are also used in mixed pickles and vegetable relishes. Corn meal, grits, and hominy are prepared forms of Maize kernels. Maize is also converted into various substances that have a wide range of usage, such as starch, syrup, dextrin, oil, and zein. Maize serves in the making of whiskey and other alcoholic products, and condensed milk. The roasted seed is a coffee substitute. Riboflavin and nicotinamide are added to fortified Maize.

The various parts of the plant have been used in the treatment of a variety of ailments.

Unexpected exposure

See under Environment.


Various allergens have been characterised:
  • Zea m 14, a 9 kDa lipid transfer protein  (1-9).
  • Zea m 25, a thioredoxin (1,8,10-11).
  • Zea m 27kD Zein, a 27 kDa protein, a glutenin (12-13).
  • Zea m 50kD Zein, a 50 kDa protein, a glutenin (12).

The following allergens have been characterised in Maize pollen: Zea m 1, Zea m 2, Zea m 3, Zea m 4, Zea m 5, Zea m 12, Zea m 13, Zea m CBP, and Zea m Zm13m. See Maize pollen g202.

Zea m 14, a lipid transfer protein, has also been isolated from Maize flour. Skin reactivity and IgE antibodies to this allergen were detected in 19 of 22 patients (86%) with systemic symptoms following the ingestion of Maize, confirming this as the Maize major allergen (1). Maize lipid transfer protein is highly heat-stable, and even heat treatment at 100°C for 160 minutes, though it almost totally eliminated the IgE-binding activity of the higher-molecular-weight bands seen in Maize, did not affect that of the lipid transfer protein (9).

Zea m 27kD Zein, a Maize zein, has been identified in an extensively hydrolyzed casein formula, Nutramigen. These proteins are water-insoluble and presumably originated from the Maize starch in Nutramigen. Although rabbits immunised with this formula developed antibodies against zeins but not against Cow's milk proteins, the clinical relevance of these proteins in Nutramigen remains to be established (13).

A 16 kDa allergen, recognised by 36% of Maize-allergic patients, was also isolated and shown to be the Maize inhibitor of trypsin (1).
A 22 kDa protein from Maize seed, with a 52% homology with the protein thaumatin and a 99% homology with the 22 kDa trypsin/alpha-amylase inhibitor, has been isolated (14). The allergenicity of this protein was not evaluated.

A 50 kDa allergen, belonging to the reduced soluble protein (RSP) fraction, has been isolated and shown to be stable to heat and digestion. In a study of 16 patients with specific IgE to Maize, only 6 patients were symptomatic. These 6 patients were DBPCFC-positive on challenges, and SPT with the purified RSP fraction was positive for all of the 6 DBPCFC-positive patients (15).

A protein similar to an isoflavone reductase (IFR) and/or an isoflavone reductase-like (IRL) protein has been isolated. (16) The allergenic potential of this protein was not determined.

In an individual with Maize dust-induced IgE-mediated occupational asthma and rhinitis, 10 IgE-binding components with sizes of 9 to 140 kDa were detected within the Maize dust extracts (17).

A chitinase has been isolated from Zea mays seeds (18). The allergenicity of this chitinase was not evaluated.

Maize seed contains the panallergen profilin, but at much lower levels than those found in Maize pollen (Zea m 12) and in foods such as Celery and Tomato (19).  This profilin may be of low clinical significance, as heat processing destroys the protein. Nonetheless, the presence of profilin in Maize seed may play a role in occupational asthma where inhalation of Maize flour or dust is possible.

Normal Maize contains about 7-13% protein, which can be fractionated into various solubility classes. The salt-extractable fraction (albumins and globulins) mainly comprises proteins with metabolic functions. Extraction with aqueous alcohol isolates the prolamin fraction that contains the storage proteins of the seed. These constitute around 60-70% of the Maize endosperm proteins and are called zeins. These are various polypeptides, classified as alpha, beta, delta and gamma zeins. The reduced soluble proteins are alcohol-extractable and soluble in water. Also present is an alcohol-insoluble glutelin fraction (15).

Potential cross-reactivity

An extensive cross-reactivity among the different individual species of the genus could be expected (20). In vitro cross-reactivity among the IgE binding proteins of Maize, Rice, Soybean and Peanut was demonstrated. The high degree of cross-reactivity between Rice and Maize was thought to be due to the fact that they both belong to the same botanical family. But the authors were not able to clarify the clinical significance of these cross-reactivities and suggested further clinical studies to put these findings into perspective (21). An earlier study reported that, by using RAST inhibition tests, cross-antigenicity could be demonstrated among different cereal grains, the degree of cross-reactivity closely paralleling their taxonomic relationship in the following order of decreasing closeness: Wheat, Triticale, Rye, Barley, Oat, Rice and Maize (22).

The major Maize allergen is a lipid transfer protein (7,23). A high degree of cross-reactivity has been demonstrated among the LTPs of Peach, Apple, Walnut, Hazel nut, Peanut, Maize, Rice, Sunflower seed, French bean and Apricot (1,24-26). Not all LTPs from plants are closely related. Mature Cherry LTP shows a great deal of identity with LTPs from Peach (88%) and Apricot (86%), but less with Maize (59%) (27). Similarly, Maize LTP was shown to cross-react completely with Rice and Peach LTP but not with Wheat or Barley LTP (1). Lipid transfer protein from Cowpea has a high homology of similarity to lipid transfer proteins of Maize (72%) (28). Rice non-specific lipid transfer protein has also been reported to closely resemble the structures of Wheat, Barley and Maize ns-LTPs (29).

A sensitisation rate of 47% among bakers with occupational asthma and of 35% among patients with grass pollen allergy, but without a clinical history of cereal allergy, was demonstrated to Tri a 25, a thioredoxin. Maize thioredoxin (Zea m 25) shares a 74% identity with Tri a 25, and exhibits distinct IgE cross-reactivity with its Wheat homologue. The study concluded that thioredoxins are cross-reactive allergens that might contribute to the symptoms of baker's asthma and might in addition be related to grass pollen allergy, and that therefore similar effects may be postulated for Zea m 25 (10). A more recent publication questioned whether this protein in Wheat is a true allergen, since it had been found that thioredoxin alleviates the allergic response and that there was no evidence that thioredoxin acted as an allergen (11).

A 16 kDa allergen, isolated and shown to be a Maize inhibitor of trypsin, was shown to cross-react completely with Grass, Wheat, Barley, and Rice trypsin inhibitors (1).

A Birch pollen protein with a mass of 35 kDa was isolated and shown to cross-react with 34 and 35 kDa proteins in Apple, Pear, Carrot, Banana and other exotic fruits. A high degree of sequence identity to isoflavone reductases (IFRs) and isoflavone reductase-like (IRL) proteins from several plants that also had a similar size was demonstrated, ranging from 56% for IFR from Pea and Chick pea and an IRL from Maize, to 80% for a Tobacco IRL. The authors postulated that this allergen may be responsible for less common pollen-related food allergies in patients allergic to Birch pollen (16).

The primary structure of the Japanese cypress (Chamaecyparis obtusa) allergen, Cha o 2, shows significant identity with the polygalacturonases of Avocado, Tomato, and Maize (30). The clinical implications of this finding have not been clarified yet.

In a study assessing the possible association of Oral allergy syndrome (OAS) with allergy to London plane tree (Platanus acerifolia), out of 720 patients evaluated, 61 (8.48%) were sensitised to P. acerifolia pollen. Food allergy was observed in 32 (52.45%) of the 61 patients, the allergens most frequently implicated being Hazel nut, Peach, Apple, Peanut, Maize, Chickpea and Lettuce. This study concluded that OAS in these patients may have been caused by primary respiratory sensitisation to Plane tree pollen. The authors suggest that profilin may be the responsible allergen (31).

Cross-allergenicity among 5 cereal grains, Rice, Wheat, Maize, Japanese millet (Echinochloa crus-galli) and Italian millet (Setaria italica), was examined by radioallergosorbent test and RAST inhibition assay. Significant close correlations between every combination of IgE antibody value for the 5 cereal grain extracts were found. A Rice protein of 16 kDa was shown to be one of the major allergens in Rice grain extracts (32).

Importantly, individuals with allergy to Maize pollen may also demonstrate allergy to Maize seed. In a group of 56 children with hay fever as a result of Maize pollen, more than half were sensitised to Maize seed allergens (33).

Clinical Experience

IgE-mediated reactions
Maize may moderately often sensitise or induce symptoms of food allergy in sensitised individuals (7,15,31,34-37). Allergic symptoms reported have included abdominal pain, nausea, vomiting, rhinitis, asthma, angioedema, atopic dermatitis, and anaphylaxis.

Latent sensitisation has often been described as a feature of Maize allergy. In 34 children with atopic dermatitis, 33 were SPT positive to Wheat and 18 to Oats. IgE antibodies to Wheat and Oats could be detected in 32 and 30 patients respectively. SPT to Rice, Maize, Millet or Buckwheat was positive in 16/34 patients (38-39). In 16 subjects with skin reactivity and the presence of IgE antibodies to Maize flour, only 6 complained of urticaria and/or other allergic symptoms following the ingestion of Maize-based foods. These patients developed symptoms following oral challenge with cooked Maize flour (polenta). The authors concluded that the presence of positive in vivo and in vitro tests to Maize flour had no clinical significance for most of the patients studied, and that food allergy to Maize has to be proven by DBPCFC studies. In these patients, a 50 kDa protein isolated was shown to be stable to cooking and digestion (15).

In a cross-sectional, descriptive, questionnaire-based survey conducted in Toulouse schools in France to determine the prevalence of food allergies among schoolchildren, of 192 questionnaires reporting a food allergy, of which 10 were excluded, the main foods reported as causing adverse reactions were Cow's milk (n=29), Egg (n=23), Kiwi (n=22), Peanut (n=20), Fish (n=19), Tree nuts (n=19), and Shrimp (n=13). Two individuals reported allergy to Maize (40).

Anaphylaxis to Maize protein has been reported (1,41). Anaphylaxis has even occurred during double-blind, placebo-controlled Maize challenges. (42) The Maize lipid transfer protein (Zea m 14) is reported to be responsible for this severe form of allergic reaction (5). Food-dependant exercise-induced anaphylaxis to Maize has also been described (43). In a study reporting on 7 cases of food-dependant exercise-induced anaphylaxis, responsible foods were Wheat (2 cases), Maize, Barley, Shrimp, Apple, Paprika and Mustard (44).

An unusual report was made of a 34-year-old carpenter who had previously been diagnosed with occupational asthma due to Rye flour added to wood boards. He developed severe anaphylaxis after testing a spoonful of baby cereal food – a non-Gluten, Rice and Corn formula. Skin reactivity and IgE antibodies were demonstrated for Wheat, Barley, Rye flour, Peanut and Mustard. A DBPCFC was positive for 0.1 g of the cereal. A 37 kDa protein band was demonstrated in the baby food, flours and Mustard. In addition, a well defined 23 kDa band was found in the Maize flour (45). The patient was specifically challenged with Maize alone.

Allergic reactions, including dermatitis, have been described with the Maize by-products Corn syrup, Corn dextrimaltose, Corn invert sugar, Corn isomerised dextrose and Corn D-psicose (46-48). Intravenous administration of a Maize-derived dextrose solution in a 23-year-old pregnant female patient at term gestation resulted in anaphylaxis. Symptoms included orofacial swelling, difficulty in breathing, hypotension, cardiac arrhythmia, voice hoarseness, total body warmth and flushing. These occurred within 8 minutes of initiation of a 5% dextrose Lactated Ringer's solution. Although the reaction elicited in this patient was unusual, clinicians should be aware of the possibility of Maize allergy due to the administration of IV fluids containing Maize-derived dextrose (49).

Patients allergic to Maize seed may also be allergic to Maize pollen, as Zea m 13 and homologous proteins are conserved plant allergens (4).

Occupational exposure to Maize, Maize flour, or Maize dust may result in occupational asthma or rhinitis, in particular in bakery workers, mill workers and those working in the animal feed industry (50). Whether atopy plays a dominant role or at most a minor role in the development of grain dust-induced airway disease has not been fully evaluated yet. Occupational asthma to grain dust resulting in bronchoconstriction induced by an IgE-mediated reaction has been reported (17). Antigen-specific IgE, IgG and IgG4 antibodies to Maize dust in exposed workers have also been described (51). In a group of 35 men working in an animal food processing plant, the most frequent positive skin prick reactions occurred to the following occupational allergens: Fish flour (82.9%), Carotene (77.1%), Maize (65.7%), four-leaf clover (62.9%), Sunflower (54.3%), Chicken meat (31.4%), Soy (28.6%), and Yeast (22.7%) (52).

In 42 employees working in the animal feed industry, 15/42 (34.9%) had work-related respiratory dysfunction with or without nasal symptoms (53). In 32 Swine farmers, 37% were reported to be allergic to Maize flour (54).

Allergic reactions have also been reported to cornstarch powder used as a glove lubricant. Symptoms included urticaria, intermittent episodes of dyspnoea, oculorhinitis, angioedema, and asthma (55). Anaphylaxis to cornstarch glove powder has been described in 2 nurses. Both exhibited skin reactivity to cornstarch powder in water, with resultant anaphylaxis in 1. Both had negative in vitro and in vivo tests to Maize. Analysis of the cornstarch powder revealed only glucose and inorganic salts. The authors tentatively suspected that cornstarch, and not residual Maize proteins, was the responsible allergen (56).

Similarly, a 33-year-old nurse presented with persistent hand dermatitis. The IgE antibody levels were moderately raised for Latex, Avocado and Banana. Despite avoidance of latex gloves, she failed to improve. Repeated investigation demon-strated no skin reactivity for Latex, but a strong reaction to Maize, which was the powder (cornstarch) being used on the gloves (57). Furthermore, if Corn oil is not purified it may contain Maize protein.


Other reactions
Maize has been implicated as one of the causative foods of eosinophilic esophagitis, a disorder with symptoms suggestive of gastroesophageal reflux disease but unresponsive to conventional reflux therapies (58).

Contact urticaria and an anaphylactoid reaction from cornstarch surgical glove powder have also been described (59-60).

The dust of stored Maize has been reported as a cause of respiratory symptoms. During the storage process, Maize dust can be contaminated by moulds and thermophilic actinomycetes, which have not been described until now as causative antigens of these symptoms. Mould as a contaminant of Maize seed should be considered as a possible cause of hypersensitivity reactions to Maize (61). A study described occupational hyper-sensitivity pneumonitis in an agricultural worker who planted and stored Maize. Clinical findings, precipitating antibodies, and his improvement after avoidance of his work environment confirmed the diagnosis. Aspergillus species contaminating the Maize dust were probably the antigens that caused the disease (62).

Compiled by Dr Harris Steinman,


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As in all diagnostic testing, the diagnosis is made by the physican based on both test results and the patient history.