Allergen Description
Immunoblot analysis has demonstrated that 70, 64, 35, and 26 kDa proteins are major allergens (1-2). Other studies have detected multiple allergens in both raw and boiled Chick pea extracts in the molecular weight range of 10-106 kDa, of which the majority were heat-stable (3-4).
The following allergens have been characterised:
- Cic a 2S Albumin, a 10-12 kDa protein (5).
- Cic a IFR, an Isoflavone Reductase (6).
The presence of an allergen belonging to the profilin family has been suggested by a study examining the possible association of oral allergy syndrome with Plane tree pollen (Platanus acerifolia) (7). This has been questioned by another study (8).
A beta-1,3-glucanase and two chitinases have been isolated from Chick pea. One of the chitinases, a 32 kDa protein, was shown to be a class I chitinase, and the second, a 28 kDa protein, showed homology to class III chitinases (9). The allergenic significance of these proteins has not yet been determined.
Infection of the Chick pea plant was shown to initiate the formation of a thaumatin-like protein in Chick pea leaves (10). Whether this protein occurs in the seed of the plant or whether it has allergenic potential has not been determined yet. Also, a trypsin and chymotrypsin inhibitor has been isolated in Chick pea (11). The clinical significance of this has not yet been determined.
Potential Cross Reactivity
An extensive cross-reactivity among the different individual species of the Fabaceae (legume family) could be expected but in fact does not occur frequently (12). In an early study, an in vitro study, the specific IgE binding by protein extracts of 11 food legumes was examined by IgE antibody determination and RAST inhibition. Cross-allergenicity was demonstrated to be most marked between the extracts of Peanut, Garden pea, Chick pea, and Soybean (13.) Legumes have a high degree of immunological cross-reactivity, at least in in vitro studies. The allergenicity of legumes is mainly is mainly related to allergens from the storage proteins of seeds. Vicilins from this group of proteins could be an important common allergen in clinical allergy to legumes. Other panallergens of increasing importance are lipid transfer proteins (14). However, some clinical studies have reported that there is little cross-reactivity between members of the legume family (15-16).
In fact, although the different legumes have structurally homologous proteins, they are not all equally allergenic, thus making it difficult to distinguish in vitro and in vivo cross-reactivity. Studies in Spanish patients, in whom a high prevalence of chick pea allergy occurs, have shown that most of the patients are sensitised to more than one species. A great degree of cross-reactivity was demonstrated among Lentil, Chick pea, Pea and Peanut by inhibition studies. The authors report that unlike the Anglo-Saxon population, this phenomenon implies clinical sensitisation for many Spanish children and that the majority of these patients have had symptoms with more than one legume (median 3 legumes). Of 39 patients challenged with two or more legumes, 32 (82 %) reacted to two or more legumes: 43,5 % to 3, 25,6 % to 2, 13 % to 4 legumes. Seventy three per cent of the patients challenged with Lentil and Pea had positive challenge to both, 69,4 % to Lentil and Chick pea, 60 % to Chickpea and 64,3 % to Lentil, Chick-Pea and Pea simultaneously. Peanut allergy was associated with to allergy to Lentil, Chick pea and Pea but less frequently, whereas White bean and Green bean and Soybean were well tolerated by children allergic to other legumes. The authors stressed that in spite of an evident clinical and immunological cross-reactivity, the diagnosis of legume allergy should not be based only on allergen-specific IgE tests (17).
Nevertheless, some reports of specific cross-reactivity between certain members of this family have been published. Lentils appear to be cross-reactive with Chick pea and beans (4,18-19), and cross-reactivity was shown between Pea, Soybean, White bean, Peanut, Lentil, Fennel, Guar gum, Carob bean, Tragacanth, Chick pea and Liquorice (20).
Of 720 patients evaluated for oral allergy syndrome (OAS), and sensitisation to Plane tree (P. acerifolia) pollen, 61 (8.48%) were sensitised to pollen from this tree, and food allergy was reported in 32 (52.45%) of these 61 patients. The food allergens most frequently implicated were Hazel nuts, Peach, Apple, Peanuts, Maize, Chick pea and Lettuce. The study concluded that cross-reactivity was observed between P. acerifolia pollen and plant-derived foods, and that OAS in these patients may have been caused by primary respiratory sensitisation to Plane tree pollen. The authors suggested that profilin may be the responsible allergen (7).
Cross-reactivity between allergens from Latex and Chick pea was recently described in a boy with spina bifida with allergy to Chick pea, which developed after the appearance of Latex allergy symptoms. IgE antibodies to Latex and Chick pea were demonstrated by SPT and serum IgE antibodies (21).
In a Spanish study, symptomatic hypersensitivity to Chick peas was frequently associated with Lentil allergy (22). In another Spanish study, aimed at determining the prevalence of Lupin sensitisation in 1,160 subjects consulting allergologists, a 4,1 % sensitisation rate (28 patients) was found, with 75% co-sensitisation between Lupin and legumes. Of 28 patients, 13 were shown to have skin reactivity to Chick pea, 8 to Pea, 12 to Peanut, 13 to Bean, and 7 to Lentil (but 18 were not tested for Lentil) (23).