rAra h 3 Peanut

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f13 Peanut

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Code: f424
Latin name: Arachis hypogaea
Source material: rAra h 3 is a CCD-free recombinant protein
Common names: Glycinin

Biological function: 11S globulin trypsin inhibitor
Mw: 57 kDa


Peanuts are the seeds of an annual legume, which grows close to the ground and produces its fruit below the soil surface. This is in contrast to tree nuts like Walnuts and Almonds. Peanut is a member of the Fabaceae or legume family, whereas tree nuts are not.

Multiple Peanut varieties are grown, with more than 40% of the American Peanut crop consumed as Peanut butter (1). Runners have become the dominant Peanut type grown in the U.S. due to the spectacular increase in yield that they allow; they are a very important source of Peanut butter. Virginias have the largest kernels and account for most of the Peanuts roasted and sold in their shells. Spanish peanuts have smaller kernels covered with a reddish-brown skin. Valencias are small, very sweet Peanuts usually roasted and sold in the shell, or boiled, but seldom used in processed foods.

The difference in the methods of preparing Peanut as practiced in China compared with that widely used in the United States and Western countries may help explain the difference in prevalence of Peanut allergy observed (28). Roasting of Peanut uses higher temperatures (150-170 °C) than boiling (100 °C) or frying (120 °C), and roasting has been shown to increase the allergenic property of Peanut proteins (2).

However, part of the difference in allergenicity may not be as a result of the heat-treatment per se but as a result of other factors. Some authors suggest that the decrease in allergenicity of boiled Peanuts results mainly from a transfer of low-molecular-weight allergens into the water during cooking (3). Allergen content may vary depending on the Peanut variety and may explain the differences in the prevalence of sensitisation between different population studies (4).

The major Peanut allergens are homologous to the seed storage proteins of the conglutin, vicilin, and glycinin families (5).
Peanut proteins were originally classified as albumins (water-soluble) or globulins (saline-soluble); the globulins were in turn subdivided into arachin and conarachin fractions (the major storage proteins). Components of the albumin fraction of Peanuts are agglutinins, lectin-reactive glycoproteins, protease inhibitors, alpha-amylase inhibitors and phospholipases (6).

Peanut contains, among other, storage and non-storage proteins. The allergens, Ara h 1, Ara h 2, Ara h 3, Ara h 4, Ara h 6, Ara h 7 are seed storage proteins. The major Peanut allergen, Ara h 1, is a heat stable 7S vicilin-like globulin, Ara h 2 is a conglutin (functioning as a trypsin inhibitor), and Ara h 3 is a glycinin. A 59% sequence identity exists between Ara h 2 and Ara h 6, and 35% between Ara h 2 and Ara h 7 (7).

Peanut contains up to 32 different proteins, of which at least 18 have been identified as being capable of binding allergen-specific IgE antibodies (8-9). Varieties of Peanuts from different parts of the world contain similar proteins, including Ara h 1 and Ara h 2, and the IgE-binding properties have also been reported to be similar to a great extent (10).

Allergens characterised to date include:

  • Ara h 1, a 7S vicilin-like globulin (11).
  • Ara h 2, a 2S albumin, a conglutin, a trypsin inhibitor (12).
  • Ara h 3, an 11S globulin, a glycinin, a trypsin inhibitor (13).
  • Ara h 4, an 11S globulin, a glycinin (14).
  • Ara h 5, a profilin (14).
  • Ara h 6, a 2S albumin, a conglutin (15).
  • Ara h 7, a 2S albumin, a conglutin (14).
  • Ara h 8, a Bet v 1-homologous allergen, PR-10 protein (16).
  • Ara h Agglutinin (17).
  • Ara h LTP, a lipid transfer protein (18).
  • Ara h Oleosin (9).

Ara h 3 and Ara h 4 are regarded as isoforms of each other, i.e., Ara h 4 and Ara h 3 are considered to be the same allergen (13,20).

Ara h 1 comprises 12% to 16% of the total protein in Peanut in population studies, sensitisation to Ara h 1 was found in 95% of Peanut-allergic patients from North America (6,21-23), but in fewer Peanut-allergic patients of 3 European populations, varying from 35% to 70% (1,15,24-25). These differences were not reported for Ara h 2, even though Peanuts from different varieties and from different parts of the world contain similar proteins and the IgE binding properties are similar (10). Unidentified Peanut proteins with molecular weights somewhat lower than 15 kDa may be important allergens as well (26). Ara h 3 is recognised by serum IgE from 45% - 50% of patients with Peanut sensitivity (27). Ara h 5 shows up to 80% amino acid sequence identity with the panallergen profilin, but is present only in low amounts in Peanut extracts. 13% to 16% of Peanut-allergic individuals are sensitised to Peanut profilin (28). Nonetheless, a number of peanut allergens are involved in the sensitisation process.

Sensitisation to Peanut occurs with a high degree of heterogeneity to a number of Peanut allergens. Mono-sensitisation to a single Peanut allergen is relatively rare (29). Although sensitisation to Ara h 1 and Ara h 2 occurs in the great majority of Peanut-allergic individuals, the wide range of allergens present in whole Peanut protein extract appears to be most appropriate to consider when testing for Peanut allergy (23).

For example, in a British study, evaluating sera of 40 Peanut-allergic individuals, of 18 allergens identified, 8 were bound by >50% of patients. The study concluded that promiscuity of IgE binding appears more important than the recognition of individual proteins (30).

Furthermore, some Peanut-allergic subjects fail to bind to either Ara h 1 or 2 suggesting that whole Peanut, rather than Ara h 1 or 2, or the use of individual Peanut allergens would be more appropriate for measuring allergen-specific-IgE responses. This also illustrates that the relative contribution of all Peanut allergens needs to be investigated (23).

In a recent Dutch study examining the IgE reactivity to major Peanut allergens in 20 Peanut-allergic children at two subsequent time-points, before DBPCFC, all 20 Peanut-allergic children were shown to have IgE antibodies to Ara h 2, 16 to Ara h 6, and 10 to both Ara h 1 and Ara h 3. After 20 months, Peanut-specific IgE levels and the individual recognition of major allergens were comparable with the levels and recognition before challenge. Skin reactivity was detected to Ara h 2 and Ara h 6 in most children, whereas for Ara h 1 and Ara h 3 in approximately 50% of the children. No parameters could be related to the severity of Peanut allergy (31).

The availability of recombinant Peanut allergens has resulted in a greater ability to assess the sensitisation and clinical profiles of individual Peanut allergens in different population groups. This is illustrated by a number of studies.

In an evaluation of recombinant allergens, Ara h 1, Ara h 2, and Ara h 3, using sera of 77 American Peanut-allergic patients, seven different patterns of sensitisation were identified. The majority of patients (97%) had IgE antibodies to at least one of the recombinant allergens (Ara h 1,
Ara h 2, and Ara h 3), and 77%, 75% and 77% recognized rAra h1, rAra h 2 and rAra h 3 respectively. High epitope diversity was found in patients with a history of more severe allergic reactions (32).

A European study evaluating sera from 40 patients for sensitisation to six recombinant Peanut allergens, showed 14 individual recognition patterns. Of the sera, Ara h 1 was recognized by 65%, Ara h 2 by 85%, Ara h 4 by 53%, Ara h 5 by 13%, Ara h 6 by 38% and Ara h 7 by 43% (14).

Similarly, a French and American study aimed at evaluating the diagnostic value of the 3 major recombinant Peanut allergens utilizing skin test and serum IgE antibody determination in 30 Peanut-allergic patients. All patients with Peanut allergy demonstrated skin reactivity to rAra h 2; 40% reacted with rAra h 1 and 27% with rAra h 3. Monosensitisation to rAra h 2 was observed in 53% of patients. Levels of allergen-specific IgE did not correlate with the disease severity. However, patients with monosensitisation to rAra h 2 had a significantly lower severity score than polysensitised subjects and a lower level of allergen-specific IgE against Peanut extract and rAra h 2. Cosensitisation to rAra h 2 and rAra h 1 and/or rAra h 3 appeared to be predictive of more severe reactions (33).

A recent Dutch study investigated whether a sensitisation to individual allergens Ara h 1, Ara h 2, Ara h 3 and Ara h 6 could be correlated with clinical severity. Purified Peanut allergens were utilized for skin test and IgE antibody evaluation in 30 patients. The majority of patients were found to have allergen-specific IgE to Ara h 2 (25/30, 83%) and Ara h 6 (26/30, 87%). Sixteen patients (53%) were sensitised to Ara h 1 and 15 patients (50%) to Ara h 3. All patients with skin reactivity for Ara h 1 and/or Ara h 3 were also sensitised to Ara h 2 and/or Ara h 6. Patients with severe symptoms had a higher skin response to Ara h 2 and Ara h 6 at low concentrations (0.1 mug/ml) and to Ara h 1 and Ara h 3 at higher concentrations (100 mug/ml) compared with patients with mild symptoms. Patients with more severe symptoms also recognized a greater number of allergens and showed a higher cumulative skin response than with patients with mild symptoms. Ara h 2 and Ara h 6 appeared to be more potent than Ara h 1 and Ara h 3. Both skin reactivity to low concentrations of Ara h 2 and Ara h 6 and to higher concentrations of Ara h 1 and Ara h 3 were shown to be indicative of severe symptoms (34).

Recombinant Peanut allergens have been evaluated for their ability to predict the outcome of tolerance in Peanut-allergic individuals. An American study was performed using sera from 15 patients with symptomatic Peanut allergy and 16 patients who were sensitized but tolerant (of which 10 of these 16 patients had ”outgrown” their allergy) investigated 8 peptides representing the immunodominant sequential epitopes on Ara h 1, 2, and 3. It was found that regardless of their Peanut-specific IgE levels, most patients with symptomatic Peanut allergy showed IgE binding to the 3 immunodominant epitopes on Ara h 2. In contrast, each of these epitopes was recognized by < 10% of the tolerant patients. Tolerant patients did not recognize 2 immunodominant epitopes on Ara h 1. At least 93% of symptomatic, but only 12.5% of tolerant patients, recognized 1 of these “predictive” epitopes on Ara h 1 or Ara h 2. With up to 50% of patients with Peanut-specific IgE levels below suggested diagnostic decision levels still being clinically reactive, oral food challenges could be avoided in approximately 90% of these patients through the determination of peptide-specific IgE. This study analyzed only selected allergen epitopes rather than whole proteins (35).

Allergens from Arachis hypogaea listed by IUIS*

Ara h 1 Ara h 2 Ara h 3
Ara h 4 Ara h 5 Ara h 6
Ara h 7 Ara h 8 Ara h 9

*International Union of Immunological Societies (www.allergen.org) Jan. 2008.

Recombinant non-glycosylated protein produced in an E. coli strain carrying a cloned cDNA encoding Arachis hypogaea allergen Ara h 3

Common name: Glycinin
Biological function: 11S globulin trypsin inhibitor
Mw: 57 kDa

Allergen description

Ara h 3 is a glycinin, a member of the 11S globulin family, and may also function as a trypsin inhibitor (13,20,44,84-89). Ara h 3 was in first identified as a 14 kDa protein (90), but cloning revealed a 57 kDa protein that appears to be posttranslationally cleaved to smaller subunits (91).

Ara h 3 consists of a series of polypeptides ranging from approximately 14 to 45 kDa that can be classified as acidic and basic subunits, similar to the subunit organization of soy glycinin. Ara h 4 and Ara h 3 are considered to be the same allergen (13). Iso-allergens may be as a result of medication by post-translational cleavage (92).

A recent study also concluded, that Peanut-derived Ara h 3, in contrast to earlier reported recombinant Ara h 3, resembles, to a large extent, the molecular organization typical for proteins from the glycinin family. Posttranslational processing of Ara h 3 was shown to affect the IgE-binding properties and have impact on the allergenicity of Ara h 3 (13).

A comparison of the Peanut allergen sequences of Ara h 3/4, Ara h 3, Ara h 4 and Peanut trypsin inhibitor and the proteins Gly 1 and iso-Ara h 3 (not yet described as allergens), concluded that these proteins are isoallergens of each other, and that these isoallergens are post-translationally cleaved and held together by disulfide bonds in accordance to the 11S plant seed storage proteins signature (20).

The 11S globulins, also known as legumins, are classified into the Cupin superfamily, and are composed of 2 polypeptide chains of different molecular masses and amino acid sequences (heterodimeric form composed of a 20- to 40-kDa chain plus a 20- to 25-kDa chain), which are linked together by one disulfide bridge (93).

Between 20%-55% of Peanut-allergic individuals are sensitised to Ara h 3 (13,26,29,91). The prevalence of sensitization to a specific Peanut allergen varies between population groups (32). Ara h 3 was regarded as a minor allergen, but it was found that a group of Peanut-allergic Italian children were specifically sensitised to the basic subunit of Ara h 3. The authors stated their surprise that the dominant immunoreactivity in these patients was in a basic subunit of Ara h 3 because previous studies had indicated that Ara h 3 was only a minor Peanut allergen and that the identified allergenic epitopes occurred mainly in the acidic Ara h 3 subunit (88). It is therefore evident that sensitization to Ara h 3 depends on the population group studied and the methodology of the study, but there is a suggestion that the frequency of Ara h 3 sensitisation may indeed vary between population groups. In another study, recombinant Ara h 3 was recognized by IgE antibodies from approximately 45% of a Peanut-allergic patient population (91).

In a study that evaluated the pattern of IgE binding to specific Peanut allergens with the severity of clinical symptoms, 40 Peanut-allergic patients underwent a double-blind placebo-controlled low-dose Peanut challenge, during which the severity of the patients’ Peanut allergy was scored. Seventeen IgE binding bands were identified between 5 and 100 kDa with eight bound by >50% of patients and the total number of bands per patient correlated significantly with challenge score and serum IgE. However, two protein bands, identified as subunits of Ara h 3/4, had peak intensities that correlated positively with challenge score and a third band (Ara h 1) that correlated negatively. The study concluded that promiscuity of IgE binding appears more important than the recognition of individual proteins (30).

It has been argued that in contrast to recombinant Ara h 3, the allergen isolated from its native source is extensively proteolytically processed, and that native Ara h 3 polypeptides are much more complex than the recombinant protein used for epitope mapping experiments. The authors concluded that characterization of the allergenicity of Ara h 3 should therefore also include IgE-binding studies with Peanut-derived Ara h 3, providing the high degree of variation in the Ara h 3 protein structure, as this is what Peanut-allergic individuals are confronted with (94).

Ara h 3 is an 11S globulin and shares homology, and therefore varying degrees of cross-reactivity, with other 11S globulins. Sin a 2, a major allergen from Yellow mustard seed, was shown to have a sequence identity with other allergenic 11S globulins ranging between 27% and 38%. Three peptides described as epitopes in Ara h 3 were moderately conserved in Sin a 2 (95). Similarly, IgE-binding epitopes of Ara h 3 exhibited some structural homology among Peanut and tree nut allergens (Jug r 4 of Walnut, Cor a 9 of Hazelnut, Ana o 2 of Cashew nut) to account for the IgE-binding cross-reactivity observed. IgE-binding epitopes similar to those found in 11S globulin allergens do not apparently occur in other vicilin allergens with the cupin fold from Peanut (Ara h 1) or tree nuts (Jug r 2 of Walnut, Cor a 1 of Hazel nut, Ana o 3 of Cashew nut) (96).

Cross-reactivity has also been demonstrated between homologous Ara h 3 proteins (but not related) in Lupin (Lupin conglutin gamma) and Soybean (Soybean Bg7S) (97). A sequence similarity between Ara h 3 and the glycinins in Soybean and Pea of 62% to 72% has been reported (98).


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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.