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The peanut allergy epidemic: allergen molecular characterisation and prospects for specific therapy.

Peanut (Arachis hypogaea) allergy is a major cause of food-induced anaphylaxis, with increasing prevalence worldwide. To date, there is no cure for peanut allergy, and, unlike many other food allergies, it usually persists through to adulthood. Prevention of exposure to peanuts is managed through strict avoidance, which can be compromised by the frequent use of peanuts and peanut products in food preparations. Conventional subcutaneous-injection allergen immunotherapy using crude peanut extract is not a recommended treatment because of the risk of severe side effects, largely as a result of specific IgE antibodies. Consequently, there is an urgent need to develop a suitable peanut allergen preparation that can induce specific clinical and immunological tolerance to peanuts in allergic individuals without adverse side effects. This requires detailed molecular and immunological characterisation of the allergenic components of peanut. This article reviews current knowledge on clinically relevant peanut allergens, in particular Ara h 1, Ara h 2 and Ara h 3, together with options for T-cell-reactive but non-IgE-binding allergen variants for specific immunotherapeutic strategies. These include T-cell-epitope peptide and hypoallergenic mutant vaccines. Alternative routes of administration such as sublingual are also considered, and appropriate adjuvants for delivering effective treatments at these sites examined.

Allergens↗

Thermal stability and mode of oligomerization of the tetrameric peanut agglutinin: a differential scanning calorimetry study.

Peanut agglutinin is a homotetrameric legume lectin. The crystal structure of peanut agglutinin shows that the four subunits associate in an unusual manner, giving rise to open quaternary structure [Banarjee, R., et al. (1994) Proc. Natl. Acad. Sci. U.S.A. 91, 227-231]. The thermal unfolding of peanut agglutinin has been characterized by differential scanning calorimetry and gel filtration to elucidate its thermal stability and its mode of oligomerization. The unfolding process is reversible and could be described by a three-state model with two transitions occurring at around 331 and 336 K. For the tetramer, the ratio of DeltaHc/DeltaHv for the first transition is close to 4 and for the second transition is close to 0.25, suggesting that 4 and 0.25 cooperative unit(s) of the tetramer are involved in the first and second transitions, respectively. The agreement between the model-independent DeltaHv(S) determined from the values of the temperatures of the peak maximum (Tp1) with the protein concentration with the values of DeltaHv obtained from the fit of the data to the transition confirms that the first peak is associated with the dissociation of peanut agglutinin tetramers (A4) to "folded" monomers (4A), whereas the second peak describes the unfolding (4U) of these monomers. The overall process for the thermal unfolding of peanut agglutinin could therefore be summarized as A4 <==> 4A <==> 4U. Gel filtration studies confirm this process, as peanut agglutinin elutes as a tetramer up to 50 degrees C, and at and above 56 degrees C (Tm of first transition), it elutes at a position commensurate with that of the folded monomer of peanut agglutinin. The unfolding behavior of peanut agglutinin in the presence of saturating amounts of carbohydrate ligands is similar to that observed for the unligated form. The temperature of maximal stability of the peanut agglutinin tetramer at pH 7.4 is calculated to be around 33 degrees C with a maximal free energy of stabilization of 8.70 kcal/mol. The results demonstrate that unfolding of peanut agglutinin goes through two distinct phases with folded monomer being the intermediate.

Calorimetry, Differential Scanning↗

Linking peanut allergenicity to the processes of maturation, curing, and roasting.

The processes of peanut maturation, curing, and roasting are known to have an important role in peanut flavors. One of these processes (i.e., roasting) has been found to have an effect on allergenicity. To determine if the other processes (i.e., maturation and curing) affect allergenicity, mature and immature roasted peanuts and peanuts cured at different temperatures (35-77 degrees C) were, respectively, tested for IgE binding and advanced glycation end adducts (AGEs). Peanuts with and without stress proteins, which are associated with peanut maturation and curing, were also tested. Results showed that mature roasted peanuts exhibited a higher IgE binding and AGEs level than immature roasted peanuts. Curing temperatures between 35 and 60 degrees C gave no difference in the profiles. However, a higher curing temperature (i.e., 77 degrees C) exhibited a profile of higher levels of AGEs and IgE binding. These levels were higher in peanuts with stress proteins than without stress proteins. Roasting increased stress protein level and IgE binding. From these results, the processes of maturation and curing, in conjunction with roasting, may be associated with allergenicity, suggesting that these processes may lead to changes in the allergenic properties of peanuts.

Allergens↗

Recent advances in peanut allergy.

Peanut remains preeminent as the food allergen most associated with severe and fatal allergic reactions. Reactions are frequent despite patients' best efforts to avoid peanut. In the future, better information sharing and communication between families and both schools and restaurants may lead to a decrease in the rate of severe reactions induced by exposure to peanut outside the home. Reaction severity may increase over time but up to 25% of young peanut allergic individuals may outgrow their peanut allergy. Personalized care plans and education programmes may have an impact on avoidance of peanut and on the appropriate responses of caregivers. Peanut's allergenicity may be affected by the method of cooking, with roasted peanuts appearing more allergenic than boiled or fried peanuts. Immunotherapy with modified peanut allergens and DNA based vaccines may soon move from animal studies to clinical trials.

Animals↗

Epicutaneous exposure to peanut protein prevents oral tolerance and enhances allergic sensitization.

BACKGROUND: Food allergies are an important cause of life-threatening hypersensitivity reactions. Oral tolerance can be considered the default immune response to dietary antigens, with immune deviation resulting in allergic sensitization. However, primary sensitization to food allergens may not solely be through the gastrointestinal mucosa, as strong T-helper type 2 (Th2)-biased immunity can result from exposure to protein allergens on barrier-disrupted skin. OBJECTIVE: The purpose of this study was to examine whether exposure to allergens through the skin may interfere with the normal development of oral tolerance and promote allergic sensitization to food proteins. METHODS: Female BALB/c mice were exposed epicutaneously to peanut protein and induction of systemic oral tolerance through high dose feeds of peanut protein was subsequently assessed. Other mice were rendered tolerant prior to epicutaneous peanut exposure. Sensitivity to peanut was determined by assessing delayed-type hypersensitivity, proliferative, cytokine and antibody responses. RESULTS: Epicutaneous exposure to peanut protein induced potent Th2-type immunity with high levels of IL-4 and serum IgE. Primary skin exposure prevented the subsequent induction of oral tolerance to peanut in an antigen-specific manner. Upon oral challenge, mice became further sensitized and developed strong peanut-specific IL-4 and IgE responses. Furthermore, animals with existing tolerance to peanut were partly sensitized following epicutaneous exposure. CONCLUSION: Epicutaneous exposure to peanut protein can prevent induction of oral tolerance, and may even modify existing tolerance to peanut. Epidermal exposure to protein allergens selectively drives Th2-type responses, and as such may promote sensitization to food proteins upon gastrointestinal exposure.

Administration, Cutaneous↗

Feeding a soy formula to children with cow's milk allergy: the development of immunoglobulin E-mediated allergy to soy and peanuts.

Peanut allergy has been associated with the intake of soy milk or a soy formula. We studied the development of immunoglobulin E antibodies specific to soy and peanuts and of allergic reactions caused by peanuts, in children with confirmed cow's milk (CM) allergy fed either a soy formula or an extensively hydrolyzed formula (EHF). One hundred and seventy infants with documented CM allergy (CMA) were randomly assigned to receive either a soy formula or an EHF. The children were followed to the age of 4 yr. Peanut-specific immunoglobulin E was measured at the age of 4. A detailed history of the occurrence of allergic reactions caused by peanuts was recorded by the parents. Soy-specific immunoglobulin E antibodies were measured at the time of diagnosis and at the ages of 1, 2 and 4 yr. Immunoglobulin E antibodies to soy (> or =0.35 kU/l) were found in 22 of 70 children fed the soy formula, and in 14 of 70 of the children fed the EHF (p = 0.082). In an open challenge with soy at the age of 4, no immediate reactions were observed. One of 72 children from the soy group had a delayed reaction. immunoglobulin E antibodies to peanuts (> or =0.35 kU/l) were found in 21 of 70 children fed the soy formula and 17 of 69 infants fed the EHF (p = 0.717). The incidence of reported peanut allergy in the soy group was two of 72 (3%) and four of 76 (5%) in the EHF group (p = 0.68). Development of immunoglobulin E-associated allergy to soy and peanuts was rare in our study group of milk allergic children. The use of a soy formula during the first 2 yr of life did not increase the risk of development of peanut-specific immunoglobulin E antibodies or of clinical peanut allergy.

Arachis↗

Allergenicity of various peanut products as determined by RAST inhibition.

Extracts of 19 different peanut products and peanut oil were tested for their allergenicity by the radioallergosorbent test inhibition assay using a crude peanut extract from raw peanuts as the standard for comparison. Seventeen of the extracts were able to competitively inhibit the binding of serum IgE from peanut-sensitive patients with the solid-phase raw peanut extract. Peanut oil and the extract from hydrolyzed peanut protein did not inhibit binding, which suggests that these products are not allergenic. The peanut hull flour extract showed a slight ability to inhibit binding, suggesting that this product contains minor amounts of the peanut allergen.

Allergens↗

Highly atopic children: formation of IgE antibody to food protein, especially peanut.

Highly atopic infants often form IgE antibodies toward multiple food protein in the first 2 years of life. They begin producing IgE antibody to inhalant allergens between the first and second year of life. We hypothesized that highly atopic children would be at significant risk of sensitization to peanut. We defined high atopy as serum IgE greater than or equal to 10 times 1 SD from normal plus multiple positive RASTs. In this study we have characterized the immunologic status of 141 patients by measuring total serum IgE and specific IgE to several allergens, including peanut. These data demonstrated that, independent of clinical history, a positive RAST to peanut was more common in the highly atopic category compared to the low atopy category. Significantly more patients who were highly atopic and had a positive peanut RAST had a positive RAST for egg or milk compared to low atopic patients. More significantly, 33 of the patients had never knowingly received peanut, yet 21 (63.6%) had a positive RAST for peanut, whereas seven (21.2%) had a peanut antibody in the highest RAST category. All these seven patients were considered highly atopic according to the definition above, and three were younger than 2 years of age. These results suggest that highly atopic infants are at special risk for sensitization to peanut, even when they have never received peanut, and that characterization of immunologic sensitization to milk, egg, and peanut will identify the highly atopic infant.(ABSTRACT TRUNCATED AT 250 WORDS)

Adolescent↗

Effects of chronic peanut consumption on energy balance and hedonics.

OBJECTIVE: To investigate the effects of chronic peanut consumption on energy balance and hedonics. DESIGN: Thirty-week, cross-over, intervention study. Participants were provided 2113+/-494 kJ/day (505+/-118 kcal/day) as peanuts for 8 weeks with no dietary guidance (free feeding-FF), 3 weeks with instructions to add peanuts to their customary diet (addition-ADD) and 8 weeks where peanuts replaced an equal amount of other fats in the diet (substitution-SUB). SUBJECTS: Fifteen, healthy, normal-weight (BMI of 23.3+/-1.8) adults, aged 33+/-9 y. MEASUREMENTS: Dietary intake, appetitive indices, energy expenditure, body weight and hedonics. RESULTS: During FF, peanut consumption elicited a strong compensatory dietary response (ie subjects compensated for 66% of the energy provided by the nuts) and body weight gain (1.0 kg) was significantly lower than predicted (3.6 kg; P<0.01). When customary dietary fat was replaced with the energy from peanuts, energy intake, as well as body weight, were maintained precisely. Participants were unaware that body weight was a research focus. Resting energy expenditure was increased by 11% after regular peanut consumption for 19 weeks (P<0.01). Chronic consumption of peanuts did not lead to a decline in pleasantness or hunger ratings for peanuts nor did it lead to any hedonic shift for selected snack foods with other taste qualities during any of the three treatments. CONCLUSIONS: Despite being energy dense, peanuts have a high satiety value and chronic ingestion evokes strong dietary compensation and little change in energy balance.

Adult↗

Carob is not allergenic in peanut-allergic subjects.

BACKGROUND: The antigenic potential of proteins from the carob bean, a member of the legume family used as a food additive, have not so far been investigated and legumes share antigenic proteins with peanut, a potent trigger of anaphylaxis. OBJECTIVE: To assess the carob protein determinants of sensitization in peanut-allergic children. METHODS: In a prospective, double-blind, placebo-controlled study 12 patients (median age 9.5 years) with a history of hyperreactivity to peanut (anaphylaxis) were assessed. Skin prick tests with a commercial peanut allergen, raw carob pulp, raw and cooked carob cotyledon formula were used to confirm the history. RAST for peanuts and cooked carob were used to evaluate sensitization to these proteins. Carob-specific IgE were identified by immunoblotting analyses. Allergic reactivity was evaluated during double-blind placebo-controlled food challenges (DBPCFC; 5.5 g carob extract and cooked carob cotyledon formula). RESULTS: Peanut allergen-induced skin prick test positivity in all children (confirmed during double-blinded challenge in 6/12 patients), carob pulp in 3/12 patients, raw carob bean in 6/12, and cooked carob cotyledon formula in none. RAST were positive for peanut in all cases but negative for carob beans in 9/12 cases. Immunoblot analyses found peanut-specific IgE in all cases and raw carob bean-specific IgE in eight cases. Carob allergens were identified in the 17.5, 48, and 66 kDa MW bands. The least allergenic density was found for cooked carob proteins. There was no clinical reactivity with either raw or cooked carob during DBPCFC. CONCLUSIONS: These data suggest that carob-specific sensitization, apparent both in vitro and in SPTs, can be concordant with peanut allergy and that cooked carob can be ingested by children who are allergic to peanuts. That heat-processing deactivates carob protein allergenicity has dietary implications for polyallergic children.

Adolescent↗

Engineering, characterization and in vitro efficacy of the major peanut allergens for use in immunotherapy.

BACKGROUND: Numerous strategies have been proposed for the treatment of peanut allergies, but despite the steady advancement in our understanding of atopic immune responses and the increasing number of deaths each year from peanut anaphylaxis, there is still no safe, effective, specific therapy for the peanut-sensitive individual. Immunotherapy would be safer and more effective if the allergens could be altered to reduce their ability to initiate an allergic reaction without altering their ability to desensitize the allergic patient. METHODS: The cDNA clones for three major peanut allergens, Ara h 1, Ara h 2, and Ara h 3, have been cloned and characterized. The IgE-binding epitopes of each of these allergens have been determined and amino acids critical to each epitope identified. Site-directed mutagenesis of the allergen cDNA clones, followed by recombinant production of the modified allergen, provided the reagents necessary to test our hypothesis that hypoallergenic proteins are effective immunotherapeutic reagents for treating peanut-sensitive patients. Modified peanut allergens were subjected to immunoblot analysis using peanut-positive patient sera IgE, T cell proliferation assays, and tested in a murine model of peanut anaphylaxis. RESULTS: In general, the modified allergens were poor competitors for binding of peanut-specific IgE when compared to their wild-type counterpart. The modified allergens demonstrated a greatly reduced IgE-binding capacity when individual patient serum IgE was compared to the binding capacity of the wild-type allergens. In addition, while there was considerable variability between patients, the modified allergens retained the ability to stimulate T cell proliferation. CONCLUSIONS: These modified allergen genes and proteins should provide a safe immunotherapeutic agent for the treatment of peanut allergy.

2S Albumins, Plant↗

A comparison study on allergen components between Korean (Arachis fastigiata Shinpung) and American peanut (Arachis hypogaea Runner).

The prevalence of peanut allergy in Korea is lower than in America. Peanut extract allergens between the two countries have not been standardized. This study was performed to compare the allergenicity of raw Korean and American peanuts with that of roasted peanuts. We prepared the peanut extracts in Korean raw (KP) and roasted peanuts (KRP), and also in American raw (AP) and roasted (ARP) peanuts. We compared the peanut extract allergens of KP, KRP, AP and ARP in vitro with sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) followed by immunoblotting, T-cell proliferation assay and skin prick test with sera from peanut-allergic patients. SDS-PAGE and Western blotting demonstrated four allergenic extracts, numerous bands that displayed a high prevalence of IgE binding. IgE-binding bands were at 64, 36 and 17 kDa. Western blot inhibition revealed that either KP or AP could almost completely inhibit the reactivity of the other extract. There were no differences between T-cell proliferation assay and skin prick test. In conclusion, this investigation showed no different allergic components in both raw and roast extracts of Korean and American peanuts.

Allergens↗

Effects of overprocessing on the nutritional quality of peanut meal.

Two experiments were conducted to evaluate the effects of overprocessing by autoclaving on the in vivo protein quality and in vitro protein solubility in 0.2% KOH of solvent-extracted peanut meal containing 48% protein. The peanut meal was autoclaved at 120 C and 105 kPa for 0, 20, 30, 40, 50, 60, or 90 min. In vivo protein quality of the autoclaved peanut meal was evaluated in chicks fed corn-peanut meal diets (22.5% protein) from 8 to 22 d of age and in adult cecectomized roosters using a precision-fed amino acid digestibility assay. Chick performance was significantly decreased when peanut meal had been autoclaved (P < 0.05) 60 min or more in one experiment and by 40 min or more in the other experiment. True digestibility of amino acids in peanut meal also decreased as autoclaving time increased. The effect of autoclaving was greatest for lysine, wherein digestibility was 87, 72, 68, and 57% for peanut meal autoclaved for 0, 30, 60, or 90 min, respectively. Protein solubility of peanut meal in 0.2% KOH decreased from 78 to 56% as autoclaving time increased from 0 to 90 min. Protein solubility values of 70% or lower were indicative of decreased in vivo peanut meal quality. The results of this study indicated that overprocessing by autoclaving reduces the protein quality of peanut meal and that protein solubility in KOH is a useful in vitro index of overprocessing.

Amino Acids↗

Polyisotypic antipeanut-specific humoral responses in peanut-allergic individuals.

BACKGROUND: Peanut-containing food products may induce severe clinical reactions in sensitized subjects, and high levels of antipeanut IgE have been reported in the literature. Immunotherapy, proposed for the prevention of severe accidents, is often ill-tolerated and only partly efficient. This could be due to the spontaneous development of polyisotypic antipeanut antibodies. OBJECTIVE: To appreciate the presence and reactivity of other isotypes other than IgE of peanut-specific antibodies in serum samples from peanut-sensitized subjects. METHODS: Serum samples were obtained from 20 non-sensitized subjects and 23 sensitized patients divided in three groups according to their response to peanut oral challenge (no response or response to high or low doses, respectively). Peanut-specific IgG, IgG subclasses, IgA and IgM were assayed using an ELISA, and their reactivity against peanut proteins tested using Western Blot. RESULTS: A large dispersion of antipeanut antibody levels was observed in the three groups of patients, high levels of IgG, IgG1, IgG4 and IgA usually correlating with highly positive radioallergosorbent test (RAST). Such high levels were observed at onset in four patients who underwent peanut immunotherapy who had side effects and poor efficiency. Western blotting demonstrated that the polyisotypic response observed was directed to several peanut antigens, including the major allergens, Ara h1 and Ara h2. CONCLUSION: Peanut-sensitized patients who spontaneously develop specific IgE, display polyisotypic-specific antibody responses, whatever their response to oral challenge. This might explain the poor efficiency of peanut rush immunotherapy attempts.

Adolescent↗

Accidental ingestions in children with peanut allergy.

BACKGROUND: Accidental exposure to peanut has been reported to occur frequently. Total avoidance of peanut is difficult because of its widespread use, manufacturing and labeling errors, utensil contamination, and label misinterpretation. OBJECTIVE: Given the apparent increased awareness of peanut allergy by both consumers and food manufacturers, we aimed to determine the current frequency of accidental exposures occurring in peanut allergic children in Quebec and to identify factors associated with exposure. METHODS: The parents of children with peanut allergy diagnosed at the Montreal Children's Hospital completed questionnaires about accidental exposure to peanut occurring over the period of the preceding year. Logistic regression was used to identify associated factors. RESULTS: Of 252 children, 62% were boys, with a mean age of 8.1 years (SD, 2.9). The mean age at diagnosis was 2.0 years (SD, 2.1). Thirty-five accidental exposures occurred in 29 children over a period of 244 patient-years, yielding an annual incidence rate of 14.3% (95% CI, 10.0% to 19.9%). Fifteen reactions were mild, 16 moderate, and 4 severe. Of 20 reactions that were moderate to severe, only 4 received epinephrine. Eighty percent of children attended schools prohibiting peanut, and only 1 accidental exposure occurred at school. No associated factors were identified. CONCLUSION: Accidental exposure to peanut occurs at a lower frequency than previously reported, but most reactions are managed inappropriately. CLINICAL IMPLICATIONS: Enhanced awareness, access to safer environments, and good food manufacturing practices may have contributed to a lower incidence of inadvertent peanut exposure, but a further reduction and better education on allergy management are desirable.

Adolescent↗

Prevalence of peanut and tree nut allergy in the United States determined by means of a random digit dial telephone survey: a 5-year follow-up study.

BACKGROUND: Allergy to peanuts and tree nuts (TNs) is the leading cause of fatal and near-fatal food allergic reactions. Peanut allergy appears to be increasing in prevalence. OBJECTIVES: We sought to determine the prevalence of self-reported peanut and TN allergy among the general population of the United States in 2002 by sex and age and to compare the results with prevalence estimates obtained 5 years earlier. METHODS: We performed a nationwide, cross-sectional, random telephone survey by using a standardized questionnaire. RESULTS: A total of 4855 households participated (53% participation rate), representing a census of 13,493 individuals. Peanut allergy, TN allergy, or both was self-reported in 166 (1.2%; 95% CI, 1.0%-1.4%) individuals in 155 (3.2%; 95% CI, 2.7%-3.7%) households, overall prevalence rates similar to those reported in 1997. Also similar to the 1997 survey, the severity level was high, with 79% reporting respiratory or multiple organ system reactions and 66% experiencing more than 5 lifetime reactions. Despite the severity and reaction frequency, only 74% of the children and 44% of the adults sought evaluation for the allergy, and fewer than half who did were prescribed self-injectable epinephrine. Applying conservative rules to adjust for persons with unconvincing reactions and a false-positive rate of the survey instrument (7%), a final prevalence estimate of 1.04% (95% CI, 0.9%-1.24%) was obtained. A male predominance of peanut-TN allergy was reported in children younger than 18 years (1.7% vs 0.7%, P =.02), and a female predominance was reported among adults (1.7% vs 0.9%, P =.0008). Although the rate of peanut allergy, TN allergy, or both was not significantly different from 1997 to 2002 among adults, the rate increased from 0.6% to 1.2% among children, primarily as a result of an increase in reported allergy to peanut (0.4% in 1997 to 0.8% in 2002, P =.05). CONCLUSIONS: Self-reported peanut allergy has doubled among children from 1997 to 2002, and peanut allergies, TN allergies, or both continue to be reported by more than 3 million Americans. Considering that reactions are severe and the allergy is persistent, these allergies represent an increasing health concern.

Adolescent↗

Lack of association of HLA class II alleles with peanut allergy.

BACKGROUND: Peanut allergy is a common and severe phenotype of food allergy with a strong genetic component; HLA class II polymorphisms are attractive candidate genes for this disorder. OBJECTIVE: To determine possible genotypic associations of HLA class II with peanut allergy and attempt replication of previously reported associations. METHODS: Sibling pairs discordant for peanut allergy were genotyped (low resolution) by polymerase chain reaction-based methods to 7 DQ and 18 DR allele groups. A chi2 analysis was undertaken against sibling controls with statistical adjustment for multiple analyses. RESULTS: Seventy-three children with confirmed peanut allergy (mean age, 6.5 years; male, 72%; asthma, 58%; atopic dermatitis, 62%; allergic rhinitis, 67%; other food allergies, 41%) and 75 of their siblings who eat peanut (mean age, 8 years; male, 52%; asthma, 12%; atopic dermatitis, 22%; allergic rhinitis, 37%; other food allergy, 7%) were genotyped. Distribution of DQ7 (29% of children with peanut allergy vs 47% sibling controls) was statistically significantly different (P = .04) before statistical correction for multiple comparisons was made by multiplying them by the number of alleles tested (and not statistically significant after correction; P = .30). Distribution of DR11 was nearly statistically significant without statistical adjustment (26% with peanut allergy vs 41% of sibling controls; P = .07; corrected P = 1.3). Alleles that were previously reported to have a weak association with peanut allergy (DRB1 *03, *08; DQB1 *0302, *04) were not verified in this cohort (unadjusted P > .44). CONCLUSIONS: We could not establish an association between the HLA class II alleles evaluated in this cohort of sibling pairs discordant for peanut allergy.

Child↗

Serological characteristics of peanut allergy in children.

BACKGROUND: Food challenge is considered an excellent clinical tool for the diagnosis of specific food allergy. However in the case of peanut allergy it may be difficult to perform because of the severity of the reactions. The quantitation of a specific immunoglobulin E (IgE) response to different peanut allergens could also contribute to the improvement of the diagnosis. We characterized the IgE response to a whole peanut protein extract and to Ara h 1 and Ara h 2 in different groups of patients classified according to the severity of their allergic reactions. METHODS: Specific serum IgE were analyzed in 96 children by enzyme-linked immunosorbent assay tests using a whole protein extract or purified peanut proteins and anti-human IgE monoclonal antibodies labeled with acetylcholinesterase. RESULTS: A parallel was observed between levels of peanut-specific IgE and the classification in five groups and subgroups of patients upon increasing severity of symptoms, especially within the group of highest severity. Moreover, the highest frequency of positive response and the highest levels of specific IgE were observed with whole peanut protein extract. CONCLUSION: In a retrospective evaluation of peanut allergy in children, we have shown that quantitation of peanut-specific IgE could be used to avoid a food challenge particularly in the case of severe reactions. When compared to Ara h 1 and Ara h 2, whole peanut protein extract appeared to be the most appropriate allergen to perform the test.

2S Albumins, Plant↗