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PubMedDate not supplied

Isolation, identification, and characterization of clones encoding antigens responsible for peanut hypersensitivity.

Peanut allergy is a significant health problem because of the frequency, the potential severity, and the chronicity of the allergic sensitivity. Serum IgE from patients with documented peanut hypersensitivity reactions and a peanut cDNA expression library were used to identify clones that encode peanut allergens. One of the major peanut allergens, Ara h I, was selected from these clones using Ara h I-specific oligonucleotides and polymerase chain reaction technology. The Ara h I clone identified a 2.3-kb mRNA species on a Northern blot containing peanut poly A+RNA. DNA sequence analysis of the cloned inserts revealed that the Ara h I allergen has significant homology with the vicilin seed storage protein family found in most higher plants. The isolation of the Ara h I clones allowed the synthesis of this protein in Escherichia coli cells and subsequent recognition of this recombinant protein in immunoblot analysis using serum IgE from patients with peanut hypersensitivity. With the production of the recombinant peanut protein it will now be possible to address the pathophysiologic and immunologic mechanisms regarding peanut hypersensitivity reactions specifically and food hypersensitivity in general.

Allergens↗
PubMed1995

Recombinant peanut allergen Ara h I expression and IgE binding in patients with peanut hypersensitivity.

Peanut allergy is a significant health problem because of the frequency, the potential severity, and the chronicity of the allergic sensitivity. Serum IgE from patients with documented peanut hypersensitivity reactions and a peanut cDNA expression library were used to identify clones that encode peanut allergens. One of the major peanut allergens, Ara h I, was selected from these clones using Ara h I specific oligonucleotides and polymerase chain reaction technology. The Ara h I clone identified a 2.3-kb mRNA species on a Northern blot containing peanut poly (A)+ RNA. DNA sequence analysis of the cloned inserts revealed that the Ara h I allergen has significant homology with the vicilin seed storage protein family found in most higher plants. The isolation of the Ara h I clones allowed the synthesis of this protein in E. coli cells and subsequent recognition of this recombinant protein in immunoblot analysis using serum IgE from patients with peanut hypersensitivity. With the production of the recombinant peanut protein it will now be possible to address the pathophysiologic and immunologic mechanisms regarding peanut hypersensitivity reactions specifically and food hypersensitivity in general

Adult↗
PubMed1997

Mapping and mutational analysis of the IgE-binding epitopes on Ara h 1, a legume vicilin protein and a major allergen in peanut hypersensitivity.

Peanut allergy is a significant health problem because of the prevelance and potential severity of the allergic reaction. Serum IgE from patients with documented peanut hypersensitivity reactions and overlapping peptides were used to identify the IgE-binding epitopes on the major peanut allergen, Ara h 1. At least twenty-three different linear IgE-binding epitopes, located throughout the length of the Ara h 1 protein, were identified. All of the epitopes were 6-10 amino acids in length, but there was no obvious sequence motif shared by all peptides. Four of the peptides appeared to be immunodominant IgE-binding epitopes in that they were recognized by serum from more than 80% of the patients tested and bound more IgE than any of the other Ara h 1 epitopes. Mutational analysis of the immunodominant epitopes revealed that single amino acid changes within these peptides had dramatic effects on IgE-binding characteristics. The identification and determination of the IgE-binding capabilities of core amino acids in epitopes on the Ara h 1 protein will make it possible to address the pathophysiologic and immunologic mechanisms regarding peanut hypersensitivity reactions specifically and food hypersensitivity in general.

Adult↗
PubMed1999

Peanut hypersensitivity in children.

Peanut is the major allergen in the United States. It is increasing in importance in Europe and has become the principal food allergen affecting children over the age of three years, once hypersensitivity to eggs has resolved. We report 132 pediatric cases of peanut hypersensitivity, confirmed by food challenge. The study group included 86 boys and 46 girls aged between 6 months and 15 years. More than half the children with peanut hypersensitivity were diagnosed before the age of three. The most common symptom was atopic dermatitis (43.1% of cases). The other symptoms observed were hoarseness (34.8%), asthma attacks (13.6%), anaphylaxis (6%), gastrointestinal symptoms (1.5%) and oral syndrome (0.7%). All patients had positive skin prick tests, with a mean wheal diameter of 8 mm (range: 2 to 25 mm). Wheal diameter was significantly smaller in the youngest children (mean 4.5 mm for children under the age of 1 year, p < 0.01). Specific IgE concentration was below 0.75 IU/ml in 16 cases (14.3%), the mean for the entire group being 30.9 IU/ml (range: 0.75 to 100 IU/ml). Food challenges were not performed in three of the eight children with a history of anaphylaxis. Labial food challenge (LFC) was positive in 85 cases (64.8%). An oral food challenge (OFC) was carried out for 45 children (34.3%) and the mean reactive dose was 850 mg (range: 1 mg to 7g). LFC with peanut oil was positive in 2 cases of 50 tested (4%) and 17 of 63 children (29.9%) tested by OFC were also found to be sensitized to peanut oil. Half the children were also hypersensitive to other foods, as demonstrated by oral challenge (53.7%) or sensitized to airborne allergens (62.8%). Hypersensitivity in the very youngest children raises questions about how sensitization occurs. Diagnosis was confirmed by food challenge. Peanut products are very difficult to eliminate from the diet because of inadequate labeling of food products. An ELISA test, available in a number of countries, can be used to detect the allergen.

Adolescent↗
PubMed2001

Oral administration of IL-12 suppresses anaphylactic reactions in a murine model of peanut hypersensitivity.

There is no satisfactory therapeutic intervention for peanut allergy, which accounts for most life-threatening food allergic reactions. Since IL-12 has been found to inhibit allergic airway responses in a mouse model of asthma and to cure Th2 cytokine-mediated murine schistosomiasis, we hypothesized that IL-12 treatment might also inhibit peanut allergic reactions. Consequently, we investigated the effects of oral IL-12 treatment in a murine model of peanut allergy and found that oral administration of liposome encapsulated rIL-12 could both prevent and reverse peanut hypersensitivity and could reduce histamine release, peanut-specific serum IgE and IgG1, and fecal IgA levels. Oral IL-12 treatment also increased IFN-gamma but did not decrease IL-4 or IL-5 levels. We conclude that oral rIL-12 treatment has therapeutic as well as preventive effects on peanut allergy, which are associated with increased IFN-gamma production.

Administration, Oral↗
PubMed1997

[Fatal and severe food hypersensitivity. Peanut and soya underestimated allergens].

Severe allergic reactions caused by foodstuffs have been reported in Sweden since 1993, 60 cases, five of them fatal, occurring during the first 3-year period. More than 70 per cent of all reactions reported were caused by patients, soya beans, nuts or almonds. In only 13 per cent of reported cases were the patients over 17 years of age. Several severe reactions were caused by soy protein, and mainly in children and adolescents with extremely severe peanut allergy and asthma. In many cases, severe symptoms first appeared more than one hour after soy intake. The report suggests soy allergy to be associated with an underestimated risk of severe reactions.

Adolescent↗
PubMed2000

The natural history of peanut allergy in young children and its association with serum peanut-specific IgE.

OBJECTIVES: To observe the nature and frequency of adverse reactions caused by accidental peanut exposure in young children with clinical peanut hypersensitivity and to determine the value of serum peanut-specific IgE levels during follow-up. STUDY DESIGN: Eighty-three children with clinical peanut hypersensitivity diagnosed before their fourth birthdays were contacted yearly to track adverse peanut reactions. Serum peanut-specific IgE levels were determined in 51 of 83 subjects. RESULTS: Fifty-eight percent (31/53) of subjects followed up for 5 years experienced adverse reactions from accidental peanut exposure. Regardless of the nature of their initial reaction, the majority with subsequent reactions (52%, 31/60) experienced potentially life-threatening symptoms. The group with isolated skin symptoms (11/51, 22%) had lower serum peanut-specific IgE levels than the group with respiratory and/or gastrointestinal symptoms (40/51, 78%) (median: 1.25 kU(A)/L vs 11. 65 kU(A)/L, P =.004, Wilcoxon rank sums test). Despite this, there was no threshold level below which only skin symptoms appeared to occur. Four selected subjects had negative double-blind placebo-controlled food challenge responses to peanuts during follow-up. CONCLUSIONS: The majority of children with clinical peanut hypersensitivity followed up for 5 years will have adverse reactions from accidental peanut exposure. Symptoms experienced during subsequent adverse peanut reactions may not be consistent with symptoms reported during initial reactions. Therefore proper education regarding peanut avoidance and treatment of adverse reactions is necessary in all cases of clinical peanut hypersensitivity. Young children who are allergic to peanuts can lose clinical hypersensitivity.

Allergens↗
PubMed2005

The prevalence of peanut sensitization and the association to pollen sensitization in a cohort of unselected adolescents--The Odense Adolescence Cohort Study on Atopic Diseases and Dermatitis (TOACS).

In the last decade an increased occurrence of peanut hypersensitivity and severe anaphylactic reactions to peanut have been reported. However, few prevalence studies have been performed in unselected populations. This study evaluated the point prevalence of peanut hypersensitivity in Danish adolescents. The point prevalence of peanut allergy confirmed by oral challenge was estimated to 0.5%. The number of adolescents sensitized to peanut by specific immunoglobulin E (IgE) (CAP FEIA) and skin prick test (SPT) were higher (5.8% resp. 3.4%). In adolescents without clinically relevant peanut sensitization most cases were sensitized to grass pollen and the IgE class for grass was higher than for peanut. A correlation between peanut and pollen (grass) sensitization is therefore plausible. Before a positive SPT or specific IgE measurement to peanut is considered clinically relevant in a patient, the case history should be evaluated together with examination for pollen sensitization.

Adolescent↗
PubMed1997

Identification and mutational analysis of the immunodominant IgE binding epitopes of the major peanut allergen Ara h 2.

A major peanut allergen, Ara h 2, is recognized by serum IgE from > 90% of patients with peanut hypersensitivity. Biochemical characterization of this allergen indicates that it is a glycoprotein of approximately 17.5 kDa. Using N-terminal amino acid sequence data from purified Ara h 2, oligonucleotide primers were synthesized and used to identify a clone (741 bp) from a peanut cDNA library. This clone was capable of encoding a 17.5-kDa protein with homology to the conglutin family of seed storage proteins. The major linear immunoglobulin E (IgE)-binding epitopes of this allergen were mapped using overlapping peptides synthesized on an activated cellulose membrane and pooled serum IgE from 15 peanut-sensitive patients. Ten IgE-binding epitopes were identified, distributed throughout the length of the Ara h 2 protein. Sixty-three percent of the amino acids represented in the epitopes were either polar uncharged or apolar residues. In an effort to determine which, if any, of the 10 epitopes were recognized by the majority of patients with peanut hypersensitivity, each set of 10 peptides was probed individually with serum IgE from 10 different patients. All of the patient sera tested recognized multiple epitopes. Three epitopes (aa27-36, aa57-66, and aa65-74) were recognized by all patients tested. In addition, these three peptides bound more IgE than all the other epitopes combined, indicating that they are the immunodominant epitopes of the Ara h 2 protein. Mutational analysis of the Ara h 2 epitopes indicate that single amino acid changes result in loss of IgE binding. Two epitopes in region aa57-74 contained the amino acid sequence DPYSP that appears to be necessary for IgE binding. These results may allow for the design of improved diagnostic and therapeutic approaches to peanut hypersensitivity.

2S Albumins, Plant↗
PubMed2005

The effect of the food matrix on in vivo immune responses to purified peanut allergens.

There is little knowledge about the factors that determine the allergenicity of food proteins. One aspect that remains to be elucidated is the effect of the food matrix on immune responses to food proteins. To study the intrinsic immunogenicity of allergens and the influence of the food matrix, purified peanut allergens (Ara h 1, Ara h 2, Ara h 3, or Ara h 6) and a whole peanut extract (PE) were tested in the popliteal lymph node assay (PLNA) and in an oral model of peanut hypersensitivity. In the PLNA, peanut proteins were injected into the hind footpad of BALB/c mice; in the oral exposure experiments C3H/HeOuJ mice were gavaged weekly with PE or allergens in the presence of cholera toxin (CT). Upon footpad injection, none of the allergens induced significant immune activation. In contrast, PE induced an increase in cell number, cytokine production, and activation of antigen-presenting cells. Furthermore, the presence of a food matrix enhanced the immune response to the individual allergens. Oral exposure to the purified allergens in the presence of CT induced specific IgE responses, irrespective of the presence of a food matrix. These results suggest that purified peanut allergens possess little intrinsic immune-stimulating capacity in contrast to a whole PE. Moreover, the data indicate that the food matrix can influence responses to individual proteins and, therefore, the food matrix must be taken into account when developing models for allergenic potential assessment.

2S Albumins, Plant↗
PubMed2002

Modification of peanut allergen Ara h 3: effects on IgE binding and T cell stimulation.

BACKGROUND: Peanut allergy is a major health concern due to the increased prevalence, potential severity, and chronicity of the reaction. The cDNA encoding a third peanut allergen, Ara h 3, has been previously cloned and characterized. Mutational analysis of the Ara h 3 IgE-binding epitopes with synthetic peptides revealed that single amino acid changes at critical residues could diminish IgE binding. METHODS: Specific oligonucleotides were used in polymerase chain reactions to modify the cDNA encoding Ara h 3 at critical IgE binding sites. Four point mutations were introduced into the Ara h 3 cDNA at codons encoding critical amino acids in epitopes 1, 2, 3 and 4. Recombinant modified proteins were used in SDS-PAGE/Western IgE immunoblot, SDS-PAGE/Western IgE immunoblot inhibition and T cell proliferation assays to determine the effects of these changes on in vitro clinical indicators of peanut hypersensitivity. RESULTS: Higher amounts of modified Ara h 3 were required to compete with the wild-type allergen for peanut-specific serum IgE. Immunoblot analysis with individual serum IgE from Ara-h-3-allergic patients showed that IgE binding to the modified protein decreased approximately 35-85% in comparison to IgE binding to wild-type Ara h 3. Also, the modified Ara h 3 retained the ability to stimulate T cell activation in PBMCs donated by Ara-h-3-allergic patients. CONCLUSIONS: The engineered hypoallergenic Ara h 3 variant displays two characteristics essential for recombinant allergen immunotherapy; it has a reduced binding capacity for serum IgE from peanut-hypersensitive patients and it can stimulate T-cell proliferation and activation.

Allergens↗
PubMed2000

A murine model of peanut anaphylaxis: T- and B-cell responses to a major peanut allergen mimic human responses.

BACKGROUND: Peanut allergy affects 0.6% of the US population. At the present time, allergen avoidance is the only therapeutic option. Animal models of food-induced anaphylaxis would facilitate attempts to design novel immunotherapeutic strategies for the treatment of peanut allergy. OBJECTIVE: The purpose of this study was to develop a murine model of IgE-mediated peanut hypersensitivity that closely mimics human peanut allergy. METHODS: C3H/HeJ mice sensitized orally with freshly ground whole peanut and cholera toxin as adjuvant were challenged orally 3 and 5 weeks later with crude peanut extract. Anaphylactic reactions were determined. T- and B-cell responses to Ara h 1 and Ara h 2, the major peanut allergens, were characterized by evaluating splenocyte proliferative responses and IgE antibody concentrations. Furthermore, IgE antibodies in the sera of patients with peanut allergy and mice were compared for antibody binding to Ara h 2 isoforms and allergenic epitopes. RESULTS: Peanut-specific IgE was induced by oral peanut sensitization, and hypersensitivity reactions were provoked by feeding peanut to sensitized mice. The symptoms were similar to those seen in human subjects. Ara h 1- and Ara h 2-specific antibodies were present in the sera of mice with peanut allergy. Furthermore, these Ara h 2-specific IgE antibodies bound the same Ara h 2 isoforms and major allergenic epitopes as antibodies in the sera of human subjects with peanut allergy. Splenocytes from mice with peanut allergy exhibited proliferative responses to Ara h 1 and Ara h 2. CONCLUSION: This murine model of peanut allergy mimics the clinical and immunologic characteristics of peanut allergy in human subjects and should be a useful tool for developing immunotherapeutic approaches for the treatment of peanut allergy.

2S Albumins, Plant↗
PubMed1994

Risks of milk formulas containing peanut oil contaminated with peanut allergens in infants with atopic dermatitis.

Four cases of infants with atopic dermatitis are reported. In all cases, a sensitization to peanut is demonstrated. Any ingestion of peanuts can be excluded, with the exception of a daily consumption of peanut oil, contained in milk formulas. Oral challenges with peanut oil induce a rash, and elimination of these brands is followed by the disappearance of eczematous lesions. The presence of residual allergenic proteins in peanut oil is thus suspected. Owing to the growing incidence of peanut hypersensitivity, the elimination of peanut oil from all milk formulas, food for babies, and ointments, seems to be highly advisable.

Allergens↗
PubMed2004

Peanut allergenicity.

OBJECTIVE: To provide the reader with a relevant review of the structure and allergenicity of the major peanut allergens, while also exploring predictors of clinical reactivity to peanuts, the natural history of peanut allergy, and novel therapeutic strategies for peanut hypersensitivity. DATA SOURCES: A PubMed search for the years 1980 to 2004 was performed using the following search terms: peanut allergy, food allergy, anaphylaxis, peanut allergen structure, and peanut immunotherapy. STUDY SELECTION: Articles highlighting major advances in the study of peanut allergy were selected for further review. RESULTS: Peanut allergy is the most serious of the hypersensitivity reactions to foods due to its persistence and high risk of severe anaphylaxis. The major peanut allergens and their associated immunodominant IgE-binding epitopes have been characterized. Definition of these allergens has lead to an increased understanding of the peanut-specific immunologic response and improved predictors of clinical reactivity to peanuts. An understanding of these mechanisms is vital for the eventual development of safe and effective immunotherapy for peanut allergic patients. Novel therapeutic and diagnostic approaches are being developed for patients with peanut hypersensitivity. CONCLUSIONS: Improved understanding of the molecular structure of the major peanut allergens and the peanut-specific immune response has lead to significant diagnostic and therapeutic advances in the study of peanut allergy.

Allergens↗
PubMed2004

Specific immunoglobulin E antibodies to peanut over time in relation to peanut intake, symptoms and age.

The clinical outcome of peanut allergy and some factors associated with development of peanut allergy remain unsolved. It has not been clarified to what extent peanut intake affects immunoglobulin (IgE) antibody formation in peanut sensitized individuals. The aim of the study was to investigate the development of peanut hypersensitivity in children and adolescents with specific IgE antibodies to peanut, using questionnaires and current serum tests and comparing it to information obtained 5-6 yr earlier, to investigate how peanut intake during this period related to subject age, IgE antibody levels and symptoms and to investigate what information this patient group was given at the time of diagnosis regarding avoidance of peanut related food. All patients with detectable peanut-specific IgE antibodies investigated during 1994-1996 deriving from two allergy laboratories in the western region of Sweden were traced and reinvestigated (n=132). A total of 111 subjects (63 with peanut allergy and 48 peanut sensitized) participated in the questionnaire. Eighty-six of them consented to be enrolled in a further interview and renewed testing of specific IgE antibody to peanut 5 yr later. All tests were done using the Pharmacia CAP system. Increased IgE antibody levels during follow-up was related to age; subjects 0-6 yr at initial test occasion were more likely to have higher IgE antibody class than the older individuals (p=0.018). Exposure to peanut during the study, i.e. 5-6 yr since diagnosis, did not seem to affect the result. During the follow-up period, 29 out of 86 (34%) increased their IgE antibody class. At the second test occasion the remaining subjects had similar (28%) or lowered (38%) levels of IgE antibodies. Exposure to peanut during follow-up was more common in subjects with IgE antibody class 1-3 compared to subjects with high value (> 3) at the initial test (p=0.003). Reported symptoms during follow-up were also more common in subjects with initially high IgE antibody value. Individuals with initially high IgE antibodies to peanut had been given more information about peanut allergy and cross-reacting allergens than other individuals. The subjects over 6 yr of age showed a decrease in peanut-specific IgE class over a 5-yr period. Together with the literature, our result suggest that follow-up and renewed testing is recommended, since there may be a change in IgE antibody classes and clinical sensitivity over time. Even in Sweden, with a low consumption of peanuts, the youngest individuals with peanut sensitization experienced a similar course of events that has been reported in other countries.

Age Factors↗
PubMed2005

Peanut-lupine antibody cross-reactivity is not associated to cross-allergenicity in peanut-sensitized mouse strains.

BACKGROUND: Peanut hypersensitivity is one of the most common food allergies and one of the most common causes of death by food anaphylaxis in children and adults. Cross-reactivity of peanut-specific antibody (Ab) with other legumes is frequently demonstrated but it still remains to be demonstrated whether these responses could lead to clinical signs of cross-allergenicity. OBJECTIVE: We sought to evaluate peanut-specific serum IgE and IgG1 antibody (Ab) responses and anaphylactic reaction in mice strains and to assess both cross-reactivity and cross-allergenicity of peanut and lupine. METHODS: Four mice strains (i.e., C3H, BALB/c, CBA and SJL) were sensitized to peanut by intraperitoneal (ip) injection of crude peanut protein extract with alum. Other groups were given oral peanut extract without adjuvant. Peanut-specific antibodies (Abs) and anaphylactic responses to peanut challenge were examined. RESULTS: The C3H, CBA (H-2(k)) and BALB/c (H2-(d)) mice exhibited high levels of peanut-specific serum IgE, IgG1 Ab responses after the intra-peritoneal sensitization. Only the two strains of mice in the H-2(k) background developed anaphylactic symptoms upon intra-peritoneal challenge with crude peanut protein extract. While cross-reactivity of peanut and lupine was confirmed by ELISA, no clinical symptom of cross-allergenicity was seen after challenge with lupine. Mice that were given oral peanut showed only increase in peanut-specific IgG2a, but no IgE or IgG1 Abs and failed to develop anaphylactic reactions following injection of either peanut or lupine protein. CONCLUSION: These results show that mice of different genetic backgrounds can be sensitized to peanut by ip injection to develop anti-peanut Abs that cross react with lupine. In addition, cross-allergenicity may not directly correlate with the presence of cross-reactive Abs since no clinical symptoms of cross-allergenicity was seen after ip challenge with lupine.

Allergens↗
PubMed2003

Persistent protective effect of heat-killed Escherichia coli producing "engineered," recombinant peanut proteins in a murine model of peanut allergy.

BACKGROUND: Peanut allergy (PNA) is a life-threatening food allergy for which there is no definitive treatment. OBJECTIVE: We investigated the long-term immunomodulatory effect of heat-killed Escherichia coli producing engineered (mutated) Ara h1, 2, and 3 (HKE-MP123) administered rectally (pr) in a murine model of PNA. METHODS: Peanut-allergic C3H/HeJ mice received 0.9 (low dose), 9 (medium dose), or 90 (high dose) microg HKE-MP123 pr, HKE-containing vector (HKE-V) alone, or vehicle alone (sham) weekly for 3 weeks. Mice were challenged 2 weeks later. A second and third challenge were performed at 4-week intervals. RESULTS: After the first challenge, all 3 HKE-MP123 and HKE-V-treated groups exhibited reduced symptom scores (P <.01,.01,.05,.05, respectively) compared with the sham-treated group. Interestingly, only the medium- and high-dose HKE-MP123-treated mice remained protected for up to 10 weeks after treatment accompanied by a significant reduction of plasma histamine levels compared with sham-treated mice (P <.05 and.01, respectively). IgE levels were significantly lower in all HKE-MP123-treated groups (P <.001), being most reduced in the high-dose HKE-MP123-treated group at the time of each challenge. IL-4, IL-13, IL-5, and IL-10 production by splenocytes of high-dose HKE-MP123-treated mice were significantly decreased (P <.01;.001,.001, and.001, respectively), and IFN-gamma and TGF-beta production were significantly increased (P <.001 and.01, respectively) compared with sham-treated mice at the time of the last challenge. CONCLUSIONS: Treatment with pr HKE-MP123 can induce long-term "downregulation" of peanut hypersensitivity, which might be secondary to decreased antigen-specific T(H)2 and increased T(H)1 and T regulatory cytokine production.

2S Albumins, Plant↗