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PubMed2004

Effect of roasting history and buffer composition on peanut protein extraction efficiency.

Peanut is a major allergenic food. Undeclared peanut (allergens) from mis-formulation or contamination during food processing pose a potential risk for sensitized individuals and must be avoided. Reliable detection and quantification methods for food allergens are necessary in order to ensure compliance with food labelling and to improve consumer protection. The extraction of proteins from allergenic foods and complex food products is an important step in any allergen detection method. In this study, the protein extraction efficiency of various buffers prepared in-house and some extraction buffers included in some commercial allergen enzyme-linked immunosorbent assay (ELISA) test kits for peanut determination in food products were tested. In addition, the effect of roasting history on the extractability of peanut protein was investigated by the biuret and the bicinchoninic acid (BCA) assays. Elevated roasting temperatures in food processing were found to have a major impact on protein extraction efficiency by reducing protein yields of oil and dry roasted peanuts by 50-75% and 75-80%, respectively, compared with the raw material. Extraction buffers operating in the higher pH range (pH 8-11) showed best yields.

Allergens↗
PubMed2005

Allergenic characteristics of a modified peanut allergen.

Attempts to treat peanut allergy using traditional methods of allergen desensitization are accompanied by a high risk of anaphylaxis. The aim of this study was to determine if modifications to the IgE-binding epitopes of a major peanut allergen would result in a safer immunotherapeutic agent for the treatment of peanut-allergic patients. IgE-binding epitopes on the Ara h 2 allergen were modified, and modified Ara h 2 (mAra h 2) protein was produced. Wild-type (wAra h 2) and mAra h 2 proteins were analyzed for their ability to interact with T-cells, their ability to bind IgE, and their ability to release mediators from a passively sensitized RBL-2H3 cell line. Multiple T-cell epitopes were identified on the major peanut allergen, Ara h 2. Ara h 2 amino acid regions 11-35, 86-125, and 121-155 contained the majority of peptides that interact with T-cells from most patients. The wAra h 2 and mAra h 2 proteins stimulated proliferation of T-cells from peanut-allergic patients to similar levels. In contrast, the mAra h 2 protein exhibited greatly reduced IgE-binding capacity compared to the wild-type allergen. In addition, the modified allergen released significantly lower amounts of beta-hexosaminidase, a marker for IgE-mediated RBL-2H3 degranulation, compared to the wild-type allergen.

2S Albumins, Plant↗
PubMed1988

Effects of dietary peanut oil on serum lipoprotein patterns of rats.

Oils prepared from two varieties of peanuts and from a hybrid corn having linoleic acid concentrations substantially different from the respective commercial oils were compared with commercial oils for their effects on serum lipids of weanling female rats. In the first experiment, serum lipid patterns appeared to reflect linoleic acid content of the dietary oil. However, with a longer feeding period in the second experiment, serum lipid patterns were determined by the plant source of the dietary oil rather than its linoleic acid content; all peanut oils differed from both corn oils in their physiological effects. Diets containing triglyceride, hydrocarbon and sterol fractions obtained by liquid chromatography of peanut and corn oils were fed to female rats. The data provide no evidence that the hydrocarbon or sterol fractions of peanut oil are responsible for its unusual atherogenicity when fed as the sole fat source or that similar fractions from corn oil are protective against the effects of peanut oil.

Animals↗
PubMed2004

Intradermal exposure of BALB/c strain mice to peanut protein elicits a type 2 cytokine response.

There is a growing need for the development of methods to characterize the allergenic properties of novel proteins, particularly those expressed by transgenic crop plants. Hence, there is considerable interest in the development of suitable animal models for this purpose. The production of specific IgE antibody has been reported following sensitization with food allergen via oral or systemic (intraperitoneal) routes of exposure. We have characterized cytokine profiles induced by intradermal treatment of BALB/c strain mice with a purified peanut allergen, Arachis hypogea lectin. Mice were exposed to peanut lectin by intradermal administration and the cytokine responses in the lymph node draining the site of exposure analyzed at the secreted protein level by enyzme-linked immunosorbent assay (ELISA) and cytokine mRNA level by ribonuclease protection assay (RPA). Exposure to peanut lectin, under conditions that induced robust IgE antibody titers, was found to be associated with a T helper 2 (Th2)-type cytokine expression profile at both the mRNA and secreted protein levels. Culture of naïve lymph node cells with peanut lectin failed to stimulate marked proliferation or cytokine production, confirming this protein is not mitogenic for mouse lymphocytes. Furthermore, the expression of Th2 cytokines was associated with the effector/memory CD62L- cell population. Similar treatment with a non-allergenic protein, potato acid phosphatase, failed to induce Th2 cytokine expression. These data demonstrate that exposure of mice to peanut allergen results in the selective stimulation of a Th2-type response.

Animals↗
PubMed2004

Should beta-blockers be given to patients with heart disease and peanut-induced anaphylaxis? A decision analysis.

BACKGROUND: Beta-blocker therapy postmyocardial infarction is generally recommended because it reduces mortality. However, beta-blockers may increase anaphylaxis mortality in the growing population of patients with peanut-induced anaphylaxis. OBJECTIVE: We sought to assess the risks and benefits of beta-blocker therapy among patients with peanut allergy and heart disease. METHODS: We created a Markov model for patients with heart disease at risk for peanut-induced anaphylaxis to compare life expectancy with the following strategies: (1) beta-blocker and (2) no beta-blocker. Meta-analysis and a literature review were used to estimate model parameters. We performed sensitivity analysis to explore parameter uncertainty. RESULTS: For peanut-allergic patients who are postmyocardial infarction or who have congestive heart failure, the heart disease benefit of beta-blockers outweighs the increased likelihood of dying from anaphylaxis, increasing life expectancy by 9.4 and 17.4 months, respectively. Beta-blocker was preferred unless (1) the annual rate of moderate to severe anaphylaxis exceeded 6.0% for postmyocardial infarction and 15% for congestive heart failure patients; (2) beta-blocker therapy increased the incidence of moderate to severe anaphylaxis >2.5-fold for postmyocardial infarction and >5.8-fold for congestive heart failure patients; (3) anaphylaxis case fatality exceeded 6.5% postmyocardial infarction; or (4) beta-blocker therapy increased anaphylaxis case fatality >25-fold postmyocardial infarction. CONCLUSION: Our results suggest that for patients postmyocardial infarction or with congestive heart failure who are at risk for peanut-induced anaphylaxis, beta-blocker use should still improve survival. However, the epidemiology of anaphylaxis and effects of beta-blocker therapy on anaphylaxis incidence and mortality require further study.

Adrenergic beta-Antagonists↗
PubMed2002

[Peanut allergy].

Clinical manifestations of peanut allergy are miscellanous extending from simple itching to anaphylactic shock. They may appear early in life. The diagnosis relies upon history, prick tests, specific IgE dosage, and if necessary oral challenge test. Most often peanut allergy is longstanding requiring a complete exclusion of peanut from the food. In addition peanut oil being a frequent hidden allergen, it is recommended that any patient with recognized peanut allergy carries a first aid kit to be used in case of allergic accident.

Age Factors↗
PubMed2005

Identification of the basic subunit of Ara h 3 as the major allergen in a group of children allergic to peanuts.

BACKGROUND: Several proteins have been identified as peanut allergens; among them, Ara h 1 (7S globulin) and Ara h 2 (2S globulin) are usually considered the major allergens. OBJECTIVE: To identify the major allergens in a group of children selected for their specific pattern of immunoreactivity. METHODS: We identified the dominant allergen by using (1) amino acid sequencing of the bands that show the strongest IgE immunoreactivity in 1-dimensional electrophoresis and immunoblotting and (2) specific animal IgGs raised against the dominant immunoreactive band to pinpoint the allergen(s) in peanut proteins separated by 2-dimensional electrophoresis and immunoblotting. To confirm these data, we further examined the peanut proteome using serum samples from the children with the unusual immunoreactivity. RESULTS: We found a group of children with marked peanut allergy who are specifically sensitized to the basic subunit of Ara h 3 (11S globulin family). CONCLUSION: That the dominant immunoreactivity in these patients is in a basic subunit of Ara h 3 was unexpected, 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.

Allergens↗
PubMed2002

Peanut roots as a source of resveratrol.

A potent antioxidant, resveratrol (3,4',5-trihydroxystilbene), was extracted using 80% methanol from peanut roots (Arachis hypogaea L.), isolated with a solid-phase extraction column, purified by a semipreparative HPLC, and identified with 1H NMR and MS. The highest and lowest resveratrol contents in the peanut roots of 2000 fall and 2001 spring crops were 1.330 and 0.130 mg/g and 0.063 and 0.015 mg/g, respectively. When the dehydrated peanut root powders of spring and fall crops were combined and cooked with pork-fat patties (1%, w/w) and the separated oils were stored at 60 degrees C for conjugated diene hydroperoxide (CDHP) determination, CDHP contents of the control oils increased after 3 days of storage, whereas the contents in the peanut root-treated oils of spring and fall crops did not increase after 9 and 15 days of storage, respectively. It is of merit to find that peanut roots, usually left in the field as agricultural waste, contain resveratrol and bear potent antioxidative activity.

Antioxidants↗
PubMed2002

Selection of alternative genetic sources of large-seed size in Virginia-type peanut: evaluation of sensory, composition, and agronomic characteristics.

Jenkins Jumbo, the ancestral source of large-seed size in the Virginia market type (Arachis hypogaea L.), has been shown to have a deleterious effect on flavor of peanut. The pervasiveness of Jenkins Jumbo in the ancestry of large-seeded germplasm contributes to the generally less intense roasted peanut flavor of U.S. cultivars of the Virginia market type. As a remedy to this problem, alternative sources of large-seed size were sought. Nine large-seeded selections, with NC 7 and Florunner as checks, were tested in replicated trials in North Carolina and Florida from 1996 to 1998. Pod yield, grade, weight of 100 seeds, and oil, sugar, and starch contents were measured. A descriptive sensory panel evaluated flavor attributes of a roasted sound mature kernel (SMK) sample from each plot. NC 7 scored low for sweet sensory attribute, high for bitter, and median for roasted peanut. UF714021, a multiline incorporating the Altika cultivar with several sister lines, had the best flavor profile of the large-seeded selections, but it did not have particularly large seeds relative to NC 7. The largest seeded selections were X90037 and X90053, both derived from Japan Jumbo. Flavor scores for X90037 were similar to those for NC 7 for roasted peanut (3.0 vs 2.9 flavor intensity units, fiu) and sweet (2.7 vs 2.6 fiu) but worse than NC 7 for bitter (3.3 vs 3.7 fiu) and astringent (3.5 vs 3.7 fiu). X90053 had intermediate values for roasted peanut and astringent, high value for sweet, and low for bitter. Other lines that had or were likely to have Jenkins Jumbo as a recent ancestor were generally poor in roasted flavor, supporting the hypothesis that ancestry from Jenkins Jumbo imparts poor flavor characteristics. With the exception of the unexpected relationship between astringent attribute and extra large kernel (ELK) content (r = 0.82, P < 0.01), there were no significant correlations between sensory attributes and the important agronomic traits: yield, meat, and ELK content. Among the nine large-seeded lines tested in this study, three appear to have greater potential for use as parents: 86x45B-10-1-2-2-b2-B, UF714021, and X90053.

Agriculture↗
PubMed2003

Combined skin prick and patch testing enhances identification of peanut-allergic patients with atopic dermatitis.

BACKGROUND: Food atopy patch tests (APTs) are considered a useful tool for the diagnosis of food allergy. Hypersensitivity to peanuts has not been investigated by means of APTs so far. METHODS: APTs and skin prick tests (SPTs) with peanuts were performed in 136 atopic dermatitis (AD) patients. Relevance of positive and negative responses to these tests was assessed by repeated open challenges with peanuts. RESULTS: Nine percent of our AD patients reacted to the challenge. Positive responses to APTs were recorded in 19% of the patients, whereas in 12% positive SPTs were observed. APTs were more frequently positive in subjects with eczematous responses after challenge with respect to those with urticarial reactions. SPT reactivity proved to be higher in patients above 12 years of age, whereas APT positivity was more frequent in children under 6 years. APT sensitivity proved significantly higher than SPT sensitivity, in particular in children under 12 years of age. On the contrary, SPT specificity and positive predictive value were significantly higher with respect to those of APT in the age group of subjects under 6 years of age. CONCLUSIONS: Our data suggest that APTs with peanuts may represent a useful integration to standard testing modalities employed for the diagnosis of peanut allergy in AD patients.

Adolescent↗
PubMed2004

Sensory testing of recipes masking peanut or hazelnut for double-blind placebo-controlled food challenges.

BACKGROUND: In a double-blind placebo-controlled food challenge (DBPCFC), it is necessary that recipes comprising the allergen cannot be distinguished from placebo. AIMS OF THE STUDY: We investigated whether the method of paired comparisons, a sensory difference test, could be used to test the suitability of recipes for a DBPCFC. METHODS: We used two recipes, each with three concentrations of peanut or hazelnut flour. The recipe for peanut consisted of mashed potatoes with 2.7, 8.9, or 26.8 mg of peanut flour, and the recipe for hazelnut of oatmeal porridge with 74, 247, or 742 mg of hazelnut flour. Corresponding amounts of protein in the provided 15 g portions of each recipe were 0.7, 2.3, and 6.8 mg for peanut, and 11.6, 39, and 117 mg for hazelnut, respectively. Recipes were offered together with a placebo, and evaluated on sensory features by 81 healthy volunteers. RESULTS: The sensory test was easy to perform. Volunteers were not able to detect peanut flour in mashed potatoes, but they recognized hazelnut flour in oatmeal porridge on visual features. CONCLUSIONS: Sensory testing by means of the method of paired comparisons is a useful method to evaluate masking of foods for DBPCFC.

Adult↗
PubMed2002

A comparison of commercially available peanut ELISA test kits on the analysis of samples of dark and milk chocolate.

Reactions to peanut proteins by certain sensitive members of the population can result in dramatic and potentially catastrophic consequences. While peanut is not the only food known to cause allergies, it is the one that is most closely monitored. To address concerns related to peanut in food products, four commercial test kits have been developed to quantitatively analyze for peanut protein in finished products. This manuscript describes a study undertaken to compare these kits on reference samples of dark and milk chocolate containing known amounts of peanut. The results are mixed with the data suggesting that all kits were suitable for qualitative screening but were not suitable for general quantitative assays.

Cacao↗
PubMed1992

Peanut lectin: a mitogen for normal human colonic epithelium and human HT29 colorectal cancer cells.

BACKGROUND: The protein peanut agglutinin (PNA) is a galactose-binding lectin whose receptor, the Thomsen-Friedenreich (TF) blood-group antigen, shows increased expression in hyperplastic and neoplastic colonic epithelium. PURPOSE: Our hypothesis was that, under these conditions, increased lectin receptors could interact with dietary lectins, which would act as tumor promoters by stimulating cell proliferation. This study was designed to confirm whether active PNA is recoverable from feces after ingestion of peanuts and to assess the mitogenic effect of PNA on proliferation of epithelial cells in the colon. METHODS: Peanut lectin was extracted from feces by lactose-agarose affinity chromatography and was assayed for hemagglutinating activity. Cultured explants of histologically normal biopsy specimens of colonic mucosa from 31 patients were examined. Crypt cell production rate and incorporation of [3H]N-acetylglucosamine into mucin were assessed as indicators of proliferative and metabolic responses to PNA. In addition, we evaluated the separate and combined effects of PNA and epidermal growth factor (EGF) on cell proliferation in human HT29 colorectal cancer cells, by using tritiated thymidine incorporation and cell counts. RESULTS: Peanut lectin extracted from feces showed hemagglutinating activity toward desialylated red blood cells similar to that of a lectin preparation extracted from raw peanuts. Evaluation of biopsy specimens of normal colonic mucosa demonstrated that PNA at a concentration of 25 micrograms/mL caused statistically significant increases in crypt cell production (31% [mean] +/- 5% [SD]; P = .00005) and mucus synthesis (77% +/- 12%; P less than .000001). At 7.5-100 micrograms/mL, PNA was mitogenic for the HT29 colorectal cancer cell line. At 25 micrograms/mL, PNA alone produced a statistically significant increase in thymidine incorporation (44% [mean] +/- 3.7% [SD]; P = .002). For PNA in combination with EGF at 100 pg/mL, the increase was significantly greater (222% +/- 11.2%) than that for EGF alone (57% +/- 5%; P = .003). CONCLUSIONS: These results suggest that expression of the PNA receptor, TF antigen, by hyperplastic or neoplastic colonic epithelium may affect cell proliferation. IMPLICATIONS: It is possible that dietary lectins such as PNA, which bind to the TF antigen, promote cell proliferation and thus cancerous growth, while galactose-containing vegetable fiber would inhibit this effect by competing for binding by these lectins.

Arachis↗
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↗
PubMed1999

Structures of the complexes of peanut lectin with methyl-beta-galactose and N-acetyllactosamine and a comparative study of carbohydrate binding in Gal/GalNAc-specific legume lectins.

The crystal structures of complexes of peanut lectin with methyl-beta-galactose and N-acetyllactosamine have been determined at 2.8 and 2.7 A, respectively. These, and the complexes involving lactose and the T-antigenic disaccharide reported previously, permit a detailed characterization of peanut-lectin-carbohydrate association and the role of water molecules therein. The water molecules in the combining site are substantially conserved in the four complexes. The role of interacting sugar hydroxyl groups, when absent, are often mimicked by ordered water molecules not only at the primary combining site, but also at the site of the second sugar ring. The similarity of peanut-lectin-sugar interactions with those in other galactose/N-acetylgalactosamine-specific lectins also extend to a substantial degree to water bridges. The comparative study provides a structural explanation for the exclusive specificity of peanut lectin for galactose at the monosaccharide level, compared with that of the other lectins for galactose as well as N-acetylgalactosamine. The complexes also provide a qualitative structural rationale for differences in the strengths of binding of peanut lectin to different sugars.

Amino Sugars↗
PubMed2005

Resolution of peanut allergy following bone marrow transplantation for primary immunodeficiency.

Peanut allergy is a severe and life-threatening form of food allergy. Treatments are being developed but the mainstays of current management remain avoidance of peanut and appropriate use of rescue medication. We report the case of a boy with peanut allergy who required a bone marrow transplant (BMT) for combined immunodeficiency. A food challenge, 2 years after transplant, showed that his peanut allergy had resolved. Allergic disorders constitute a form of immune deviation and while we do not advocate BMT as a treatment for peanut allergy, we believe this case provides an insight into the basic mechanisms involved in food allergy.

Bone Marrow Transplantation↗
PubMed2025

Functional analysis of a GWAS pleiotropic hotspot suggests an auxin biosynthesis gene (AhPDS1), regulating pod development in peanut (Arachis hypogaea L.).

Peanut productivity and quality improvement rely on understanding the genetic factors influencing pod and seed size. This study aims to identify genetic factors and regulatory mechanisms influencing pod and seed size in peanuts. Herein, a genome-wide association study (GWAS) was conducted using 390 accessions from 15 peanut growing regions to analyze pod and seed traits across multiple planting seasons. A significant phenotypic variation was observed, with broad-sense heritability ranging from 53.6 to 85.4%. Strong correlations between pod and seed traits further suggest potential for co-selection in breeding efforts. A pleiotropic hotspot on chromosome B06 was strongly associated with six pod and seed traits. A peanut pod size regulator AhPDS1 (PODSIZE-1, Ahy_B06g085516) homolog of Arabidopsis thaliana YUCCA4 (AtYUC4, AT5G11320), involved in auxin biosynthesis, was selected as a candidate regulating pod and seed size. Quantitative reverse transcriptase-polymerase chain reaction (qRT-PCR) confirmed higher AhPDS1 expression in large pod as compared with the small pod genotypes. Subcellular localization showed AhPDS1 to be predominantly cytoplasmic, and GUS reporter assays indicated widespread expression in roots, stems, leaves, flowers, and pods, suggesting a broad functional role. Further overexpression of AhPDS1 in Arabidopsis and rice enhanced pod, seed, and grain sizes via the indole-3-pyruvic acid pathway in transgene lines. These findings highlight AhPDS1 as a potential target for peanut molecular breeding, offering opportunities to enhance pod size via auxin biosynthesis and support sustainable crop improvement.

Arachis↗
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↗