Adsorption of peanut (Arachis hypogaea, Leguminosae) proteins by activated charcoal.

The binding of peanut protein allergens to activated charcoal (AC), used medically for gastric decontamination following the ingestion of toxic substances, was investigated for potential clinical application. Crude peanut extract (CPE) or purified peanut protein allergens Ara h 1 and 2 were co-incubated with AC under a variety of conditions followed by centrifugation to remove the AC and adsorbed protein. The resulting supernatant solution was analyzed for unadsorbed protein by gel electrophoresis and quantitative protein assay.

Diet regulates the development of gut-associated lymphoid tissue in neonatal piglets.

Background: Controversy exists concerning diet-induced changes to gut epithelia and immunocytes that occur during weaning. Furthermore, studies on dietary effects on the development of the neonatal immune system, especially gut-associated lymphoid tissue (GALT), are lacking.

Objective: The purpose of this study was to investigate growth and development, intestinal morphology, and GALT immune maturation in sow-reared littermates in comparison with early-weaned piglets fed a casein-based liquid diet.

Comparison of physiological and in vitro porcine gastric fluid digestion.

Background: In previous studies, the major peanut allergen Ara h 1 was digested in vitro using pepsin and porcine gastric fluid. The results suggested that in vivo gastric digestion of allergen protein can be modeled accurately by peptic hydrolysis in vitro. In the current investigation, studies were designed to follow the gastrointestinal (GI) digestion of peanut allergens under true physiological conditions.

Intralesional immunotherapy of warts with mumps, Candida, and Trichophyton skin test antigens: a single-blinded, randomized, and controlled trial.

Background: Warts occur commonly in humans. Destructive modalities are generally the first physician-administered therapy. Other treatment options include immunotherapy.

Sensitization and allergic response and intervention therapy in animal models.

A review is presented of 3 murine models and a swine neonatal model used to investigate immunotherapeutic options. In Model 1, mutation of linear IgE-binding epitopes of Ara h 1 for the preparation of a hypoallergenic Ara h 1 is discussed with respect to expression in transgenic tobacco plants and correct folding following expression in the pET16b construct. In Model 2, the mutations of Ara h 1 were assessed for use as an immunotherapeutic agent.

Peanut protein allergens: the effect of roasting on solubility and allergenicity.

Background: A contributing factor to food allergen stability is heat resistance. Peanut allergens in particular are resistant to heat, which results in their decreased solubility upon routine extraction and may have a profound influence on their continued presence in the digestive tract. Although there have been a number of studies characterizing soluble extracts of raw and roasted proteins, the relative solubility of the insoluble material following routine extraction for residual allergen characterization has not been investigated.

Soy immunotherapy for peanut-allergic mice: modulation of the peanut-allergic response.

Background: Allergen-specific immunotherapy (IT) is an effective therapeutic modality to prevent further anaphylactic episodes in patients with insect sting hypersensitivity and is being investigated for peanut allergy. So far, peanut-specific IT has been unsuccessful because of the side effects of therapy. Soybean seed storage proteins share significant homology with the respective peanut allergens.

Peanut protein allergens: gastric digestion is carried out exclusively by pepsin.

Background: A major characteristic of many food allergens, including Ara h 1, a major peanut allergen, is their resistance to gastric digestion. One estimate of the allergenic potential of a possible protein allergen is its stability under simulated gastric conditions.

Objective: Because the rate and extent of digestion of allergenic proteins will affect the severity of any subsequent allergic response, it is important to correlate protein allergen digestion in simulated gastric fluid with that in actual gastric fluid.

Diet and the development of atopic disease.

Purpose Of Review: The present review addresses the current literature regarding the impact of diet and the development of atopic disease. A search of the literature was carried out covering the following topics: diet and nutrition combined with immediate hypersensitivity, atopy, atopic disease, atopic dermatitis, and food allergy.

Recent Findings: The search results identified a significant contribution in the form of reviews considering this important topic, which ultimately led to the author's recommendation of these reviews to impress upon readers the impact of the atopy triad: atopic dermatitis to allergic rhinitis and asthma.

Animal models of food allergy.

Purpose Of Review: The focus of this review will be on recent animal models of food allergy. Animal models are being used to investigate underlying mechanisms of IgE-mediated disease and for prophylactic/intervention therapies to treat allergic disease.

Recent Findings: Considerable advances have been made in the dosage and use of sensitization routes with and without adjuvant and determinations of the pathophysiology of food allergy in murine, dog and swine food allergy models.

Food biotechnology: is this good or bad? Implications to allergic diseases.

Background: Food biotechnology represents advancement in the traditional interspecies and intergeneric breeding methods for improving food supplies worldwide. With respect to safety, foods developed through biotechnology techniques represent one of the most extensively reviewed agricultural advancements in history.

Objective: To review the relevant issues with respect to foods from genetically modified crops and allergenicity.

Assessment of protein allergenicity on the basis of immune reactivity: animal models.

Because of the public concern surrounding the issue of the safety of genetically modified organisms, it is critical to have appropriate methodologies to aid investigators in identifying potential hazards associated with consumption of foods produced with these materials. A recent panel of experts convened by the Food and Agriculture Organization and World Health Organization suggested there is scientific evidence that using data from animal studies will contribute important information regarding the allergenicity of foods derived from biotechnology. This view has given further impetus to the development of suitable animal models for allergenicity assessment.

Genetic modification removes an immunodominant allergen from soybean.

The increasing use of soybean (Glycine max) products in processed foods poses a potential threat to soybean-sensitive food-allergic individuals. In vitro assays on soybean seed proteins with sera from soybean-sensitive individuals have immunoglobulin E reactivity to abundant storage proteins and a few less-abundant seed proteins. One of these low abundance proteins, Gly m Bd 30 K, also referred to as P34, is in fact a major (i.

Workshop overview: approaches to the assessment of the allergenic potential of food from genetically modified crops.

There is a need to assess the safety of foods deriving from genetically modified (GM) crops, including the allergenic potential of novel gene products. Presently, there is no single in vitro or in vivo model that has been validated for the identification or characterization of potential food allergens. Instead, the evaluation focuses on risk factors such as source of the gene (i.

Monitoring peanut allergen in food products by measuring Ara h 1.

Background: Peanut allergy is an important health problem in the United States, affecting approximately 0.6% of children. Inadvertent exposure to peanut is a risk factor for life-threatening food-induced anaphylaxis.

Nonmurine animal models of food allergy.

Food allergy can present as immediate hypersensitivity [manifestations mediated by immunoglobulin (Ig)E], delayed-type hypersensitivity (reactions associated with specific T lymphocytes), and inflammatory reactions caused by immune complexes. For reasons of ethics and efficacy, investigations in humans to determine sensitization and allergic responses of IgE production to innocuous food proteins are not feasible. Therefore, animal models are used a) to bypass the innate tendency to develop tolerance to food proteins and induce specific IgE antibody of sufficient avidity/affinity to cause sensitization and upon reexposure to induce an allergic response, b) to predict allergenicity of novel proteins using characteristics of known food allergens, and c) to treat food allergy by using immunotherapeutic strategies to alleviate life-threatening reactions.

IgE reactivity of tandem repeats derived from cockroach allergen, Bla g 1.

Sensitization to cockroach allergens is associated with the development of asthma. Bla g 1 is a German cockroach allergen that shows allergenic cross-reactivity with American cockroach allergen, Per a 1, and has a molecular structure composed of multiple tandem amino-acid repeats. Two consecutive repeats are not identical but form a duplex that constitutes a basic molecular unit of Bla g 1.

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.

Food allergy animal models: an overview.

Specific food allergy is characterized by sensitization to innocuous food proteins with production of allergen-specific IgE that binds to receptors on basophils and mast cells. Upon recurrent exposure to the same allergen, an allergic response is induced by mediator release following cross-linking of cell-bound allergen-specific IgE. The determination of what makes an innocuous food protein an allergen in predisposed individuals is unknown; however, mechanistic and protein allergen predictive models are being actively investigated in a number of animal models.

Biotechnology and food allergy.

The production of genetically modified foods for an increasingly informed and selective consumer requires the coordinated activities of both the companies developing the transgenic food and regulatory authorities to ensure that these foods are at least as safe as the traditional foods they are supplementing in the diet. Although the size and complexity of the food sector ensures that no single player can control the process from seed production through farming and processing to final products marketed in a retail outlet, checks and balances are in place to ensure that transgenic foods will provide a convenient, wholesome, tasty, safe, affordable food source. Ultimately, it is the responsibility of companies developing the genetically modified food to provide relevant data to regulatory agencies, such as the US Department of Agriculture, Environmental Protection Agency, and Food and Drug Administration, to confirm that the transgenic product is reasonably safe for the consumer, as zero risk from allergen sensitization is nonexistent.

A neonatal swine model for peanut allergy.

Background: Peanut allergy represents a significant health threat in the United States. The factors contributing to the severity of the allergic response and the immunopathogenic mechanisms underlying peanut allergy remain to be completely characterized. As yet, no animal model has been developed that will completely mimic the physical, immunologic, and histologic features of food allergy.