Publications by authors named "Burks A"

Mammalian Toll-like receptors (TLRs) recognize microbial pathogen-associated molecular patterns and are critical for innate immunity against microbial infection. Diacylglycerol (DAG) kinases (DGKs) regulate the intracellular levels of two important second messengers involved in signaling from many surface receptors by converting DAG to phosphatidic acid (PA). We demonstrate that the zeta isoform of the DGK family (DGKzeta) is expressed in macrophages (Mphi) and dendritic cells.

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Background: There is no current active treatment for food allergy. Traditional injection immunotherapy has been proved unsafe, and thus there is a need for other forms of immunotherapy.

Objective: The purpose was to study the safety and immunologic effects of egg oral immunotherapy (OIT).

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Before a novel protein can be used in foods, its potential allergenicity must be assessed. In this study, healthy volunteers consumed ice structuring protein (ISP) Type III preparation or a control material 5 days a week for a total of 8 weeks. General measures of health were recorded during the study, and the immunogenicity of the protein was assessed by monitoring the levels of IgG and IgE antibodies specific for ISP Type III.

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Nonmammalian glycan structures from helminths act as Th2 adjuvants. Some of these structures are also common on plant glycoproteins. We hypothesized that glycan structures present on peanut glycoallergens act as Th2 adjuvants.

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X-linked agammaglobulinemia (XLA) is a primary immunodeficiency caused by mutations in the gene for Bruton tyrosine kinase (BTK) that result in the deficient development of B lymphocytes and hypogammaglobulinemia. Because the disorder is uncommon, no single institution has had sufficient numbers of patients to develop a comprehensive clinical picture of the disorder. Accordingly, a national registry of United States residents with XLA was established in 1999 to provide an updated clinical view of the disorder in a large cohort of patients.

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Background: Current diagnosis of peanut allergy relies on natural extracts that lack standardization. Recombinant DNA technology allows production of pure biochemically characterized proteins. Their usefulness for peanut allergy diagnosis is not established.

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A significant proportion of the population is either affected by or concerned about food allergy. Our knowledge about food allergens and how they stimulate the immune system has increased dramatically over the past decade. However, reasons for the increased prevalence of food allergy are not clear.

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Omalizumab, a recombinant humanized monoclonal antibody against immunoglobulin (Ig)E, represents a unique therapeutic approach for the treatment of allergic diseases. This agent acts as a neutralizing antibody by binding IgE at the same site as the high-affinity receptor. Subsequently, IgE is prevented from sensitizing cells bearing high-affinity receptors.

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To assess the relative potency of the major peanut allergens, Ara h 1 and Ara h 2, we examined the relative ability of purified proteins to bind IgE on immunoblots, to cross-link allergen specific IgE in an in vitro assay of degranulation based on RBL SX-38 cells, and to bind IgE in the ImmunoCap assay. Sera from 12 highly sensitive, peanut allergic patients were studied in all assays. IgE immunoblots with crude peanut extracts showed binding of IgE to multiple bands including the 63 kDa and 17-19 kDa bands that contain Ara h 1 and Ara h 2, respectively.

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Food allergic reactions have generated increasing concern in the United States, with approximately one fourth of American households altering their dietary habits because a member of the family is perceived to suffer from food allergies. IgE-mediated (type I) hypersensitivity accounts for most well-characterized food allergic reactions, although non-IgE-mediated immune mechanisms are believed to be responsible for a variety of hypersensitivity disorders. This article examines adverse food reactions that are IgE-mediated, non-IgE-mediated, and those entities that have characteristics of both.

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Allergies to peanuts are becoming an increasingly important health problem as a result of the persistence and severity of the reaction in allergic individuals. Because no treatment currently is available, avoidance is the only option for peanut-allergic individuals. Avoidance of an abundant and often disguised food such as peanuts, however, is very difficult; therefore, competitive inhibition ELISAs were developed to detect and quantitate each of the major peanut allergens, Ara h 1 and Ara h 2.

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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.

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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.

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Peanut allergenicity.

Ann Allergy Asthma Immunol

November 2004

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.

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Background: Although peanut allergy may recur, the frequency with which this occurs is unknown.

Objective: The goals of this study were to determine the rate of peanut allergy recurrence, identify risk factors for recurrent peanut allergy, and develop specific recommendations for the treatment of patients with resolved peanut allergy.

Methods: Children who outgrew peanut allergy were evaluated with questionnaires, skin tests, and peanut-specific IgE levels.

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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.

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Background: While the ingestion of small amounts of an offending food can elicit adverse reactions in individuals with IgE-mediated food allergies, little information is known regarding these threshold doses for specific allergenic foods. While low-dose challenge trials have been conducted on an appreciable number of allergic individuals, a variety of different clinical protocols were used making the estimation of the threshold dose very difficult.

Objective: A roundtable conference was convened to develop a consensus clinical protocol for low-dose challenge trials for the estimation of threshold doses for specific allergenic foods.

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Background: IgE epitope mapping of food allergens is a prerequisite for engineering hypoallergenic immunotherapeutic agents and might reveal basic information regarding a patient's immune response. Mapping of large numbers of epitopes by using individual patient sera has been impractical with current techniques.

Objective: We sought to develop a peptide microarray-based immunoassay to map peanut epitopes by using microliter quantities of serum.

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Animal models of food allergy.

Curr Opin Allergy Clin Immunol

December 2002

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.

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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.

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Background: It was once thought that peanut allergy is a lifelong problem. We previously reported that about 20% of children outgrow their peanut allergy and that more than 60% of patients with a peanut-IgE level of 5 or less passed an oral challenge.

Objective: The goal of this study was to further describe the natural progression of peanut allergy by reviewing patients who have undergone oral peanut challenges since the previous study.

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Background: Pesticide exposure has been suggested as one causal factor for the rise in asthma prevalence. The goal of this investigation was to determine the effect of pesticide exposure on respiratory symptoms and lung function in workers with occupational exposure to pesticides.

Methods: A prospective, case-controlled study was conducted among pesticide aviators (AV) and community controls (Con).

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