Current developments in peanut allergy.

Kricia Palmer; Wesley Burks

doi:10.1097/01.all.0000225161.60274.31

Home/Archive/PubMed

PubMed · 16670515

Current developments in peanut allergy.

Kricia Palmer·Wesley Burks

View original source ↗Export metadata ↓

Abstract

PURPOSE OF REVIEW: Peanut allergy is among the most serious, life-threatening food sensitivities, and recent studies indicate increasing prevalence, particularly among children. Our objective is to highlight recent advances in the immunology and treatment of peanut allergy. RECENT FINDINGS: Peanut sensitization may be both a Th1- and Th2-driven process, and cytotoxic T-lymphocyte-associated antigen 4 (CTLA-4) may play a role in regulating the response intensity. Preliminary work shows that the food matrix is important in the immune response to peanut and that purified peanut allergens may have little intrinsic stimulatory capacity. Studies characterizing peanut allergens have revealed Ara h 1 and Ara h 2 as the most potent allergens, but Ara h 3 may be more allergenic than previously thought. There appears to be a relationship between the diversity of IgE-binding patterns and the severity of clinical symptoms. Multiple novel approaches to treatment are being investigated, which include traditional Chinese medicine, various forms of modified immunotherapy and the use of adjuvants in modified immunotherapy. SUMMARY: By understanding the immunologic response to peanut and the roles of the major peanut allergens, it may be possible to predict those at risk for severe reactions, prevent peanut sensitization and effectively treat those already sensitized.

Explore related subjects

Allergens Antibodies, Anti-Idiotypic Antigens, CD Antigens, Differentiation Arachis CTLA-4 Antigen Desensitization, Immunologic Humans Immunization Medicine, Chinese Traditional Peanut Hypersensitivity Vaccines, DNA Journal Article Review

Keep this discovery

Explore connections, maps & timelines

BibTeX RIS

Kricia Palmer, Wesley Burks. 2006. Current developments in peanut allergy.. https://doi.org/10.1097/01.all.0000225161.60274.31

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related citations

PubMed2007

Towards abolition of immunogenic structures in insect cells: characterization of a honey-bee (Apis mellifera) multi-gene family reveals both an allergy-related core alpha1,3-fucosyltransferase and the first insect Lewis-histo-blood-group-related antigen-synthesizing enzyme.

Glycoproteins from honey-bee (Apis mellifera), such as phospholipase A2 and hyaluronidase, are well-known major bee-venom allergens. They carry N-linked oligosaccharide structures with two types of alpha1,3-fucosylation: the modification by alpha1,3-fucose of the innermost core GlcNAc, which constitutes an epitope recognized by IgE from some bee-venom-allergic patients, and an antennal Lewis-like GalNAcbeta1,4(Fucalpha1,3)GlcNAc moiety. We now report the cloning and expression of two cDNAs encoding the relevant active alpha1,3-FucTs (alpha1,3-fucosyltransferases). The first sequence, closest to that of fruitfly (Drosophila melanogaster) FucTA, was found to be a core alpha1,3-FucT (EC 2.4.1.214), as judged by several enzyme and biochemical assays. The second cDNA encoded an enzyme, most related to Drosophila FucTC, that was shown to be capable of generating the Le(x) [Galbeta1-4(Fucalpha1-3)GlcNAc] epitope in vitro and is the first Lewis-type alpha1,3-FucT (EC 2.4.1.152) to be described in insects. The transcription levels of these two genes in various tissues were examined: FucTA was found to be predominantly expressed in the brain tissue and venom glands, whereas FucTC transcripts were detected at highest levels in venom and hypopharyngeal glands. Very low expression of a third homologue of unknown function, FucTB, was also observed in various tissues. The characterization of these honey-bee gene products not only accounts for the observed alpha1,3-fucosylation of bee-venom glycoproteins, but is expected to aid the identification and subsequent down-regulation of the FucTs in insect cell lines of biotechnological importance.

Allergens↗

PubMed2007

Animal models to test respiratory allergy of low molecular weight chemicals: a guidance.

At present, there are no widely applied or fully validated test methods to identify respiratory LMW allergens, i.e. compounds that are considered capable of inducing allergic asthma. Most tests have been investigated using strong respiratory allergens. Moreover, they are meant to detect the potential of a chemical to induce respiratory sensitisation at relatively high doses. Consequently, the sensitivity of the tests is not well-known, and they do not provide information on low doses such as generally found in occupational situations, and on threshold levels to be used in risk assessment. In addition, the various test methods use different application routes, i.e. intradermal, topical or inhalation exposure, and different parameters. Therefore standardised and validated dose-response test methods are urgently required in order to be able to identify respiratory allergens and to recommend safe exposure levels for consumers and workers. In the present paper, methods or testing strategies are described to detect respiratory sensitisation and/or allergy. Overall, assays that utilize only an induction phase may serve as indicators of respiratory sensitisation potential whereas assays that use both an induction and an elicitation or challenge phase may provide information on potency and presence of thresholds. The dermal route as sensitisation route has the advantage of the respiratory tract not being exposed to the allergen prior to challenge which facilitates the distinction between irritant and allergic effects.

Allergens↗

PubMed2007

Animal models for protein respiratory sensitizers.

Protein induced respiratory hypersensitivity, particularly atopic disease in general, and allergic asthma in particular, has increased dramatically over the last several decades in the US and other industrialized nations as a result of ill-defined changes in living conditions in modern western society. In addition, work-related asthma has become the most frequently diagnosed occupational respiratory illness. Animal models have demonstrated great utility in developing an understanding of the etiology and mechanisms of many diseases. A few models been developed as predictive models to identify a protein as an allergen or to characterize its potency. Here we describe animal models that have been used to investigate and identify protein respiratory sensitizers. In addition to prototypical experimental design, methods for exposure route, sample collection, and endpoint assessment are described. Some of the most relevant endpoints in assessing the potential for a given protein to induce atopic or allergic asthma respiratory hypersensitivity are the development of cytotropic antibodies (IgE, IgG1), eosinophil influx into the lung, and airway hyperresponsiveness to the sensitizing protein and/or to non-antigenic stimuli (Mch). The utility of technologies such as PCR and multiplexing assay systems is also described. These models and methods have been used to elucidate the potential for protein sources to induce allergy, identify environmental conditions (pollutants) to impact allergy responsiveness, and establish safe exposure limits. As an example, data are presented from an experiment designed to compare the allergenicity of a fungal biopesticide Metarhizium anisopliae (MACA) crude extract with the one of its components, conidia (CON) extract.

Allergens↗