Nomenclature and structural biology of allergens

Christian Doppler Laboratory for Allergy Diagnosis and Therapy, University of Salzburg, Salzburg, Salzburg, Austria
Journal of Allergy and Clinical Immunology (Impact Factor: 11.48). 03/2007; 119(2):414-20. DOI: 10.1016/j.jaci.2006.11.001
Source: PubMed


Purified allergens are named using the systematic nomenclature of the Allergen Nomenclature Sub-Committee of the World Health Organization and International Union of Immunological Societies. The system uses abbreviated Linnean genus and species names and an Arabic number to indicate the chronology of allergen purification. Most major allergens from mites, animal dander, pollens, insects, and foods have been cloned, and more than 40 three-dimensional allergen structures are in the Protein Database. Allergens are derived from proteins with a variety of biologic functions, including proteases, ligand-binding proteins, structural proteins, pathogenesis-related proteins, lipid transfer proteins, profilins, and calcium-binding proteins. Biologic function, such as the proteolytic enzyme allergens of dust mites, might directly influence the development of IgE responses and might initiate inflammatory responses in the lung that are associated with asthma. Intrinsic structural or biologic properties might also influence the extent to which allergens persist in indoor and outdoor environments or retain their allergenicity in the digestive tract. Analyses of the protein family database suggest that the universe of allergens comprises more than 120 distinct protein families. Structural biology and proteomics define recombinant allergen targets for diagnostic and therapeutic purposes and identify motifs, patterns, and structures of immunologic significance.

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Available from: Martin D Chapman
    • "Isoallergen Cor a 1.04 comprise four variants or isoforms (Cor a 1.0401-Cor a 1.0404) with 161 amino acids (aa), a calculated molecular mass of 17.4 kDa and an isoelectric point (pI) of 6.1 (Lüttkopf et al., 2001). They are polymorphic variants of the same allergen (Chapman et al., 2007) and among them exhibit 97-99% of amino acid identity with a maximum of six substitutions in five of the highly conserved regions. "
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    ABSTRACT: In the last years, special attention has been devoted to food-induced allergies, from which hazelnut allergy is highlighted. Hazelnut is one of the most commonly consumed tree nuts, being largely used by the food industry in a wide variety of processed foods. It has been regarded as a food with potential health benefits, but also as a source of allergens capable of inducing mild to severe allergic reactions in sensitised individuals. Considering the great number of reports addressing hazelnut allergens, with an estimated increasing trend, this review intends to assemble all the relevant information available so far on the main issues: prevalence of tree nut allergy, clinical threshold levels, molecular characterisation of hazelnut allergens (Cor a 1, Cor a 2, Cor a 8, Cor a 9, Cor a 10, Cor a 11, Cor a 12, Cor a 14 and Cor a TLP) and their clinical relevance, and methodologies for hazelnut allergen detection in foods. A comprehensive overview on the current data about the molecular characterisation of hazelnut allergens is presented, relating biochemical classification and biological function with clinical importance. Recent advances on hazelnut allergen detection methodologies are summarised and compared, including all the novel protein- and DNA-based approaches.
    No preview · Article · Jan 2016 · Critical reviews in food science and nutrition
    • "The similarity between Der p2 and MD2 provided a nice explanation for the molecular basis of house dust mite recognition by the host, but many other allergen proteins bear no structural relationship to MD2 (Chapman et al., 2007). "
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    ABSTRACT: As we learn more about the biology of the Toll-like receptors (TLRs), a wide range of molecules that can activate this fascinating family of pattern recognition receptors emerges. In addition to conserved pathogenic components, endogenous danger signals created upon tissue damage are also sensed by TLRs. Detection of these types of stimuli results in TLR mediated inflammation that is vital to fight pathogenic invasion and drive tissue repair. Aberrant activation of TLRs by pathogenic and endogenous ligands has also been linked with the pathogenesis of an increasing number of infectious and autoimmune diseases, respectively. Most recently, allergen activation of TLRs has also been described, creating a third broad class of TLR stimulus that has helped to shed light on the pathogenesis of allergic disease. To date, microbial activation of TLRs remains best characterized. Each member of the TLR family senses a specific subset of pathogenic ligands, pathogen associated molecular patterns (PAMPS), and a wealth of structural and biochemical data continues to reveal the molecular mechanisms of TLR activation by PAMPs, and to demonstrate how receptor specificity is achieved. In contrast, the mechanisms by which endogenous molecules and allergens activate TLRs remain much more mysterious. Here, we provide an overview of our current knowledge of how very diverse stimuli activate the same TLRs and the structural basis of these modes of immunity.
    No preview · Article · Apr 2015 · Critical Reviews in Biochemistry and Molecular Biology
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    • "Their role in sensitizing asthmatic patients was first reported in 1921, and the association of HDM allergy, asthma, and atopic dermatitis has frequently been reported (Fuiano and Incorvaia 2004; Maeda et al. 1992; Sonmez Tamer and Caliskan 2009; Vieluf et al. 1993). Exposure to HDM allergens triggers inflammatory diseases in atopic patients, and allergens belonging to protein families with diverse biological functions contribute to allergenicity, (Chapman et al. 2007; Pomes 2008) such as the protease activity of group 1 mite allergens Der p 1 and the interaction with the innate immune system by the highly allergenic Abbreviations: SLE, systemic lupus erythematosus; Der p 2, recombinant protein of Dermatophagoides pteronyssinus group 2; PGK-1, phosphoglycerate kinase 1; TIM, triosephosphate isomerase; EBV, Epstein–Barr virus; PBMCs, peripheral blood mononuclear cells; ELISA, enzyme-linked immunosorbent assay; SDS-PAGE, sodium dodecyl sulfate-polyacrylamide gel electrophoresis; APC, antigen presenting cells. * Corresponding author at: Taichung Veterans General Hospital, No. 160, Section 3, Chung-Kang Road, Taichung 40705, Taiwan. "
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    ABSTRACT: Although many patients with SLE also have allergies, the immunological events triggering the onset and progression of the clinical manifestations of SLE by allergens have yet to be clarified. A total of three autoantigens, phosphoglycerate kinase 1 (PGK-1), triosephosphate isomerase (TIM) and enolase were identified by autologous serum in B cell lysate derived from HDM allergic SLE patients after Der p 2 stimulation. Autoantigen, TRIM-21 expression were also significantly increased in B cells derived from HDM allergic SLE patients. In PBMCs derived from SLE patients, the concentration of anti-PGK-1 was significantly upregulated after Der p 2 stimulation compared to HDM allergic without SLE patients and healthy subjects. Inflammatory related cytokines and chemokines include IL-1β, IL-6, IL-8, CXCL5 could be upregulated after Der p 2 stimulation in PBMCs derived from HDM allergic SLE patients. In conclusion, our data demonstrated that long-term allergen exposure could be a contributing factor in the development of SLE.
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