Environmental and occupational respiratory disorders Current perspectives

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, Oct 05, 2015
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    • "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.
    Critical Reviews in Biochemistry and Molecular Biology 04/2015; DOI:10.3109/10409238.2015.1033511 · 7.71 Impact Factor
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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.
    Immunobiology 08/2014; 219(12). DOI:10.1016/j.imbio.2014.07.018 · 3.04 Impact Factor
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    • "Dataset for similarity based module ASM and APNSM For the in-house allergen database used in this study, the allergenic proteins were obtained from literature search and allergen databases including (a) Allergome (Mari et al., 2005); (b) Comprehensive allergen database (Hileman et al., 2002); (c) SDAP database (Ivanciuc et al., 2003); (d) Allergen structural database (Chapman et al., 2007), and Swiss- Prot Allergen Index ( .txt). "
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    ABSTRACT: Abstract The path to personalized medicine demands the use of new and customized biopharmaceutical products containing modified proteins. Hence, assessment of these products for allergenicity becomes mandatory before they are introduced as therapeutics. Despite the availability of different tools to predict the allergenicity of proteins, it remains challenging to predict the allergens and nonallergens, when they share significant sequence similarity with known nonallergens and allergens, respectively. Hence, we propose "FuzzyApp," a novel fuzzy rule based system to evaluate the quality of the query protein to be an allergen. It measures the allergenicity of the protein based on the fuzzy IF-THEN rules derived from five different modules. On various datasets, FuzzyApp outperformed other existing methods and retained balance between sensitivity and specificity, with positive Mathew's correlation coefficient. The high specificity of allergen-like putative nonallergens (APN) revealed the FuzzyApp's capability in distinguishing the APN from allergens. In addition, the error analysis and whole proteome dataset analysis suggest the efficiency and consistency of the proposed method. Further, FuzzyApp predicted the Tropomyosin from various allergenic and nonallergenic sources accurately. The web service created allows batch sequence submission, and outputs the result as readable sentences rather than values alone, which assists the user in understanding why and what features are responsible for the prediction. FuzzyApp is implemented using PERL CGI and is freely accessible at . We suggest the use of Fuzzy logic has much potential in biomarker and personalized medicine research to enhance predictive capabilities of post-genomics diagnostics.
    Omics A Journal of Integrative Biology 07/2014; 18(A head of print). DOI:10.1089/omi.2014.0021 · 2.36 Impact Factor
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