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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    • "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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    • "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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