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Allergens are distributed into few protein families and possess a restricted number of biochemical functions.

Radauer, Christian, Bublin, Merima, Wagner, Stefan, Mari, Adriano, Breiteneder, Heimo·2008·Journal of Allergy and Clinical Immunology
DOI 10.1016/j.jaci.2008.01.025
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Abstract

Background Existing allergen databases classify their entries by source and route of exposure, thus lacking an evolutionary, structural, and functional classification of allergens. Objective We sought to build AllFam, a database of allergen families, and use it to extract common structural and functional properties of allergens. Methods Allergen data from the Allergome database and protein family definitions from the Pfam database were merged into AllFam, a database that is freely accessible on the Internet at http://www.meduniwien.ac.at/allergens/allfam/. A structural classification of allergens was established by matching Pfam families with families from the Structural Classification of Proteins database. Biochemical functions of allergens were extracted from the Gene Ontology Annotation database. Results Seven hundred seven allergens were classified by sequence into 134 AllFam families containing 184 Pfam domains (2% of 9318 Pfam families). A random set of 707 sequences with the same taxonomic distribution contained a significantly higher number of different Pfam domains (479 +/- 17). Classifying allergens by structure revealed that 5% of 3012 Structural Classification of Proteins families contained allergens. The biochemical functions of allergens most frequently found were limited to hydrolysis of proteins, polysaccharides, and lipids; binding of metal ions and lipids; storage; and cytoskeleton association. Conclusion The small number of protein families that contain all…

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  • Molecular properties of food allergens

    Breiteneder, H., & Mills, E. N. C. (2005) · Journal of Allergy and Clinical Immunology · doi:10.1016/j.jaci.2004.10.022 · Cited by 359 · cited 1×

    “In contrast, common structural features have been established for food allergens that sensitize through the gastrointestinal tract.(24) These features, such as high numbers of disulfide bonds, repetitive structures, binding of lipid or metal ions, and formation of stable oligomers, confer stability toward heat, acid,…”
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Metadata

Authors
Radauer, C., Bublin, M., Wagner, S., Mari, A., & Breiteneder, H.
Venue
Journal of Allergy and Clinical Immunology
Publisher
Elsevier BV
Published
2008-04
Volume
121
Issue
4
Pages
847-852.e7
ISSN
0091-6749
DOI
10.1016/j.jaci.2008.01.025
Cited by
429
References
1
Language
en
Licence
www.elsevier.com/tdm/userlicense/1.0/ (tdm)

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