Nomenclature and structural biology of allergens
- PMID: 17166572
- DOI: 10.1016/j.jaci.2006.11.001
Nomenclature and structural biology of allergens
Abstract
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.
Similar articles
-
Pollen allergens are restricted to few protein families and show distinct patterns of species distribution.J Allergy Clin Immunol. 2006 Jan;117(1):141-7. doi: 10.1016/j.jaci.2005.09.010. Epub 2005 Nov 28. J Allergy Clin Immunol. 2006. PMID: 16387597
-
Evolutionary distance from human homologs reflects allergenicity of animal food proteins.J Allergy Clin Immunol. 2007 Dec;120(6):1399-405. doi: 10.1016/j.jaci.2007.08.019. Epub 2007 Nov 1. J Allergy Clin Immunol. 2007. PMID: 17935767
-
Update of the WHO/IUIS Allergen Nomenclature Database based on analysis of allergen sequences.Allergy. 2014 Apr;69(4):413-9. doi: 10.1111/all.12348. Allergy. 2014. PMID: 24738154 Review.
-
Recombinant allergens for diagnosis and therapy of allergic disease.J Allergy Clin Immunol. 2000 Sep;106(3):409-18. doi: 10.1067/mai.2000.109832. J Allergy Clin Immunol. 2000. PMID: 10984358 Review.
-
Plant food allergens--structural and functional aspects of allergenicity.Biotechnol Adv. 2005 Sep;23(6):395-9. doi: 10.1016/j.biotechadv.2005.05.004. Biotechnol Adv. 2005. PMID: 15985358 Review.
Cited by
-
Population growth and allergen accumulation of Dermatophagoides farinae cultured at 20 and 25 °C.Exp Appl Acarol. 2013 May;60(1):117-26. doi: 10.1007/s10493-012-9626-x. Epub 2012 Oct 16. Exp Appl Acarol. 2013. PMID: 23070476
-
Der p 5 crystal structure provides insight into the group 5 dust mite allergens.J Biol Chem. 2010 Aug 13;285(33):25394-401. doi: 10.1074/jbc.M110.128306. Epub 2010 Jun 9. J Biol Chem. 2010. PMID: 20534590 Free PMC article.
-
Epithelial PI3K-δ Promotes House Dust Mite-Induced Allergic Asthma in NLRP3 Inflammasome-Dependent and -Independent Manners.Allergy Asthma Immunol Res. 2020 Mar;12(2):338-358. doi: 10.4168/aair.2020.12.2.338. Allergy Asthma Immunol Res. 2020. PMID: 32009326 Free PMC article.
-
Molecular allergology approach to allergic diseases in the paediatric age.Ital J Pediatr. 2009 Oct 5;35(1):29. doi: 10.1186/1824-7288-35-29. Ital J Pediatr. 2009. PMID: 19804642 Free PMC article.
-
A history of hookworm vaccine development.Hum Vaccin. 2011 Nov;7(11):1234-44. doi: 10.4161/hv.7.11.18443. Epub 2011 Nov 1. Hum Vaccin. 2011. PMID: 22064562 Free PMC article. Review.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources