| Literature DB >> 27539850 |
Kareem Gamal ElRamlawy1,2, Takashi Fujimura3, Koji Baba1, Ji Won Kim1, Chika Kawamoto1, Toshihide Isobe1, Takuya Abe1, Kelsey Hodge-Hanson4, Diana M Downs4, Inas Hussein Refaat2, Diaa Beshr Al-Azhary2, Tsunehiro Aki1, Yoshiko Asaoku5, Takaharu Hayashi5, Takashi Katsutani6, Shinji Tsuboi7, Kazuhisa Ono1,8, Seiji Kawamoto9.
Abstract
The high prevalence of house dust mite (HDM) allergy is a growing health problem worldwide, and the characterization of clinically important HDM allergens is a prerequisite for the development of diagnostic and therapeutic strategies. Here, we report a novel HDM allergen that belongs structurally to the highly conserved Rid/YjgF/YER057c/UK114 family (Rid family) with imine deaminase activity. Isolated HDM cDNA, named der f 34, encodes 128 amino acids homologous to Rid-like proteins. This new protein belongs to the Rid family and has seven conserved residues involved in enamine/imine deaminase activity. Indeed, we demonstrated that purified Der f 34 had imine deaminase activity that preferentially acted on leucine and methionine. Native Der f 34 showed a high IgE binding frequency as revealed by two-dimensional immunoblotting (62.5%) or ELISA (68%), which was comparable with those of a major HDM allergen Der f 2 (77.5 and 79%, respectively). We also found that Der f 34 showed cross-reactivity with another prominent indoor allergen source, Aspergillus fumigatus This is the first report showing that the Rid family imine deaminase represents an additional important pan-allergen that is conserved across organisms.Entities:
Keywords: Aspergillus; Rid/YjgF/YER057c/UK114 family; allergen; allergy; asthma; fungi; house dust mite; imine deaminase; immunoglobulin E (IgE)
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Year: 2016 PMID: 27539850 PMCID: PMC5076831 DOI: 10.1074/jbc.M116.728006
Source DB: PubMed Journal: J Biol Chem ISSN: 0021-9258 Impact factor: 5.157