Article ; Online: The minor house dust mite allergen Der p 13 is a fatty acid-binding protein and an activator of a TLR2-mediated innate immune response.
2016 Volume 71, Issue 10, Page(s) 1425–1434
Abstract: Background: The house dust mite (HDM) allergen Der p 13 could be a lipid-binding protein able ... reactivity of recombinant Der p 13 (rDer p 13), its lipid-binding activities, and its capacity to stimulate ... airway epithelium cells.: Methods: Purified rDer p 13 was characterized by mass spectrometry ...
| Abstract | Background: The house dust mite (HDM) allergen Der p 13 could be a lipid-binding protein able to activate key innate signaling pathways in the initiation of the allergic response. We investigated the IgE reactivity of recombinant Der p 13 (rDer p 13), its lipid-binding activities, and its capacity to stimulate airway epithelium cells. Methods: Purified rDer p 13 was characterized by mass spectrometry, circular dichroism, fluorescence-based lipid-binding assays, and in silico structural prediction. IgE-binding activity and allergenic potential of Der p 13 were examined by ELISA, basophil degranulation assays, and in vitro airway epithelial cell activation assays. Results: Protein modeling and biophysical analysis indicated that Der p 13 adopts a β-barrel structure with a predominately apolar pocket representing a potential binding site for hydrophobic ligands. Fluorescent lipid-binding assays confirmed that the protein is highly selective for ligands and that it binds a fatty acid with a dissociation constant typical of lipid transporter proteins. The low IgE-binding frequency (7%, n = 224) in Thai HDM-allergic patients as well as the limited propensity to activate basophil degranulation classifies Der p 13 as a minor HDM allergen. Nevertheless, the protein with its presumptively associated lipid(s) triggered the production of IL-8 and GM-CSF in respiratory epithelial cells through a TLR2-, MyD88-, NF-kB-, and MAPK-dependent signaling pathway. Conclusions: Although a minor allergen, Der p 13 may, through its lipid-binding capacity, play a role in the initiation of the HDM-allergic response through TLR2 activation. |
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| MeSH term(s) | Allergens/immunology ; Animals ; Antigens, Dermatophagoides/chemistry ; Antigens, Dermatophagoides/immunology ; Antigens, Dermatophagoides/metabolism ; Basophils/immunology ; Basophils/metabolism ; Carrier Proteins/metabolism ; Cell Degranulation/immunology ; Dermatophagoides pteronyssinus/immunology ; Fatty Acid-Binding Proteins/chemistry ; Fatty Acid-Binding Proteins/immunology ; Fatty Acid-Binding Proteins/metabolism ; Humans ; Immunity, Innate ; Immunoglobulin E/immunology ; Lipid Metabolism ; Models, Molecular ; Protein Binding ; Protein Conformation ; Respiratory Mucosa/immunology ; Respiratory Mucosa/metabolism ; Toll-Like Receptor 2/agonists ; Toll-Like Receptor 2/metabolism |
| Chemical Substances | Allergens ; Antigens, Dermatophagoides ; Carrier Proteins ; Fatty Acid-Binding Proteins ; Toll-Like Receptor 2 ; Immunoglobulin E (37341-29-0) |
| Language | English |
| Publishing date | 2016-04-29 |
| Publishing country | Denmark |
| Document type | Journal Article ; Research Support, Non-U.S. Gov't |
| ZDB-ID | 391933-x |
| ISSN | 1398-9995 ; 0105-4538 |
| ISSN (online) | 1398-9995 |
| ISSN | 0105-4538 |
| DOI | 10.1111/all.12899 |
| Database | MEDical Literature Analysis and Retrieval System OnLINE |
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