Lipopolysaccharide binding of the mite allergen Der f 2

Lipid‐binding properties and/or involvement with host defense are often found in allergen proteins, implying that these intrinsic biological functions likely contribute to the allergenicity of allergens. The group 2 major mite allergens, Der f 2 and Der p 2, show structural homology with MD‐2, the l...

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Bibliographic Details
Published in:Genes to cells : devoted to molecular & cellular mechanisms 2009-09, Vol.14 (9), p.1055-1065
Main Authors: Ichikawa, Saori, Takai, Toshiro, Yashiki, Tomoe, Takahashi, Seizo, Okumura, Ko, Ogawa, Hideoki, Kohda, Daisuke, Hatanaka, Hideki
Format: Article
Language:English
Subjects:
Allergenicity
Allergens
Allergens - metabolism
Animals
Antigens, Dermatophagoides - chemistry
Antigens, Dermatophagoides - metabolism
Arthropod Proteins
Binding Sites
Chromatography, Gel
Der f 2 antigen
Escherichia coli
Escherichia coli - metabolism
Filtration
Fluorescence
Homology
Immunity
Ligands
Lipopolysaccharides
Lipopolysaccharides - chemistry
Lipopolysaccharides - metabolism
Magnetic Resonance Spectroscopy
Models, Molecular
N.M.R
Signal transduction
TLR4 protein
Toll-like receptors
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Summary:Lipid‐binding properties and/or involvement with host defense are often found in allergen proteins, implying that these intrinsic biological functions likely contribute to the allergenicity of allergens. The group 2 major mite allergens, Der f 2 and Der p 2, show structural homology with MD‐2, the lipopolysaccharide (LPS)‐binding component of the Toll‐like receptor (TLR) 4 signalling complex. Elucidation of the ligand‐binding properties of group 2 mite allergens and identification of interaction sites by structural studies are important to explore the relationship between allergenicity and biological function. Here, we report a ligand‐fishing approach in which His‐tagged Der f 2 was incubated with sonicated stable isotope‐labelled Escherichia coli as a potential ligand source, followed by isolation of Der f 2‐bound material by a HisTrap column and NMR analysis. We found that Der f 2 binds to LPS with a nanomolar affinity and, using fluorescence and gel filtration assays that LPS binds to Der f 2 in a molar ratio of 1 : 1. We mapped the LPS‐binding interface of Der f 2 by NMR perturbation studies, which suggested that LPS binds Der f 2 between the two large β‐sheets, similar to its binding to MD‐2, the LPS‐binding component of the innate immunity receptor TLR4.
ISSN:1356-9597
1365-2443
DOI:10.1111/j.1365-2443.2009.01334.x