Lipopolysaccharide binding of the mite allergen Der f 2

Saori Ichikawa, Toshiro Takai, Tomoe Yashiki, Seizo Takahashi, Ko Okumura, Hideoki Ogawa, Daisuke Kohda, Hideki Hatanaka

    Research output: Contribution to journalArticlepeer-review

    75 Citations (Scopus)


    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.

    Original languageEnglish
    Pages (from-to)1055-1065
    Number of pages11
    JournalGenes to Cells
    Issue number9
    Publication statusPublished - 2009

    All Science Journal Classification (ASJC) codes

    • Genetics
    • Cell Biology


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