Structure of the house dust mite allergen Der f 2: implications for function and molecular basis of IgE cross-reactivity

Birthe R Johannessen, Lars Skov, Jette S Kastrup, Ole Kristensen, Caroline Bolwig, Jørgen Larsen, Michael Spangfort, Kaare Lund, Michael Gajhede

    41 Citations (Scopus)

    Abstract

    The X-ray structure of the group 2 major allergen from Dermatophagoides farinae (Der f 2) was determined to 1.83 A resolution. The overall Der f 2 structure comprises a single domain of immunoglobulin fold with two anti-parallel beta-sheets. A large hydrophobic cavity is formed in the interior of Der f 2. Structural comparisons to distantly related proteins suggest a role in lipid binding. Immunoglobulin E (IgE) cross-reactivity between group 2 house dust mite major allergens can be explained by conserved surface areas representing IgE binding epitopes.
    Original languageEnglish
    JournalF E B S Letters
    Volume579
    Issue number5
    Pages (from-to)1208-12
    Number of pages5
    ISSN0014-5793
    DOIs
    Publication statusPublished - 2005

    Keywords

    • Allergens
    • Animals
    • Antigens, Dermatophagoides
    • Arthropod Proteins
    • Cross Reactions
    • Crystallography, X-Ray
    • Epitopes
    • Hydrophobic and Hydrophilic Interactions
    • Immunoglobulin E
    • Lipid Metabolism
    • Models, Molecular
    • Protein Structure, Tertiary
    • Pyroglyphidae

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