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

Abstract 

The X-ray structure of the group 2 major allergen from Dermatophagoides farinae (Der f 2) was determined to 1.83Å resolution. The overall Der f 2 structure comprises a single domain of immunoglobulin fold with two anti-parallel β-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.

Abbreviations: Eur m 2, Euroglyphus maynei major allergen 2, GM2-AP, GM2-activator protein, HE1, human epidymal secretory protein, IgE, immunoglobulin E, Lep d 2, major type 2 allergen Lepidoglyphus destructor, Der f 2, major type 2 allergen from Dermatophagoides farinae, Der p 2, major type 2 allergen from Dermatophagoides pteronyssinus, ML, MD-2-related lipid-recognition, MR, molecular replacement, PEG, Polyethylene glycol, RhoGDI, Rho-specific guanine dissociation inhibitor, RMSD, root mean square deviation

Keywords: Dermatophagoides farinae group 2 major allergen, Cross-reacting epitope, Hydrophobic cavity, Lipid binding