Molecular interactions between a recombinant IgE antibody and the beta-lactoglobulin allergen

Merja Niemi, Sirpa Jylhä, Marja-Leena Laukkanen, Hans Söderlund, Soili Mäkinen-Kiljunen, Johanna M. Kallio, Nina Hakulinen, Tari Haahtela, Kristiina Takkinen, Juha Rouvinen

    Research output: Contribution to journalArticleScientificpeer-review

    121 Citations (Scopus)


    Allergies are caused by the immune reaction to commonly harmless proteins, allergens.
    This reaction is typified by immunoglobulin E (IgE) antibodies. We report the crystal structure of an IgE Fab fragment in complex with β-lactoglobulin (BLG), one of the major allergens of bovine milk. The solved structure shows how two IgE/Fab molecules bind the dimeric BLG. The epitope of BLG consists of six different short fragments of the polypeptide chain, which are located especially in the β strands, covering a flat area on the allergen surface.
    All six CDR (complementary-determining region) loops of the IgE Fab participate in the binding of BLG. The light chain CDR loops are responsible for the binding of the flat β sheet region of BLG.
    The IgE epitope is different from common IgG epitopes that are normally located in the exposed loop regions of antigens and observed also in the two recently determined allergen-IgG complexes.
    Original languageEnglish
    Pages (from-to)1413-1421
    Issue number11
    Publication statusPublished - 2007
    MoE publication typeA1 Journal article-refereed


    • allergen
    • allergy
    • IgE antibody
    • antibodies
    • recombinant antibodies
    • lactoglobulin


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