Transient dimers of allergens

Juha Rouvinen (Corresponding Author), Janne Jänis, Marja-Leena Laukkanen, Sirpa Jylhä, Merja Niemi, Tero Päivinen, Soili Mäkinen-Kiljunen, Tari Haahtela, Hans Söderlund, Kristiina Takkinen

    Research output: Contribution to journalArticleScientificpeer-review

    60 Citations (Scopus)



    Allergen-mediated cross-linking of IgE antibodies bound to the FcεRI receptors on the mast cell surface is the key feature of the type I allergy. If an allergen is a homodimer, its allergenicity is enhanced because it would only need one type of antibody, instead of two, for cross-linking.

    Methodology/Principal Findings

    An analysis of 55 crystal structures of allergens showed that 80% of them exist in symmetric dimers or oligomers in crystals. The majority are transient dimers that are formed at high protein concentrations that are reached in cells by colocalization. Native mass spectrometric analysis showed that native allergens do indeed form transient dimers in solution, while hypoallergenic variants of them exist almost solely in the monomeric form. We created a monomeric Bos d 5 allergen and show that it has a reduced capability to induce histamine release.


    The results suggest that dimerization would be a very common and essential feature for allergens. Thus, the preparation of purely monomeric variants of allergens could open up novel possibilities for specific immunotherapy.

    Original languageEnglish
    Article numbere9037
    Number of pages9
    JournalPLoS ONE
    Issue number2
    Publication statusPublished - 2010
    MoE publication typeA1 Journal article-refereed


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