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  • 1.
    Markovic, Maja Pavlovic
    et al.
    Södertörn University, School of Life Sciences.
    Kylsten, Per
    Södertörn University, School of Life Sciences, Molecular biology.
    Dushay, Mitchell S.
    Södertörn University, School of Life Sciences.
    Drosophila lamin mutations cause melanotic mass formation and lamellocyte differentiation2009In: Molecular Immunology, ISSN 0161-5890, E-ISSN 1872-9142, Vol. 46, no 16, p. 3245-3250Article in journal (Refereed)
    Abstract [en]

    The fruit fly immune system is a valuable model for invertebrate and innate immunity. Cellular immune reactions in Drosophila are of great interest, especially the molecular genetic mechanisms of hemocyte differentiation and the encapsulation of foreign bodies. Here we report that changes in the lamin gene cause melanotic masses. These darkened clusters of cells result from autoimmune-like encapsulation of self-tissue, as shown by the presence in lam larvae of lamellocytes, effector hemocytes that appear in larvae following wounding or parasitization. Lamins thus affect immunity in Drosophila, and lam mutations can serve as genetic tools to dissect cellular immune signaling and effector pathways.

  • 2. Vilhelmsson, Monica
    et al.
    Glaser, Andreas G.
    Martinez, Daniel Badia
    Schmidt, Margit
    Johansson, Catharina
    Rhyner, Claudio
    Berndt, Kurt D.
    Södertörn University, School of Life Sciences. Karolinska Institutet.
    Scheynius, Annika
    Crameri, Reto
    Achour, Adnane
    Zargari, Arezou
    Mutational analysis of amino acid residues involved in IgE-binding to the Malassezia sympodialis allergen Mala s 112008In: Molecular Immunology, ISSN 0161-5890, E-ISSN 1872-9142, Vol. 46, no 2, p. 294-303Article in journal (Refereed)
    Abstract [en]

    The yeast Malassezia sympodialis, which is an integral part of the normal cutaneous flora, has been shown to elicit specific IgE- and T-cell reactivity in atopic eczema (AE) patients. The M. sympodialis allergen Mala s 11 has a high degree of amino acid sequence homology to manganese superoxide dismutase (MnSOD) from Homo sapiens (50%) and Aspergillus fumigatus (56%). Humoral and cell-mediated cross-reactivity between MnSOD from H. sapiens and A. fumigatus has been demonstrated. Taken together with the recent finding that human MnSOD (hMnSOD) can act as an autoallergen in AE patients sensitised to M. sympodialis, we hypothesized that cross-reactivity could also occur between hMnSOD and Mala s 11, endogenous hMnSOD thus being capable of stimulating an immune response through molecular mimicry. Herein we demonstrate that recombinant Mala s 11 (rMala s 11) is able to inhibit IgE-binding to recombinant hMnSOD and vice versa, indicating that these two homologues share common IgE-binding epitopes and providing an explanation at a molecular level for the autoreactivity to hMnSOD observed in AE patients sensitised to Mala s 11. Using molecular modelling and mapping of identical amino acids exposed on the surface of both Mala s 11 and hMnSCE) we identified four regions each composed of 4-5 residues which are potentially involved in IgE-mediated cross-reactivity. Mutated rMala s 11 molecules were produced in which these residues were altered. Native-like folding was verified by enzymatic activity tests and circular dichroism. The rMala s 11 mutants displayed lower IgE-binding in comparison to wild-type rMala s 11 using plasma from AE patients. In particular, mutation of the residues E29, P30, E122 and K125 lowered the IgE-binding to Mala s 11. The results of this study provide new insights in the molecular basis underlying the cross-reactivity between Mala s 11 and hMnSOD.

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