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    Interaction of an esophageal MEG protein from schistosomes with a human S100 protein involved in inflammatory response

    Orcia, D. and Zeraik, A.E. and Lopes, J.L.S. and Macedo, J.N.A. and Santos, C.R.d. and Oliveira, K.C. and Anderson, L. and Wallace, Bonnie A. and Verjovski-Almeida, S. and Araujo, A.P.U. and DeMarco, R. (2016) Interaction of an esophageal MEG protein from schistosomes with a human S100 protein involved in inflammatory response. Biochimica et Biophysica Acta (BBA) - General Subjects 1861 (1A), pp. 3490-3497. ISSN 0304-4165.

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    BACKGROUND: The Micro-Exon Gene-14 (MEG-14) displays a remarkable structure that allows the generation of antigenic variation in Schistosomes. Previous studies showed that the soluble portion of the MEG-14 protein displays features of an intrinsically disordered protein and is expressed exclusively in the parasite esophageal gland. These features indicated a potential for interaction with host proteins present in the plasma and cells from ingested blood. METHODS: A yeast two-hybrid experiment using as bait the soluble domain of Schistosoma mansoni MEG-14 (sMEG-14) against a human leukocyte cDNA library was performed. Pull-down and surface plasmon resonance (SPR) experiments were used to validate the interaction between sMEG-14 and human S100A9. Synchrotron radiation circular dichroism (SRCD) were used to detect structural changes upon interaction between sMEG-14 and human S100A9. Feeding of live parasites with S100A9 attached to a fluorophore allowed the tracking of the fate of this protein in the parasite digestive system. RESULTS: S100A9 interacted with sMEG-14 consistently in yeast two-hybrid assay, pull-down and SPR experiments. SRCD suggested that MEG-14 acquired a more regular structure as a result of the interaction with S100A9. Accumulation of recombinant S100A9 in the parasite's esophageal gland, when ingested by live worms suggests that such interaction may occur in vivo. CONCLUSION: S100A9, a protein previously described to be involved in modulation of inflammatory response, was found to interact with sMEG-14. GENERAL SIGINFICANCE: Our results allow proposing a mechanism involving MEG-14 for the parasite to block inflammatory signaling, which would occur upon release of S100A9 when ingested blood cells are lysed.


    Item Type: Article
    Keyword(s) / Subject(s): Synchrotron radiation circular dichroism spectroscopy, Micro-exon gene, Protein-protein interaction, Intrinsically disordered proteins
    School: Birkbeck Faculties and Schools > Faculty of Science > School of Natural Sciences
    Research Centres and Institutes: Bioinformatics, Bloomsbury Centre for (Closed), Structural Molecular Biology, Institute of (ISMB)
    Depositing User: Administrator
    Date Deposited: 14 Oct 2016 13:34
    Last Modified: 02 Aug 2023 17:27


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