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.
Abstract
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.
Metadata
| 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 |
| URI: | https://eprints.bbk.ac.uk/id/eprint/16340 |
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