Interaction of an esophageal MEG protein from schistosomes with a human S100 protein involved in inflammatory response
Zeraik, Ana Eliza
Lopes, Jose L. S.
Macedo, Joci N. A.
dos Santos, Clarissa Romano
Oliveira, Katia Cristina [UNIFESP]
Wallace, B. A.
Araujo, Ana P. U.
Is part ofBiochimica Et Biophysica Acta-General Subjects
MetadataShow full item record
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 significance: 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. (C) 2016 Elsevier B.V. All rights reserved.
CitationBiochimica Et Biophysica Acta-General Subjects. Amsterdam, v. 1861, n. 1, p. 3490-3497, 2017.
KeywordsSynchrotron radiation circular dichroism spectroscopy
Intrinsically disordered proteins
SponsorshipConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
UK Biotechnology and Biological Research Council (BBSRC)
Institute for Synchrotron Facilities (ISA, Denmark)
- EPM - Artigos 
Showing items related by title, author, creator and subject.
Structural and mutational analyses of protein-protein interactions between transthyretin and retinol-binding protein Zanotti, Giuseppe; Folli, Claudia; Cendron, Laura; Alfieri, Beatrice; Nishida, Sonia Kiyomi [UNIFESP]; Gliubich, Francesca; Pasquato, Nicola; Negro, Alessandro; Berni, Rodolfo (Wiley-Blackwell, 2008-12-01)Transthyretin is a tetrameric binding protein involved in the transport of thyroid hormones and in the cotransport of retinol by forming a complex in plasma with retinol-binding protein. in the present study, we report the ...
Prion protein interaction with stress-inducible protein 1 enhances neuronal protein synthesis via mTOR Roffe, Martin [UNIFESP]; Beraldo, Flavio Henrique; Bester, Romina; Nunziante, Max; Bach, Christian; Mancini, Gabriel; Gilch, Sabine; Vorberg, Ina; Castilho, Beatriz Amaral de [UNIFESP]; Martins, Vilma Regina; Maroso Hajj, Glaucia Noeli (Natl Acad Sciences, 2010-07-20)Transmissible spongiform encephalopathies are fatal neurodegenerative diseases caused by the conversion of prion protein (PrPC) into an infectious isoform (PrPSc). How this event leads to pathology is not fully understood. ...
Increase in skeletal muscle protein content by the ß-2 selective adrenergic agonist clenbuterol exacerbates hypoalbuminemia in rats fed a low-protein diet Sawaya, Ana Lydia [UNIFESP]; Lunn, P.g. (Associação Brasileira de Divulgação Científica, 1998-06-01)This investigation examined how the nutritional status of rats fed a low-protein diet was affected when the animals were treated with the ß-2 selective agonist clenbuterol (CL). Males (4 weeks old) from an inbred, ...