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

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dc.citation.issue1
dc.citation.volume1861
dc.contributor.authorOrcia, Debora
dc.contributor.authorZeraik, Ana Eliza
dc.contributor.authorLopes, Jose L. S.
dc.contributor.authorMacedo, Joci N. A.
dc.contributor.authordos Santos, Clarissa Romano
dc.contributor.authorOliveira, Katia Cristina [UNIFESP]
dc.contributor.authorAnderson, Leticia
dc.contributor.authorWallace, B. A.
dc.contributor.authorVerjovski-Almeida, Sergio
dc.contributor.authorAraujo, Ana P. U.
dc.contributor.authorDeMarco, Ricardo
dc.coverageAmsterdam
dc.date.accessioned2020-07-31T12:47:00Z
dc.date.available2020-07-31T12:47:00Z
dc.date.issued2017
dc.description.abstractBackground: 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.en
dc.description.affiliationUniv Sao Paulo, Inst Fis Sao Carlos, Sao Carlos, SP, Brazil
dc.description.affiliationAdolfo Lutz Inst, Ctr Parasitol & Micol, Nucleo Enteroparasitas, Sao Paulo, Brazil
dc.description.affiliationUniv Sao Paulo, Inst Quim, Sao Paulo, Brazil
dc.description.affiliationUniv London, Inst Struct & Mol Biol, Birkbeck Coll, London, England
dc.description.affiliationInst Butantan, Sao Paulo, SP, Brazil
dc.description.affiliationUniv Sao Paulo, Inst Fis, Dept Fis Aplicada, Sao Paulo, SP, Brazil
dc.description.affiliationUniv Fed Sao Paulo, Dept Microbiol Imunol & Parasit, Disciplina Parasitol, Escola Paulista Med, Sao Paulo, SP, Brazil
dc.description.affiliationUnifespDisciplina de Parasitologia, Departamento de Microbiologia, Imunologia e Parasitogia, Escola Paulista de Medicina, Universidade Federal de São Paulo, Brazil
dc.description.provenanceMade available in DSpace on 2020-07-31T12:47:00Z (GMT). No. of bitstreams: 0 Previous issue date: 2017en
dc.description.sourceWeb of Science
dc.description.sponsorshipConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.description.sponsorshipUK Biotechnology and Biological Research Council (BBSRC)
dc.description.sponsorshipInstitute for Synchrotron Facilities (ISA, Denmark)
dc.description.sponsorshipIDFAPESP: 2014/09361-9
dc.description.sponsorshipIDFAPESP: 2012/09186-7
dc.description.sponsorshipIDBBSRC: J019135
dc.description.sponsorshipIDFAPESP: 2012/07288-7
dc.description.sponsorshipIDFAPESP: 2013/20715-4
dc.description.sponsorshipIDFAPESP: 2010/20290-5
dc.description.sponsorshipIDCNPq: 150304/2015-3
dc.description.sponsorshipIDBBSRC: J019747
dc.description.sponsorshipIDCNPq: 553056/2011-5
dc.description.sponsorshipIDCNPq: 407337/2013-0
dc.description.sponsorshipIDISA, Denmark: ISA-13-1007
dc.format.extent3490-3497
dc.identifierhttp://dx.doi.org/10.1016/j.bbagen.2016.09.015
dc.identifier.citationBiochimica Et Biophysica Acta-General Subjects. Amsterdam, v. 1861, n. 1, p. 3490-3497, 2017.
dc.identifier.doi10.1016/j.bbagen.2016.09.015
dc.identifier.issn0304-4165
dc.identifier.urihttps://repositorio.unifesp.br/handle/11600/56511
dc.identifier.wosWOS:000390736300053
dc.language.isoeng
dc.publisherElsevier Science Bv
dc.relation.ispartofBiochimica Et Biophysica Acta-General Subjects
dc.rightsAcesso restrito
dc.subjectSynchrotron radiation circular dichroism spectroscopyen
dc.subjectMicro-exon geneen
dc.subjectProtein-protein interactionen
dc.subjectIntrinsically disordered proteinsen
dc.titleInteraction of an esophageal MEG protein from schistosomes with a human S100 protein involved in inflammatory responseen
dc.typeArtigo
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