Human TNF-alpha induces differential protein phosphorylation in Schistosoma mansoni adult male worms

Página do item simplificado
dc.citation.issue2
dc.citation.volume115
dc.contributor.authorOliveira, Katia C. [UNIFESP]
dc.contributor.authorCarvalho, Mariana L. P.
dc.contributor.authorBonatto, Jose Matheus C.
dc.contributor.authorSchechtman, Debora
dc.contributor.authorVerjovski-Almeida, Sergio
dc.coverageNew York
dc.date.accessioned2020-11-03T14:40:30Z
dc.date.available2020-11-03T14:40:30Z
dc.date.issued2016
dc.description.abstractSchistosoma mansoni and its vertebrate host have a complex and intimate connection in which several molecular stimuli are exchanged and affect both organisms. Human tumor necrosis factor alpha (hTNF-alpha), a pro-inflammatory cytokine, is known to induce large-scale gene expression changes in the parasite and to affect several parasite biological processes such as metabolism, egg laying, and worm development. Until now, the molecular mechanisms for TNF-alpha activity in worms are not completely understood. Here, we aimed at exploring the effect of hTNF-alpha on S. mansoni protein phosphorylation by 2D gel electrophoresis followed by a quantitative analysis of phosphoprotein staining and protein identification by mass spectrometry. We analyzed three biological replicates of adult male worms exposed to hTNF-alpha and successfully identified 32 protein spots with a statistically significant increase in phosphorylation upon in vitro exposure to hTNF-alpha. Among the differentially phosphorylated proteins, we found proteins involved in metabolism, such as glycolysis, galactose metabolism, urea cycle, and aldehyde metabolism, as well as proteins related to muscle contraction and to cytoskeleton remodeling. The most differentially phosphorylated protein (30-fold increase in phosphorylation) was 14-3-3, whose function is known to be modulated by phosphorylation, belonging to a signal transduction protein family that regulates a variety of processes in all eukaryotic cells. Further, 75 % of the identified proteins are known in mammals to be related to TNF-alpha signaling, thus suggesting that TNF-alpha response may be conserved in the parasite. We propose that this work opens new perspectives to be explored in the study of the molecular crosstalk between host and pathogen.en
dc.description.affiliationAdolfo Lutz Inst, Centro Parasitol & Micol, Nucleo Enteroparasitas, BR-01614000 Sao Paulo, SP, Brazil
dc.description.affiliationUniv Sao Paulo, Inst Quim, Dept Bioquim, BR-05508900 Sao Paulo, SP, Brazil
dc.description.affiliationInst Butantan, BR-05503900 Sao Paulo, SP, Brazil
dc.description.affiliationUniv Fed Sao Paulo, Dept Microbiol Immunol & Parasitol, Disciplina Parasitol, Sao Paulo, Brazil
dc.description.affiliationUnifespUniv Fed Sao Paulo, Dept Microbiol Immunol & Parasitol, Disciplina Parasitol, Sao Paulo, Brazil
dc.description.sourceWeb of Science
dc.description.sponsorshipFundacao de Amparo a Pesquisa do Estado de Sao Paulo (FAPESP)
dc.description.sponsorshipConselho Nacional de Desenvolvimento Cientifico e Tecnologico (CNPq)
dc.description.sponsorshipFAPESP
dc.description.sponsorshipCNPq
dc.format.extent817-828
dc.identifierhttps://doi.org/10.1007/s00436-015-4812-5
dc.identifier.citationParasitology Research. New York, v. 115, n. 2, p. 817-828, 2016.
dc.identifier.doi10.1007/s00436-015-4812-5
dc.identifier.issn0932-0113
dc.identifier.urihttps://repositorio.unifesp.br/handle/11600/58595
dc.identifier.wosWOS:000370868800041
dc.language.isoeng
dc.publisherSpringer
dc.relation.ispartofParasitology Research
dc.rightsinfo:eu-repo/semantics/openAccess
dc.subjectSchistosoma mansonien
dc.subjectHuman TNF-alphaen
dc.subjectSignalingen
dc.subjectPhosphoproteomic analysisen
dc.subjectMass spectrometryen
dc.subjectHost-parasite interactionen
dc.titleHuman TNF-alpha induces differential protein phosphorylation in Schistosoma mansoni adult male wormsen
dc.typeinfo:eu-repo/semantics/article
Arquivos
Coleções
EPM - Artigos