Human TNF-alpha induces differential protein phosphorylation in Schistosoma mansoni adult male worms
Autor(a) principal: | |
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Data de Publicação: | 2016 |
Outros Autores: | , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Institucional da UNIFESP |
Texto Completo: | https://repositorio.unifesp.br/handle/11600/58595 https://doi.org/10.1007/s00436-015-4812-5 |
Resumo: | Schistosoma 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. |
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Oliveira, Katia C. [UNIFESP]Carvalho, Mariana L. P.Bonatto, Jose Matheus C.Schechtman, DeboraVerjovski-Almeida, Sergio2020-11-03T14:40:30Z2020-11-03T14:40:30Z2016Parasitology Research. New York, v. 115, n. 2, p. 817-828, 2016.0932-0113https://repositorio.unifesp.br/handle/11600/58595https://doi.org/10.1007/s00436-015-4812-510.1007/s00436-015-4812-5WOS:000370868800041Schistosoma 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.Fundacao de Amparo a Pesquisa do Estado de Sao Paulo (FAPESP)Conselho Nacional de Desenvolvimento Cientifico e Tecnologico (CNPq)FAPESPCNPqAdolfo Lutz Inst, Centro Parasitol & Micol, Nucleo Enteroparasitas, BR-01614000 Sao Paulo, SP, BrazilUniv Sao Paulo, Inst Quim, Dept Bioquim, BR-05508900 Sao Paulo, SP, BrazilInst Butantan, BR-05503900 Sao Paulo, SP, BrazilUniv Fed Sao Paulo, Dept Microbiol Immunol & Parasitol, Disciplina Parasitol, Sao Paulo, BrazilUniv Fed Sao Paulo, Dept Microbiol Immunol & Parasitol, Disciplina Parasitol, Sao Paulo, BrazilWeb of Science817-828engSpringerParasitology ResearchSchistosoma mansoniHuman TNF-alphaSignalingPhosphoproteomic analysisMass spectrometryHost-parasite interactionHuman TNF-alpha induces differential protein phosphorylation in Schistosoma mansoni adult male wormsinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleNew York1152info:eu-repo/semantics/openAccessreponame:Repositório Institucional da UNIFESPinstname:Universidade Federal de São Paulo (UNIFESP)instacron:UNIFESP11600/585952022-02-08 11:52:12.014metadata only accessoai:repositorio.unifesp.br:11600/58595Repositório InstitucionalPUBhttp://www.repositorio.unifesp.br/oai/requestopendoar:34652022-02-08T14:52:12Repositório Institucional da UNIFESP - Universidade Federal de São Paulo (UNIFESP)false |
dc.title.en.fl_str_mv |
Human TNF-alpha induces differential protein phosphorylation in Schistosoma mansoni adult male worms |
title |
Human TNF-alpha induces differential protein phosphorylation in Schistosoma mansoni adult male worms |
spellingShingle |
Human TNF-alpha induces differential protein phosphorylation in Schistosoma mansoni adult male worms Oliveira, Katia C. [UNIFESP] Schistosoma mansoni Human TNF-alpha Signaling Phosphoproteomic analysis Mass spectrometry Host-parasite interaction |
title_short |
Human TNF-alpha induces differential protein phosphorylation in Schistosoma mansoni adult male worms |
title_full |
Human TNF-alpha induces differential protein phosphorylation in Schistosoma mansoni adult male worms |
title_fullStr |
Human TNF-alpha induces differential protein phosphorylation in Schistosoma mansoni adult male worms |
title_full_unstemmed |
Human TNF-alpha induces differential protein phosphorylation in Schistosoma mansoni adult male worms |
title_sort |
Human TNF-alpha induces differential protein phosphorylation in Schistosoma mansoni adult male worms |
author |
Oliveira, Katia C. [UNIFESP] |
author_facet |
Oliveira, Katia C. [UNIFESP] Carvalho, Mariana L. P. Bonatto, Jose Matheus C. Schechtman, Debora Verjovski-Almeida, Sergio |
author_role |
author |
author2 |
Carvalho, Mariana L. P. Bonatto, Jose Matheus C. Schechtman, Debora Verjovski-Almeida, Sergio |
author2_role |
author author author author |
dc.contributor.author.fl_str_mv |
Oliveira, Katia C. [UNIFESP] Carvalho, Mariana L. P. Bonatto, Jose Matheus C. Schechtman, Debora Verjovski-Almeida, Sergio |
dc.subject.eng.fl_str_mv |
Schistosoma mansoni Human TNF-alpha Signaling Phosphoproteomic analysis Mass spectrometry Host-parasite interaction |
topic |
Schistosoma mansoni Human TNF-alpha Signaling Phosphoproteomic analysis Mass spectrometry Host-parasite interaction |
description |
Schistosoma 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. |
publishDate |
2016 |
dc.date.issued.fl_str_mv |
2016 |
dc.date.accessioned.fl_str_mv |
2020-11-03T14:40:30Z |
dc.date.available.fl_str_mv |
2020-11-03T14:40:30Z |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
format |
article |
status_str |
publishedVersion |
dc.identifier.citation.fl_str_mv |
Parasitology Research. New York, v. 115, n. 2, p. 817-828, 2016. |
dc.identifier.uri.fl_str_mv |
https://repositorio.unifesp.br/handle/11600/58595 https://doi.org/10.1007/s00436-015-4812-5 |
dc.identifier.issn.none.fl_str_mv |
0932-0113 |
dc.identifier.doi.none.fl_str_mv |
10.1007/s00436-015-4812-5 |
dc.identifier.wos.none.fl_str_mv |
WOS:000370868800041 |
identifier_str_mv |
Parasitology Research. New York, v. 115, n. 2, p. 817-828, 2016. 0932-0113 10.1007/s00436-015-4812-5 WOS:000370868800041 |
url |
https://repositorio.unifesp.br/handle/11600/58595 https://doi.org/10.1007/s00436-015-4812-5 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.ispartof.none.fl_str_mv |
Parasitology Research |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
817-828 |
dc.coverage.none.fl_str_mv |
New York |
dc.publisher.none.fl_str_mv |
Springer |
publisher.none.fl_str_mv |
Springer |
dc.source.none.fl_str_mv |
reponame:Repositório Institucional da UNIFESP instname:Universidade Federal de São Paulo (UNIFESP) instacron:UNIFESP |
instname_str |
Universidade Federal de São Paulo (UNIFESP) |
instacron_str |
UNIFESP |
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UNIFESP |
reponame_str |
Repositório Institucional da UNIFESP |
collection |
Repositório Institucional da UNIFESP |
repository.name.fl_str_mv |
Repositório Institucional da UNIFESP - Universidade Federal de São Paulo (UNIFESP) |
repository.mail.fl_str_mv |
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1802764152619401216 |