Human TNF-α induces differential protein phosphorylation in Schistosoma mansoni adult male worms
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- 作者：Katia C. Oliveira ; Mariana L. P. Carvalho ; José Matheus C. Bonatto…
- 关键词：Schistosoma mansoni ; Human TNF ; α ; Signaling ; Phosphoproteomic analysis ; Mass spectrometry ; Host ; parasite interaction
- 刊名：Parasitology Research
- 出版年：2016
- 出版时间：February 2016
- 年：2016
- 卷：115
- 期：2
- 页码：817-828
- 全文大小：1,267 KB
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Mariana L. P. Carvalho (2)
José Matheus C. Bonatto (2)
Debora Schechtman (2)
Sergio Verjovski-Almeida (2) (3)
1. Núcleo de Enteroparasitas, Centro de Parasitologia e Micologia, Instituto Adolfo Lutz, 01614-000, São Paulo, SP, Brazil
4. Disciplina de Parasitologia, Departamento de Microbiologia, Imunologia e Parasitologia, Universidade Federal de São Paulo, São Paulo, Brazil
2. Departamento de Bioquímica, Instituto de Química, Universidade de São Paulo, 05508-900, São Paulo, SP, Brazil
3. Instituto Butantan, 05503-900, São Paulo, SP, Brazil - 刊物类别：Biomedical and Life Sciences
- 刊物主题：Biomedicine
Medical Microbiology
Microbiology
Immunology - 出版者：Springer Berlin / Heidelberg
- ISSN：1432-1955
文摘
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-α), 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-α activity in worms are not completely understood. Here, we aimed at exploring the effect of hTNF-α 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-α and successfully identified 32 protein spots with a statistically significant increase in phosphorylation upon in vitro exposure to hTNF-α. 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-α signaling, thus suggesting that TNF-α 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. Keywords Schistosoma mansoni Human TNF-α Signaling Phosphoproteomic analysis Mass spectrometry Host-parasite interaction