Streptococcus pneumoniae Infection Promotes Histone H3 Dephosphorylation by Modulating Host PP1 Phosphatase
| العنوان: | Streptococcus pneumoniae Infection Promotes Histone H3 Dephosphorylation by Modulating Host PP1 Phosphatase |
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| المؤلفون: | Michael G. Connor, Matthew J. G. Eldridge, Christine Chevalier, Melanie Hamon, Orhan Rasid, Wenyang Dong |
| المساهمون: | Chromatine et Infection - Chromatin and Infection, Institut Pasteur [Paris] (IP), Université Sorbonne Paris Cité (USPC), Work in the M.A.H. laboratory received financial support from Institut Pasteur and the National Research Agency (ANR-EPIBACTIN). W.D. is part of the Pasteur-Paris University (PPU) International PhD Program, a project which has received funding from the European Union’s Horizon 2020 research and innovation programme under the Marie Sklodowska-Curie grant agreement 665807. W.D. is supported by the EUR G.E.N.E. (reference ANR-17-EURE-0013) and is part of the Université de Paris IdEx ANR-18-IDEX-0001 funded by the French government through its 'Investments for the Future' program. M.C. is supported by the Pasteur Foundation Fellowship. M.J.G.E. is supported by a fellowship from the French Government’s Investissement d’Avenir program, the Laboratoire d’Excellence 'Integrative Biology of Emerging Infectious Diseases' (ANR-10-LABX-62-IBEID)., ANR-17-CE12-0007,EpiBactIn,Modifications epigenomiques induites par l'interaction hote-bacteries(2017), ANR-18-IDEX-0001,Université de Paris,Université de Paris(2018), ANR-10-LABX-0062,IBEID,Integrative Biology of Emerging Infectious Diseases(2010), European Project: 665807,H2020,H2020-MSCA-COFUND-2014,PASTEURDOC(2015), Institut Pasteur [Paris] |
| المصدر: | Cell Reports, Vol 30, Iss 12, Pp 4016-4026.e4 (2020) Cell Reports Cell Reports, 2020, 30 (12), pp.4016-4026.e4. ⟨10.1016/j.celrep.2020.02.116⟩ Cell Reports, Elsevier Inc, 2020, 30 (12), pp.4016-4026.e4. ⟨10.1016/j.celrep.2020.02.116⟩ |
| بيانات النشر: | Elsevier, 2020. |
| سنة النشر: | 2020 |
| مصطلحات موضوعية: | 0301 basic medicine, Transcription, Genetic, [SDV.BC.BC]Life Sciences [q-bio]/Cellular Biology/Subcellular Processes [q-bio.SC], medicine.disease_cause, Histones, Serine, Phosphoserine, 0302 clinical medicine, Phosphoprotein Phosphatases, histone modification, Phosphorylation, lcsh:QH301-705.5, Epigenomics, 0303 health sciences, biology, Chemistry, [SDV.BBM.MN]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Molecular Networks [q-bio.MN], pneumolysin, Cell biology, 3. Good health, Histone, Streptococcus pneumoniae, Host-Pathogen Interactions, Streptolysins, Female, Intracellular, Phosphatase, Pneumococcal Infections, General Biochemistry, Genetics and Molecular Biology, Cell Line, Microbiology, Dephosphorylation, 03 medical and health sciences, Histone H3, Bacterial Proteins, protein phosphatase 1, medicine, Animals, Humans, 030304 developmental biology, Inflammation, Pneumolysin, 030306 microbiology, bacterial infection, Protein phosphatase 1, SpxB, [SDV.BBM.BM]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Molecular biology, Gene Expression Regulation, Bacterial, Hydrogen Peroxide, [SDV.MP.BAC]Life Sciences [q-bio]/Microbiology and Parasitology/Bacteriology, Mice, Inbred C57BL, 030104 developmental biology, H3S10 dephosphorylation, lcsh:Biology (General), biology.protein, 030217 neurology & neurosurgery |
| الوصف: | Summary: Pathogenic bacteria can alter host gene expression through post-translational modifications of histones. We show that a natural colonizer, Streptococcus pneumoniae, induces specific histone modifications, including robust dephosphorylation of histone H3 on serine 10 (H3S10), during infection of respiratory epithelial cells. The bacterial pore-forming toxin pneumolysin (PLY), along with the pyruvate oxidase SpxB responsible for H2O2 production, play important roles in the induction of this modification. The combined effects of PLY and H2O2 trigger host signaling that culminates in H3S10 dephosphorylation, which is mediated by the host cell phosphatase PP1. Strikingly, S. pneumoniae infection induces dephosphorylation and subsequent activation of PP1 catalytic activity. Colonization of PP1 catalytically deficient cells results in impaired intracellular S. pneumoniae survival and infection. Interestingly, PP1 activation and H3S10 dephosphorylation are not restricted to S. pneumoniae and appear to be general epigenomic mechanisms favoring intracellular survival of pathogenic bacteria. : Dong et al. show that Streptococcus pneumoniae infection induces histone H3 dephosphorylation in lung epithelial cells, through two bacterial factors, PLY and SpxB. Infection-triggered activation of the host phosphatase PP1 is required for this histone modification and efficient intracellular infection. Keywords: histone modification, Streptococcus pneumoniae, H3S10 dephosphorylation, protein phosphatase 1, bacterial infection, pneumolysin, SpxB |
| وصف الملف: | application/pdf |
| اللغة: | English |
| تدمد: | 2211-1247 |
| URL الوصول: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0c8a5494392fa38b603bb32ece2cd923 http://www.sciencedirect.com/science/article/pii/S2211124720302977 |
| حقوق: | OPEN |
| رقم الأكسشن: | edsair.doi.dedup.....0c8a5494392fa38b603bb32ece2cd923 |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 22111247 |
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