Schaeffer Evelyne, Flacher Vincent, Papageorgiou Vasiliki, Decossas Marion, Fauny Jean-Daniel, Krämer Melanie, Mueller Christopher G
Dermal CD14(+) Dendritic Cell and Macrophage Infection by Dengue Virus Is Stimulated by Interleukin-4 Article de journal
Dans: The Journal of Investigative Dermatology, vol. 135, no. 7, p. 1743–1751, 2015, ISSN: 1523-1747.
Résumé | Liens | BibTeX | Étiquettes: Abdominal Wall, Activation, Adhesion, adhesion molecules, Antigen-Presenting Cells, arbovirus, C-Type, Cell Adhesion, Cell Adhesion Molecules, Cell Surface, Cells, Chemistry, Confocal, Cultured, cytokine, Cytokines, cytology, Dendritic Cells, Dengue, Dengue virus, DERMAL DENDRITIC CELLS, Dermatitis, DERMIS, development, disease, Enzyme-Linked Immunosorbent Assay, Epidermal Cells, Epidermis, Human, Humans, ICAM-3, IL-4, Immunology, immunopathology, infection, Interleukin-4, Langerhans Cells, LECTIN, Lectins, Lymphocyte Activation, Macrophage, Macrophages, metabolism, Microscopy, pathogenicity, physiopathology, Receptor, Receptors, Scabies, Sensitivity and Specificity, Skin, Skin Diseases, SUBSETS, T CELL ACTIVATION, target, Team-Mueller, TNF ALPHA, Viral, viral Infection, Viral Load, virology, virus
@article{schaeffer_dermal_2015b,
title = {Dermal CD14(+) Dendritic Cell and Macrophage Infection by Dengue Virus Is Stimulated by Interleukin-4},
author = {Evelyne Schaeffer and Vincent Flacher and Vasiliki Papageorgiou and Marion Decossas and Jean-Daniel Fauny and Melanie Krämer and Christopher G Mueller},
doi = {10.1038/jid.2014.525},
issn = {1523-1747},
year = {2015},
date = {2015-07-01},
journal = {The Journal of Investigative Dermatology},
volume = {135},
number = {7},
pages = {1743--1751},
abstract = {Dengue virus (DENV) is responsible for the most prevalent arthropod-borne viral infection in humans. Events decisive for disease development occur in the skin after virus inoculation by the mosquito. Yet, the role of human dermis-resident immune cells in dengue infection and disease remains elusive. Here we investigated how dermal dendritic cells (dDCs) and macrophages (dMs) react to DENV and impact on immunopathology. We show that both CD1c(+) and CD14(+) dDC subsets were infected, but viral load greatly increased in CD14(+) dDCs upon IL-4 stimulation, which correlated with upregulation of virus-binding lectins Dendritic Cell-Specific Intercellular adhesion molecule-3-Grabbing Nonintegrin (DC-SIGN/CD209) and mannose receptor (CD206). IL-4 also enhanced T-cell activation by dDCs, which was further increased upon dengue infection. dMs purified from digested dermis were initially poorly infected but actively replicated the virus and produced TNF-α upon lectin upregulation in response to IL-4. DC-SIGN(+) cells are abundant in inflammatory skin with scabies infection or Th2-type dermatitis, suggesting that skin reactions to mosquito bites heighten the risk of infection and subsequent immunopathology. Our data identify dDCs and dMs as primary arbovirus target cells in humans and suggest that dDCs initiate a potent virus-directed T-cell response, whereas dMs fuel the inflammatory cascade characteristic of dengue fever.},
keywords = {Abdominal Wall, Activation, Adhesion, adhesion molecules, Antigen-Presenting Cells, arbovirus, C-Type, Cell Adhesion, Cell Adhesion Molecules, Cell Surface, Cells, Chemistry, Confocal, Cultured, cytokine, Cytokines, cytology, Dendritic Cells, Dengue, Dengue virus, DERMAL DENDRITIC CELLS, Dermatitis, DERMIS, development, disease, Enzyme-Linked Immunosorbent Assay, Epidermal Cells, Epidermis, Human, Humans, ICAM-3, IL-4, Immunology, immunopathology, infection, Interleukin-4, Langerhans Cells, LECTIN, Lectins, Lymphocyte Activation, Macrophage, Macrophages, metabolism, Microscopy, pathogenicity, physiopathology, Receptor, Receptors, Scabies, Sensitivity and Specificity, Skin, Skin Diseases, SUBSETS, T CELL ACTIVATION, target, Team-Mueller, TNF ALPHA, Viral, viral Infection, Viral Load, virology, virus},
pubstate = {published},
tppubtype = {article}
}
Schaeffer Evelyne, Flacher Vincent, Papageorgiou Vasiliki, Decossas Marion, Fauny Jean-Daniel, Krämer Melanie, Mueller Christopher G
Dermal CD14(+) Dendritic Cell and Macrophage Infection by Dengue Virus Is Stimulated by Interleukin-4 Article de journal
Dans: The Journal of Investigative Dermatology, vol. 135, no. 7, p. 1743–1751, 2015, ISSN: 1523-1747.
Résumé | Liens | BibTeX | Étiquettes: Abdominal Wall, Antigen-Presenting Cells, C-Type, Cell Adhesion Molecules, Cell Surface, Cells, Confocal, Cultured, Cytokines, Dengue, Dengue virus, Enzyme-Linked Immunosorbent Assay, Epidermis, Humans, I2CT, Imagerie, Interleukin-4, Langerhans Cells, Lectins, Lymphocyte Activation, Macrophages, Microscopy, Receptors, Sensitivity and Specificity, Skin Diseases, Team-Mueller, Viral
@article{schaeffer_dermal_2015,
title = {Dermal CD14(+) Dendritic Cell and Macrophage Infection by Dengue Virus Is Stimulated by Interleukin-4},
author = {Evelyne Schaeffer and Vincent Flacher and Vasiliki Papageorgiou and Marion Decossas and Jean-Daniel Fauny and Melanie Krämer and Christopher G Mueller},
doi = {10.1038/jid.2014.525},
issn = {1523-1747},
year = {2015},
date = {2015-01-01},
journal = {The Journal of Investigative Dermatology},
volume = {135},
number = {7},
pages = {1743--1751},
abstract = {Dengue virus (DENV) is responsible for the most prevalent arthropod-borne viral infection in humans. Events decisive for disease development occur in the skin after virus inoculation by the mosquito. Yet, the role of human dermis-resident immune cells in dengue infection and disease remains elusive. Here we investigated how dermal dendritic cells (dDCs) and macrophages (dMs) react to DENV and impact on immunopathology. We show that both CD1c(+) and CD14(+) dDC subsets were infected, but viral load greatly increased in CD14(+) dDCs upon IL-4 stimulation, which correlated with upregulation of virus-binding lectins Dendritic Cell-Specific Intercellular adhesion molecule-3-Grabbing Nonintegrin (DC-SIGN/CD209) and mannose receptor (CD206). IL-4 also enhanced T-cell activation by dDCs, which was further increased upon dengue infection. dMs purified from digested dermis were initially poorly infected but actively replicated the virus and produced TNF-α upon lectin upregulation in response to IL-4. DC-SIGN(+) cells are abundant in inflammatory skin with scabies infection or Th2-type dermatitis, suggesting that skin reactions to mosquito bites heighten the risk of infection and subsequent immunopathology. Our data identify dDCs and dMs as primary arbovirus target cells in humans and suggest that dDCs initiate a potent virus-directed T-cell response, whereas dMs fuel the inflammatory cascade characteristic of dengue fever.},
keywords = {Abdominal Wall, Antigen-Presenting Cells, C-Type, Cell Adhesion Molecules, Cell Surface, Cells, Confocal, Cultured, Cytokines, Dengue, Dengue virus, Enzyme-Linked Immunosorbent Assay, Epidermis, Humans, I2CT, Imagerie, Interleukin-4, Langerhans Cells, Lectins, Lymphocyte Activation, Macrophages, Microscopy, Receptors, Sensitivity and Specificity, Skin Diseases, Team-Mueller, Viral},
pubstate = {published},
tppubtype = {article}
}
Hammann P, Parmentier D, Cerciat M, Reimegård J, Helfer A-C, Boisset S, Guillier M, Vandenesch F, Wagner G E H, Romby P, Fechter P
A method to map changes in bacterial surface composition induced by regulatory RNAs in Escherichia coli and Staphylococcus aureus. Article de journal
Dans: Biochimie, vol. 106, p. 175–179, 2014, ISSN: 1638-6183 0300-9084, (Place: France).
Résumé | Liens | BibTeX | Étiquettes: Bacterial Outer Membrane Proteins/metabolism, Bacterial Proteins/*metabolism, Bacterial/genetics/*metabolism, Base Sequence, Carbocyanines/metabolism, Cell Membrane/*metabolism, Cell Wall/metabolism, Confocal, DIGE, Electrophoresis, Escherichia coli/genetics/*metabolism, Gel, Mass, Matrix-Assisted Laser Desorption-Ionization, Microscopy, Molecular Sequence Data, Non-coding RNAs, Post-transcriptional regulation, PPSE, Reproducibility of Results, RNA, Spectrometry, Staining and Labeling/methods, Staphylococcus aureus/genetics/*metabolism, Surface proteins, Two-Dimensional/methods
@article{hammann_method_2014,
title = {A method to map changes in bacterial surface composition induced by regulatory RNAs in Escherichia coli and Staphylococcus aureus.},
author = {P Hammann and D Parmentier and M Cerciat and J Reimegård and A-C Helfer and S Boisset and M Guillier and F Vandenesch and G E H Wagner and P Romby and P Fechter},
doi = {10.1016/j.biochi.2014.07.011},
issn = {1638-6183 0300-9084},
year = {2014},
date = {2014-01-01},
journal = {Biochimie},
volume = {106},
pages = {175--179},
abstract = {We have adapted a method to map cell surface proteins and to monitor the effect of specific regulatory RNAs on the surface composition of the bacteria. This method involves direct labeling of surface proteins of living bacteria using fluorescent dyes and a subsequent separation of the crude extract by 2D gel electrophoresis. The strategy yields a substantial enrichment in surface proteins over cytoplasmic proteins. We validated this method by monitoring the effect of the regulatory RNA MicA in Escherichia coli, which regulates the synthesis of several outer membrane proteins, and highlighted the role of Staphylococcus aureus RNAIII for the maintenance of cell wall integrity.},
note = {Place: France},
keywords = {Bacterial Outer Membrane Proteins/metabolism, Bacterial Proteins/*metabolism, Bacterial/genetics/*metabolism, Base Sequence, Carbocyanines/metabolism, Cell Membrane/*metabolism, Cell Wall/metabolism, Confocal, DIGE, Electrophoresis, Escherichia coli/genetics/*metabolism, Gel, Mass, Matrix-Assisted Laser Desorption-Ionization, Microscopy, Molecular Sequence Data, Non-coding RNAs, Post-transcriptional regulation, PPSE, Reproducibility of Results, RNA, Spectrometry, Staining and Labeling/methods, Staphylococcus aureus/genetics/*metabolism, Surface proteins, Two-Dimensional/methods},
pubstate = {published},
tppubtype = {article}
}
Serag Maged F, Kaji Noritada, Tokeshi Manabu, Bianco Alberto, Baba Yoshinobu
The plant cell uses carbon nanotubes to build tracheary elements Article de journal
Dans: Integrative Biology: Quantitative Biosciences from Nano to Macro, vol. 4, no. 2, p. 127–131, 2012, ISSN: 1757-9708.
Résumé | Liens | BibTeX | Étiquettes: Arabidopsis, Atomic Force, carbon, Cell Differentiation, Confocal, Endocytosis, I2CT, Lignin, Microscopy, Nanotubes, Plant Cells, Team-Bianco
@article{serag_plant_2012,
title = {The plant cell uses carbon nanotubes to build tracheary elements},
author = {Maged F Serag and Noritada Kaji and Manabu Tokeshi and Alberto Bianco and Yoshinobu Baba},
doi = {10.1039/c2ib00135g},
issn = {1757-9708},
year = {2012},
date = {2012-02-01},
journal = {Integrative Biology: Quantitative Biosciences from Nano to Macro},
volume = {4},
number = {2},
pages = {127--131},
abstract = {Since their discovery, carbon nanotubes (CNTs) have been eminent members of the nanomaterial family. Because of their unique physical, chemical and mechanical properties, they are regarded as new potential materials to bring enormous benefits in cell biology studies. Undoubtedly, the first step to prove the advantages of CNTs is to understand the basic behavior of CNTs inside the cells. In a number of studies, CNTs have been demonstrated as new carrier systems for the delivery of DNA, proteins and therapeutic molecules into living cells. However, post-uptake behavior of CNTs inside the cells has not received much consideration. Utilizing the plant cell model, we have shown in this study that the plant cells, differentiating into tracheary elements, incorporate cup-stacked carbon nanotubes (CSCNTs) into cell structure via oxidative cross-linking of monolignols to the nanotubes surface during lignin biosynthesis. This finding highlights the fate of CNTs inside plant cells and provides an example on how the plant cell can handle internalized carbon nanomaterials.},
keywords = {Arabidopsis, Atomic Force, carbon, Cell Differentiation, Confocal, Endocytosis, I2CT, Lignin, Microscopy, Nanotubes, Plant Cells, Team-Bianco},
pubstate = {published},
tppubtype = {article}
}
Pantarotto Davide, Briand Jean-Paul, Prato Maurizio, Bianco Alberto
Translocation of bioactive peptides across cell membranes by carbon nanotubes Article de journal
Dans: Chemical Communications (Cambridge, England), no. 1, p. 16–17, 2004, ISSN: 1359-7345.
Résumé | Liens | BibTeX | Étiquettes: 3T3 Cells, Animals, carbon, Cell Membrane, Confocal, Flow Cytometry, fluorescence, I2CT, Mice, Microscopy, Nanotubes, Particle Size, Peptides, Protein Transport, Team-Bianco
@article{pantarotto_translocation_2004,
title = {Translocation of bioactive peptides across cell membranes by carbon nanotubes},
author = {Davide Pantarotto and Jean-Paul Briand and Maurizio Prato and Alberto Bianco},
doi = {10.1039/b311254c},
issn = {1359-7345},
year = {2004},
date = {2004-01-01},
journal = {Chemical Communications (Cambridge, England)},
number = {1},
pages = {16--17},
abstract = {Functionalised carbon nanotubes are able to cross the cell membrane and to accumulate in the cytoplasm or reach the nucleus without being toxic for the cell up to 10 [micro sign]M.},
keywords = {3T3 Cells, Animals, carbon, Cell Membrane, Confocal, Flow Cytometry, fluorescence, I2CT, Mice, Microscopy, Nanotubes, Particle Size, Peptides, Protein Transport, Team-Bianco},
pubstate = {published},
tppubtype = {article}
}
Nisole S, Krust B, Callebaut C, Guichard G, Muller S, Briand J P, Hovanessian A G
The anti-HIV pseudopeptide HB-19 forms a complex with the cell-surface-expressed nucleolin independent of heparan sulfate proteoglycans Article de journal
Dans: The Journal of Biological Chemistry, vol. 274, no. 39, p. 27875–27884, 1999, ISSN: 0021-9258.
Résumé | Liens | BibTeX | Étiquettes: Anti-HIV Agents, Binding Sites, CD4-Positive T-Lymphocytes, Cell Line, Cell Membrane, Confocal, Fibroblast Growth Factor 2, Flow Cytometry, Heparan Sulfate Proteoglycans, HIV-1, Humans, Microscopy, Oligopeptides, Peptides, Phospholipid Ethers, Phosphoproteins, Proteins, RNA-Binding Proteins
@article{nisole_anti-hiv_1999,
title = {The anti-HIV pseudopeptide HB-19 forms a complex with the cell-surface-expressed nucleolin independent of heparan sulfate proteoglycans},
author = {S Nisole and B Krust and C Callebaut and G Guichard and S Muller and J P Briand and A G Hovanessian},
doi = {10.1074/jbc.274.39.27875},
issn = {0021-9258},
year = {1999},
date = {1999-09-01},
journal = {The Journal of Biological Chemistry},
volume = {274},
number = {39},
pages = {27875--27884},
abstract = {The HB-19 pseudopeptide 5[Kpsi(CH(2)N)PR]-TASP, psi(CH(2)N) for reduced peptide bond, is a specific inhibitor of human immunodeficiency virus (HIV) infection in different CD4(+) cell lines and in primary T-lymphocytes and macrophages. Here, by using an experimental CD4(+) cell model to monitor HIV entry and infection, we demonstrate that HB-19 binds the cell surface and inhibits attachment of HIV particles to permissive cells. At concentrations that inhibit HIV attachment, HB-19 binds cells irreversibly, becomes complexed with the cell-surface-expressed nucleolin, and eventually results in its degradation. Accordingly, by confocal immunofluorescence microscopy, we demonstrate the drastic reduction of the cell-surface-expressed nucleolin following treatment of cells with HB-19. HIV particles can prevent the binding of HB-19 to cells and inhibit complex formation with nucleolin. Such a competition between viral particles and HB-19 is consistent with the implication of nucleolin in the process of HIV attachment to target cells. We show that another inhibitor of HIV infection, the fibroblast growth factor-2 (FGF-2) that uses cell-surface-expressed heparan sulfate proteoglycans as low affinity receptors, binds cells and blocks attachment of HIV to permissive cells. FGF-2 does not prevent the binding of HB-19 to cells and to nucleolin, and similarly HB-19 has no apparent effect on the binding of FGF-2 to the cell surface. The lack of competition between these two anti-HIV agents rules out the potential involvement of heparan sulfate proteoglycans in the mechanism of anti-HIV effect of HB-19, thus pointing out that nucleolin is its main target.},
keywords = {Anti-HIV Agents, Binding Sites, CD4-Positive T-Lymphocytes, Cell Line, Cell Membrane, Confocal, Fibroblast Growth Factor 2, Flow Cytometry, Heparan Sulfate Proteoglycans, HIV-1, Humans, Microscopy, Oligopeptides, Peptides, Phospholipid Ethers, Phosphoproteins, Proteins, RNA-Binding Proteins},
pubstate = {published},
tppubtype = {article}
}