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1. Cryo-electron microscopy three-dimensional structure of the jumbo phage ΦRSL1 infecting the phytopathogen Ralstonia solanacearum

Author

Takeru Kawasaki, Maria Bacia, Grégory Effantin, Takashi Yamada, Ryosuke Hamasaki, Winfried Weissenhorn, Guy Schoehn, Christine Moriscot, Unit for Virus Host-Cell Interactions [Grenoble] (UVHCI), Centre National de la Recherche Scientifique (CNRS)-European Molecular Biology Laboratory [Grenoble] (EMBL)-Université Joseph Fourier - Grenoble 1 (UJF), Centre Science des Matériaux et des Structures (SMS-ENSMSE), École des Mines de Saint-Étienne (Mines Saint-Étienne MSE), Institut Mines-Télécom [Paris] (IMT)-Institut Mines-Télécom [Paris] (IMT), Unité Mixte de Thérapie Cellulaire et Tissulaire, CHU Grenoble, Unité de Biochimie des Cancers et Biothérapies, Institut de biologie structurale (IBS - UMR 5075 ), Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS), Université Joseph Fourier - Grenoble 1 (UJF)-European Molecular Biology Laboratory [Grenoble] (EMBL)-Centre National de la Recherche Scientifique (CNRS), Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), and Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)

Subjects
Models, Molecular, MESH: Protein Structure, Quaternary, Cryo-electron microscopy, MESH: Ralstonia solanacearum, Myoviridae, 03 medical and health sciences, Protein structure, Capsid, Structural Biology, MESH: Capsid, Bacteriophages, MESH: Bacteriophages, MESH: Viral Tail Proteins, Protein Structure, Quaternary, Molecular Biology, MESH: Capsid Proteins, 030304 developmental biology, Appendage, Host cell surface, 0303 health sciences, Ralstonia solanacearum, [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Structural Biology [q-bio.BM], biology, 030306 microbiology, Cryoelectron Microscopy, Viral Tail Proteins, biology.organism_classification, Virology, Biophysics, Capsid Proteins, MESH: Cryoelectron Microscopy, MESH: Models, Molecular, Bacteria
Abstract

International audience; ϕRSL1 jumbo phage belongs to a new class of viruses within the Myoviridae family. Here, we report its three-dimensional structure determined by electron cryo microscopy. The icosahedral capsid, the tail helical portion, and the complete tail appendage were reconstructed separately to resolutions of 9 Å, 9 Å, and 28 Å, respectively. The head is rather complex and formed by at least five different proteins, whereas the major capsid proteins resemble those from HK97, despite low sequence conservation. The helical tail structure demonstrates its close relationship to T4 sheath proteins and provides evidence for an evolutionary link of the inner tail tube to the bacterial type VI secretion apparatus. Long fibers extend from the collar region, and their length is consistent with reaching the host cell surface upon tail contraction. Our structural analyses indicate that ϕRSL1 is an unusual member of the Myoviridae that employs conserved protein machines related to different phages and bacteria.

Published
2012

2. Magnetic resonance imaging and fluorescence labeling of clinical-grade mesenchymal stem cells without impacting their phenotype: study in a rat model of stroke

Author

Christoph Segebarth, Marie-Jeanne Richard, C. Moriscot, Anaïck Moisan, Olivier Detante, Emmanuelle Grillon, Emmanuel L. Barbier, Chantal Rémy, Josiane Arnaud, Samuel Valable, Florence de Fraipont, Marc Hommel, INSERM U836, équipe 5, Neuroimagerie fonctionnelle et perfusion cérébrale, Grenoble Institut des Neurosciences (GIN), Université Joseph Fourier - Grenoble 1 (UJF)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Joseph Fourier - Grenoble 1 (UJF)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Unité neuro-vascularie, neurologie, CHU Grenoble-CHU Grenoble, Université Joseph Fourier - Grenoble 1 (UJF)-Institut National de la Santé et de la Recherche Médicale (INSERM), Institut d'oncologie/développement Albert Bonniot de Grenoble (INSERM U823), Université Joseph Fourier - Grenoble 1 (UJF)-CHU Grenoble-EFS-Institut National de la Santé et de la Recherche Médicale (INSERM), Unité de Biochimie des Cancers et Biothérapies, CHU Grenoble, Neuro-imagerie fonctionnelle et métabolique (ANTE-INSERM U836, équipe 5), Université Joseph Fourier - Grenoble 1 (UJF)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Joseph Fourier - Grenoble 1 (UJF)-Institut National de la Santé et de la Recherche Médicale (INSERM), Biochimie Hormonale et Nutritionnelle, Université Joseph Fourier - Grenoble 1 (UJF)-CHU Grenoble, Unité Mixte de Thérapie Cellulaire et Tissulaire, CIC - Grenoble, O.D. was the recipient of an INSERM grant, INSERM/Direction de l'Hospitalisation et de l'Organisation des Soins grant, Clinical Research Department of Grenoble University Hospital, J. Fourier Grenoble University Vivier de la Recherche Médicale grant, and Dojat, Michel

Subjects
Male, Pathology, medicine.medical_specialty, Transplantation, Heterologous, [INFO.INFO-IM] Computer Science [cs]/Medical Imaging, Biology, Mesenchymal Stem Cell Transplantation, Ferric Compounds, Rats, Sprague-Dawley, Cell therapy, 03 medical and health sciences, 0302 clinical medicine, In vivo, medicine, [INFO.INFO-IM]Computer Science [cs]/Medical Imaging, Animals, Humans, Cell migration, Viability assay, [SDV.NEU] Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC], Original Articles and Reviews, Cell damage, Fluorescent Dyes, 030304 developmental biology, 0303 health sciences, In vivo tracking, medicine.diagnostic_test, Mesenchymal stem cell, Magnetic resonance imaging, Cell Biology, General Medicine, medicine.disease, equipment and supplies, Magnetic Resonance Imaging, Rats, 3. Good health, Cell biology, Stroke, Transplantation, Disease Models, Animal, Microscopy, Fluorescence, Mesenchymal stem cells, [SDV.NEU]Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC], Cell culture, Stem cell, 030217 neurology & neurosurgery, Developmental Biology
Abstract

Human mesenchymal stem cells (hMSCs) have strong potential for cell therapy after stroke. Tracking stem cells in vivo following a graft can provide insight into many issues regarding optimal route and/or dosing. hMSCs were labeled for magnetic resonance imaging (MRI) and histology with micrometer-sized superparamagnetic iron oxides (M-SPIOs) that contained a fluorophore. We assessed whether M-SPIO labeling obtained without the use of a transfection agent induced any cell damage in clinical-grade hMSCs and whether it may be useful for in vivo MRI studies after stroke. M-SPIOs provided efficient intracellular hMSC labeling and did not modify cell viability, phenotype, or in vitro differentiation capacity. Following grafting in a rat model of stroke, labeled hMSCs could be detected using both in vivo MRI and fluorescent microscopy until 4 weeks following transplantation. However, whereas good label stability and unaffected hMSC viability were observed in vitro, grafted hMSCs may die and release iron particles in vivo.

Published
2012
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3. M-ficolin interacts with the long pentraxin PTX3: a novel case of cross-talk between soluble pattern-recognition molecules

Author

Gérard J. Arlaud, Christine Moriscot, Andrea Doni, Guy Schoehn, Chantal Dumestre-Pérard, Nicole M. Thielens, Monique Lacroix, Evelyne Gout, Julien Pérard, Alberto Mantovani, Institut de biologie structurale (IBS - UMR 5075 ), Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA), Unité de Biochimie des Cancers et Biothérapies, CHU Grenoble, Unité Mixte de Thérapie Cellulaire et Tissulaire, Laboratoire Adaptation et pathogénie des micro-organismes [Grenoble] (LAPM), Université Joseph Fourier - Grenoble 1 (UJF)-Centre National de la Recherche Scientifique (CNRS), Unit for Virus Host-Cell Interactions [Grenoble] (UVHCI), Université Joseph Fourier - Grenoble 1 (UJF)-European Molecular Biology Laboratory [Grenoble] (EMBL)-Centre National de la Recherche Scientifique (CNRS), Humanitas Clinical and Research Institute, Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS), Centre National de la Recherche Scientifique (CNRS)-Université Joseph Fourier - Grenoble 1 (UJF), and Centre National de la Recherche Scientifique (CNRS)-European Molecular Biology Laboratory [Grenoble] (EMBL)-Université Joseph Fourier - Grenoble 1 (UJF)

Subjects
MESH: Signal Transduction, MESH: Serum Amyloid P-Component, Ligands, chemistry.chemical_compound, MESH: Protein Structure, Tertiary, MESH: Mutant Proteins, 0302 clinical medicine, MESH: Lectins, Lectins, MESH: Ligands, Immunology and Allergy, MESH: Immunity, Humoral, 0303 health sciences, biology, MESH: Acetylglucosamine, PTX3, Cell biology, MESH: Surface Plasmon Resonance, Serum Amyloid P-Component, C-Reactive Protein, [SDV.MP]Life Sciences [q-bio]/Microbiology and Parasitology, Biochemistry, MESH: Calcium, MESH: N-Acetylneuraminic Acid, Ficolin, Protein Binding, Signal Transduction, MESH: Immune Tolerance, Immunology, MESH: Microscopy, Electron, Acetylglucosamine, 03 medical and health sciences, Tetramer, MESH: C-Reactive Protein, Immune Tolerance, Humans, MESH: Protein Binding, 030304 developmental biology, Innate immune system, MESH: Humans, Pentraxins, Lectin, Surface Plasmon Resonance, N-Acetylneuraminic Acid, Immunity, Humoral, Protein Structure, Tertiary, Sialic acid, Complement system, Microscopy, Electron, chemistry, biology.protein, Calcium, Mutant Proteins, 030215 immunology
Abstract

Ficolins and pentraxins are soluble oligomeric pattern-recognition molecules that sense danger signals from pathogens and altered self-cells and might act synergistically in innate immune defense and maintenance of immune tolerance. The interaction of M-ficolin with the long pentraxin pentraxin 3 (PTX3) has been characterized using surface plasmon resonance spectroscopy and electron microscopy. M-ficolin was shown to bind PTX3 with high affinity in the presence of calcium ions. The interaction was abolished in the presence of EDTA and inhibited by N-acetyl-D-glucosamine, indicating involvement of the fibrinogen-like domain of M-ficolin. Removal of sialic acid from the single N-linked carbohydrate of the C-terminal domain of PTX3 abolished the interaction. Likewise, an M-ficolin mutant with impaired sialic acid-binding ability did not interact with PTX3. Interaction was also impaired when using the isolated recognition domain of M-ficolin or the monomeric C-terminal domain of PTX3, indicating requirement for oligomerization of both proteins. Electron microscopy analysis of the M-ficolin–PTX3 complexes revealed that the M-ficolin tetramer bound up to four PTX3 molecules. From a functional point of view, immobilized PTX3 was able to trigger M-ficolin–dependent activation of the lectin complement pathway. These data indicate that interaction of M-ficolin with PTX3 arises from its ability to bind sialylated ligands and thus differs from the binding to the short pentraxin C-reactive protein and from the binding of L-ficolin to PTX3. The M-ficolin–PTX3 interaction described in this study represents a novel case of cross-talk between soluble pattern-recognition molecules, lending further credit to the integrated view of humoral innate immunity that emerged recently.

Published
2011
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4. Plasmacytoid dendritic cells and dermatological disorders: focus on their role in autoimmunity and cancer

Author

Joel Plumas, Marie-Jeanne Richard, Jeremy Di Domizio, Laurence Chaperot, Julie Charles, Remy Gressin, Caroline Aspord, Marie-Christine Jacob, Dimitri Salameire, Jean-Claude Beani, Marie-Thérèse Leccia, Institut d'oncologie/développement Albert Bonniot de Grenoble (INSERM U823), Université Joseph Fourier - Grenoble 1 (UJF)-CHU Grenoble-EFS-Institut National de la Santé et de la Recherche Médicale (INSERM), Laboratoire recherche et développement, EFS, Département Pluridisciplinaire de Médecine, Dermatologie, CHU Grenoble-Hôpital Michallon, Département d'anatomie et cythologie pathologique, INSERM U823, équipe 9 (Immunobiologie et Immunothérapie des Cancers), Université Joseph Fourier - Grenoble 1 (UJF)-CHU Grenoble-EFS-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Joseph Fourier - Grenoble 1 (UJF)-CHU Grenoble-EFS-Institut National de la Santé et de la Recherche Médicale (INSERM)-Laboratoire recherche et développement, INSERM U823, équipe 7 (Voies Oncogéniques Des Hémopathies Malignes), Université Joseph Fourier - Grenoble 1 (UJF)-CHU Grenoble-EFS-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Joseph Fourier - Grenoble 1 (UJF)-CHU Grenoble-EFS-Institut National de la Santé et de la Recherche Médicale (INSERM)-Département de cancérologie et d'hématologie, CHU Grenoble-Hôpital Michallon-Hôpital Michallon, Laboratoire d'Immunocytologie, Unité Mixte de Thérapie Cellulaire et Tissulaire, CHU Grenoble-EFS-UJF, and Chaperot, Laurence

Subjects
Skin Neoplasms, Myeloid, [SDV.IMM] Life Sciences [q-bio]/Immunology, Alpha interferon, MESH: Skin Diseases, Dermatology, Plasmacytoid dendritic cell, medicine.disease_cause, Skin Diseases, Article, Autoimmune Diseases, Autoimmunity, 030207 dermatology & venereal diseases, 03 medical and health sciences, 0302 clinical medicine, MESH: Autoimmune Diseases, medicine, Humans, Antigen-presenting cell, 030304 developmental biology, 0303 health sciences, Toll-like receptor, MESH: Humans, MESH: Dendritic Cells, business.industry, MESH: Skin Neoplasms, Interferon-alpha, Dendritic Cells, Dendritic cell, Acquired immune system, 3. Good health, medicine.anatomical_structure, Immunology, [SDV.IMM]Life Sciences [q-bio]/Immunology, MESH: Interferon-alpha, business
Abstract

International audience; Dendritic cells (DC), considered as immunological sentinels of the organism since they are antigen presenting cells, create the link between innate and adaptive immunity. DC include myeloid dendritic cells (MDC) and plasmacytoid dendritic cells (PDC). The presence of PDC, cells capable of producing large quantities of interferon alpha (IFN-alpha) in response to pathogenic agents or danger signals, seems to be closely related to pathological conditions. PDC have been observed in inflammatory immunoallergic dermatological disorders, in malignant cutaneous tumours and in cutaneous lesions of infectious origin. They seem to play a crucial role in the initiation of the pathological processes of autoimmune diseases such as lupus or psoriasis. Their function within a tumour context is not as well known and is controversial. They could have a tolerogenic role towards tumour cells in the absence of an activator but they also have the capacity to become activated in response to Toll-like receptor (TLR) ligands and could therefore be useful for therapeutic purposes.

Published
2010
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5. Intravenous administration of 99mTc-HMPAO-labeled human mesenchymal stem cells after stroke: in vivo imaging and biodistribution

Author

Julien Dimastromatteo, Marie-Jeanne Richard, Laurent Riou, Christoph Segebarth, Emmanuel L. Barbier, Catherine Ghezzi, Chantal Rémy, Anaïck Moisan, Emmanuelle Grillon, Olivier Detante, Marie-Dominique Desruet, Assia Jaillard, Florence de Fraipont, Marc Hommel, Grenoble Institut des Neurosciences (GIN), Université Joseph Fourier - Grenoble 1 (UJF)-Institut National de la Santé et de la Recherche Médicale (INSERM), Unité Neuro-Vasculaire, CHU Grenoble, Radiopharmaceutiques biocliniques, Service de Biophysique et Médecine Nucléaire, Eras Labo, Institut d'oncologie/développement Albert Bonniot de Grenoble (INSERM U823), Université Joseph Fourier - Grenoble 1 (UJF)-CHU Grenoble-EFS-Institut National de la Santé et de la Recherche Médicale (INSERM), Unité Mixte de Thérapie Cellulaire et Tissulaire, CHU Grenoble-EFS-UJF, Unité de Cancérologie Biologique et biothérapies, INSERM U823, équipe 5 (cibles diagnostiques ou thérapeutiques et vectorisation de drogues dans le cancer du poumon), Université Joseph Fourier - Grenoble 1 (UJF)-CHU Grenoble-EFS-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Joseph Fourier - Grenoble 1 (UJF)-CHU Grenoble-EFS-Institut National de la Santé et de la Recherche Médicale (INSERM)-Unité de Cancérologie Biologique et biothérapies, Unité d'Imagerie par Résonance Magnétique, CIC - Grenoble, INSERM 'Association Nationale de la Recherche Technique (ANRT)' INSERM/DHOS J. Fourier Grenoble University 'UJF-Vivier de la Recherche Medicale', and Dojat, Michel

Subjects
Pathology, MESH: Rats, Sprague-Dawley, Whole-Body Counting, MESH: Technetium Tc 99m Exametazime, MESH: Magnetic Resonance Imaging, Cell therapy, Brain ischemia, Rats, Sprague-Dawley, 0302 clinical medicine, Biodistribution, MESH: Whole-Body Counting, Tissue Distribution, MESH: Animals, 0303 health sciences, Magnetic Resonance Imaging, 3. Good health, Stroke, medicine.anatomical_structure, Injections, Intravenous, [SDV.IB]Life Sciences [q-bio]/Bioengineering, Nuclear imaging, Preclinical imaging, MESH: Radiopharmaceuticals, medicine.medical_specialty, [SDV.OT]Life Sciences [q-bio]/Other [q-bio.OT], MESH: Rats, Biomedical Engineering, Spleen, Human mesenchymal stem cell (hMSC), Mesenchymal Stem Cell Transplantation, MESH: Stroke, 03 medical and health sciences, Technetium Tc 99m Exametazime, medicine, Animals, Humans, MESH: Mesenchymal Stem Cell Transplantation, MESH: Tissue Distribution, 030304 developmental biology, [SDV.IB] Life Sciences [q-bio]/Bioengineering, Transplantation, Lung, MESH: Humans, [SDV.OT] Life Sciences [q-bio]/Other [q-bio.OT], business.industry, Mesenchymal stem cell, Histology, Mesenchymal Stem Cells, Cell Biology, medicine.disease, equipment and supplies, MESH: Injections, Intravenous, Rats, MESH: Mesenchymal Stem Cells, Radiopharmaceuticals, Cell transplantation, business, 030217 neurology & neurosurgery
Abstract

Human mesenchymal stem cells (hMSC) are a promising source for cell therapy after stroke. To deliver these cells, an IV injection appears safer than a local graft. We aimed to assess the whole-body biodistribution of IV-injected 99mTc-HMPAO-labeled hMSC in normal rats ( n = 9) and following a right middle cerebral artery occlusion (MCAo, n = 9). Whole-body nuclear imaging, isolated organ counting (at 2 and 20 h after injection) and histology were performed. A higher activity was observed in the right damaged hemisphere of the MCAo group [6.5 ± 0.9 × 10−3 % of injected dose (ID)/g] than in the control group (3.6 ± 1.2 × 10−3 %ID/g), 20 h after injection. In MCAo rats, right hemisphere activity was higher than that observed in the contralateral hemisphere at 2 h after injection (11.6 ± 2.8 vs. 9.8 ± 1.7 × 10−3 %ID/g). Following an initial hMSC lung accumulation, there was a decrease in pulmonary activity from 2 to 20 h after injection in both groups. The spleen was the only organ in which activity increased between 2 and 20 h. The presence of hMSC was documented in the spleen, liver, lung, and brain following histology. IV-injected hMSC are transiently trapped in the lungs, can be sequestered in the spleen, and are predominantly eliminated by kidneys. After 20 h, more hMSC are found in the ischemic lesion than into the undamaged cerebral tissue. IV delivery of hMSC could be the initial route for a clinical trial of tolerance.

Published
2009
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6. An interaction between CD16 and CR3 enhances iC3b binding to CR3 but is lost during differentiation of monocytes into dendritic cells.

Author

Preynat-Seauve O, Villiers CL, Jourdan G, Richard MJ, Plumas J, Favier A, Marche PN, and Favrot MC

Subjects
Apoptosis physiology, Cell Differentiation physiology, Flow Cytometry, Humans, Macrophages physiology, Phagocytosis physiology, Complement C3b metabolism, Dendritic Cells metabolism, Macrophage-1 Antigen metabolism, Monocytes metabolism, Receptors, IgG metabolism
Abstract

The receptor for the iC3b fragment of complement, CR3, is involved in monocytes/macrophages and neutrophils phagocytosis. CR3 is known to interact with the low affinity receptor for Ig (CD16) and previous studies have suggested that this cooperation modulates CR3 functions. Herein we have studied the effect of CD16 on the ability of human monocytes CR3 to bind to iC3b. We show that iC3b binding to CR3 is inhibited by several reagents that are known to dissociate the CD16/CR3 complex. In addition, treatment of monocytes with soluble CD16 inhibited iC3b binding to CR3. Together, these data indicate that iC3b binding to monocyte CR3 is up-regulated by an interaction between membrane CD16 and CR3. The implication of CD16 in CR3 binding to iC3b was also analyzed after monocyte differentiation into dendritic cells (DC). Differentiation of monocytes into DC abrogates the cooperation between CD16 and CR3, due to a loss of CD16/CR3 interaction. In accordance, this phenomenon is associated with a lack of iC3b binding to DC. As a consequence, deposition of iC3b on apoptotic cells does not modify their phagocytosis by DC. In conclusion, we demonstrate a cooperation between CD16 and CR3 that favors iC3b binding to CR3 but is lost on DC.

Published
2004
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