Search

Your search keyword '"Marie-Paule Kieny"' showing total 5 results
Start Over Author "Marie-Paule Kieny" Publisher hal ccsd
5 results on '"Marie-Paule Kieny"'

1. A comparison of Sars-Cov-2 vaccine platforms: the CoviCompare project

Author

Diana Molino, Christine Durier, Anne Radenne, Corinne Desaint, Jacques Ropers, Soizic Courcier, Louis Victorien Vieillard, Claire Rekacewicz, Beatrice Parfait, Victor Appay, Frédéric Batteux, Emmanuel Barillot, Michel Cogné, Béhazine Combadière, Christiane S. Eberhardt, Guy Gorochov, Philippe Hupé, Laetitia Ninove, Stéphane Paul, Isabelle Pellegrin, Sylvie van der Werf, Maeva Lefebvre, Elisabeth Botelho-Nevers, Inmaculada Ortega-Perez, Marie Jaspard, Samba Sow, Jean Daniel Lelièvre, Xavier de Lamballerie, Marie Paule Kieny, Eric Tartour, Odile Launay, CIC Cochin Pasteur (CIC 1417), Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Hôpital Cochin [AP-HP], Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Hôtel-Dieu-Groupe hospitalier Broca-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Paris Cité (UPCité), F-CRIN, Innovative clinical research network in vaccinology (I-REIVAC), Essais Thérapeutiques et Maladies Infectieuses, Université Paris-Sud - Paris 11 (UP11)-Institut National de la Santé et de la Recherche Médicale (INSERM), Centre d'investigation clinique Paris Est [CHU Pitié Salpêtrière] (CIC Paris-Est), Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Institut National de la Santé et de la Recherche Médicale (INSERM)-CHU Pitié-Salpêtrière [AP-HP], Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Sorbonne Université (SU)-Sorbonne Université (SU), Hôpital Cochin [AP-HP], Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP), Composantes innées de la réponse immunitaire et différenciation (CIRID), Université Bordeaux Segalen - Bordeaux 2-Centre National de la Recherche Scientifique (CNRS), Cancer et génome: Bioinformatique, biostatistiques et épidémiologie d'un système complexe, Mines Paris - PSL (École nationale supérieure des mines de Paris), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Institut Curie [Paris]-Institut National de la Santé et de la Recherche Médicale (INSERM), Microenvironment and B-cells: Immunopathology,Cell Differentiation, and Cancer (MOBIDIC), Université de Rennes (UR)-Etablissement français du sang [Rennes] (EFS Bretagne)-Institut National de la Santé et de la Recherche Médicale (INSERM), CHU Pontchaillou [Rennes], Centre d'Immunologie et des Maladies Infectieuses (CIMI), Institut National de la Santé et de la Recherche Médicale (INSERM)-Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS), Faculté de médecine [Genève], Biologie Cellulaire et Cancer, Institut Curie [Paris]-Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS), Unité des Virus Emergents (UVE), Institut de Recherche pour le Développement (IRD)-Aix Marseille Université (AMU)-Institut National de la Santé et de la Recherche Médicale (INSERM), Institut de Recherche pour le Développement (IRD), Physiologie cellulaire des régulations hormonale, nutritionnelles et pharmacologiques (UMR-S-530), Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM), Centre International de Recherche en Infectiologie (CIRI), École normale supérieure de Lyon (ENS de Lyon)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Université Jean Monnet - Saint-Étienne (UJM)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Génétique Moléculaire des Virus à ARN - Molecular Genetics of RNA Viruses (GMV-ARN (UMR_3569 / U-Pasteur_2)), Institut Pasteur [Paris] (IP)-Centre National de la Recherche Scientifique (CNRS)-Université Paris Cité (UPCité), Centre d’Investigation Clinique de Nantes (CIC Nantes), Université de Nantes (UN)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre hospitalier universitaire de Nantes (CHU Nantes), Centre Hospitalier Universitaire de Saint-Etienne [CHU Saint-Etienne] (CHU ST-E), Agence Nationale de Recherches sur le Sida et les Hépatites Virales (ANRS), Alliance for International medical Action (ALIMA), Bordeaux population health (BPH), Université de Bordeaux (UB)-Institut de Santé Publique, d'Épidémiologie et de Développement (ISPED)-Institut National de la Santé et de la Recherche Médicale (INSERM), Centre pour le Développement des Vaccins [Mali], Institut Mondor de Recherche Biomédicale (IMRB), Institut National de la Santé et de la Recherche Médicale (INSERM)-IFR10-Université Paris-Est Créteil Val-de-Marne - Paris 12 (UPEC UP12), Biochimie des Lipides, Institut National de la Santé et de la Recherche Médicale (INSERM), Paris-Centre de Recherche Cardiovasculaire (PARCC (UMR_S 970/ U970)), Hôpital Européen Georges Pompidou [APHP] (HEGP), Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Hôpitaux Universitaires Paris Ouest - Hôpitaux Universitaires Île de France Ouest (HUPO)-Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Hôpitaux Universitaires Paris Ouest - Hôpitaux Universitaires Île de France Ouest (HUPO)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Paris Cité (UPCité), Ministere des Solidarites et de la Sante, Ministere de l'Enseignement Superieur, de la Recherche et de l'Innovation, Coalition for Epidemic Preparedness Innovations (CEPI), ANRS \Emerging Infectious Diseases, ANR-20-COV3-0004,CoMemRep,Caractérisation des complexes de réplication associés à la membrane du SARS CoV 2(2020), Unité de Recherche Clinique des hôpitaux Pitié-Salpêtrière – Charles Foix [CHU Pitié Salpêtrière] (URC PSL-CFX), CHU Charles Foix [AP-HP], Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Sorbonne Université (SU)-Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Sorbonne Université (SU)-CHU Pitié-Salpêtrière [AP-HP], Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Sorbonne Université (SU)-Direction de la Recherche Clinique et de l'Innovation [AP-HP] (DRCI), Centre International de Recherche en Infectiologie - UMR (CIRI), École normale supérieure - Lyon (ENS Lyon)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Centre Hospitalier Universitaire de Saint-Etienne (CHU de Saint-Etienne), Chard-Hutchinson, Xavier, Université de Rennes 1 (UR1), Université de Rennes (UNIV-RENNES)-Université de Rennes (UNIV-RENNES)-Etablissement français du sang [Rennes] (EFS Bretagne)-Institut National de la Santé et de la Recherche Médicale (INSERM), and Institut Pasteur [Paris]-Centre National de la Recherche Scientifique (CNRS)-Université Paris Cité (UPCité)

Subjects
[SDV] Life Sciences [q-bio], COVID-19 Vaccines, [SDV.SPEE] Life Sciences [q-bio]/Santé publique et épidémiologie, SARS-CoV-2, [SDV]Life Sciences [q-bio], Spike Glycoprotein, Coronavirus, COVID-19, Humans, [SDV.SPEE]Life Sciences [q-bio]/Santé publique et épidémiologie, General Medicine, General Biochemistry, Genetics and Molecular Biology, ComputingMilieux_MISCELLANEOUS
Abstract

International audience

Published
2022

2. French research strategy to tackle antimicrobial resistance

Author

Céline Couderc-Obert, Céline Pulcini, Corinne Danan, Marie-Paule Kieny, Evelyne Jouvin-Marche, Antoine Andremont, Guia Carrara, Yazdan Yazdanpanah, Christian Lienhardt, Institute for Advanced Biosciences / Institut pour l'Avancée des Biosciences (Grenoble) (IAB), Centre Hospitalier Universitaire [Grenoble] (CHU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Etablissement français du sang - Auvergne-Rhône-Alpes (EFS)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes (UGA), Inserm, 75013, Paris, France, Ministry of Solidarity and Health, Paris, France, Ministry of Higher Education, Research and Innovation, Directorate General for Research and Innovation, Paris, France, Ministry of Agriculture and Food, General Directorate for Research and Education, Paris, France, Ministry for an Ecological and Solidary Transition, Research Department, Tour Séquoia, La Défense, France, Recherches Translationnelles sur le VIH et les maladies infectieuses endémiques er émergentes (TransVIHMI), Université Cheikh Anta Diop [Dakar, Sénégal] (UCAD)-Institut de Recherche pour le Développement (IRD)-Université de Yaoundé I-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Montpellier (UM)-Université Montpellier 1 (UM1), and Infection Antimicrobials Modelling Evolution, UMR 1137, Inserm, Université Paris Diderot, Sorbonne Paris Cité, Paris, France

Subjects
medicine.medical_specialty, business.industry, International Cooperation, MEDLINE, Drug Resistance, Microbial, General Medicine, Drug resistance, 010501 environmental sciences, 01 natural sciences, Anti-Bacterial Agents, 03 medical and health sciences, 0302 clinical medicine, Antibiotic resistance, [SDV.MHEP.MI]Life Sciences [q-bio]/Human health and pathology/Infectious diseases, Animals, Humans, Medicine, [SDV.SPEE]Life Sciences [q-bio]/Santé publique et épidémiologie, France, 030212 general & internal medicine, business, Intensive care medicine, ComputingMilieux_MISCELLANEOUS, 0105 earth and related environmental sciences
Abstract

International audience

Published
2020

3. The α-Glucosidase Inhibitor 1-Deoxynojirimycin Blocks Human Immunodeficiency Virus Envelope Glycoprotein-Mediated Membrane Fusion at the CXCR4 Binding Step

Author

Régis Guieu, Marie-Jeanne Papandréou, Marie Paule Kieny, Rym Barbouche, Emmanuel Fenouillet, Centre de recherche en neurobiologie - neurophysiologie de Marseille (CRN2M), Aix Marseille Université (AMU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Laboratoire des Venins et Toxines, Institut Pasteur de Tunis, Institut Pasteur de Tunis, Réseau International des Instituts Pasteur (RIIP)-Réseau International des Instituts Pasteur (RIIP), CNRS FRE2738 (FRE2738), Hôpital de la Timone [CHU - APHM] (TIMONE), Transgene SA, Neurobiologie des interactions cellulaires et neurophysiopathologie - NICN (NICN), and Université de la Méditerranée - Aix-Marseille 2-Centre National de la Recherche Scientifique (CNRS)

Subjects
Receptors, CXCR4, 1-Deoxynojirimycin, Glycosylation, viruses, [SDV]Life Sciences [q-bio], HIV Envelope Protein gp120, Biology, Ligands, Antiviral Agents, Membrane Fusion, Virus, law.invention, Mice, chemistry.chemical_compound, law, Viral entry, Cricetinae, [SDV.BC.IC]Life Sciences [q-bio]/Cellular Biology/Cell Behavior [q-bio.CB], Animals, Humans, Glycoside Hydrolase Inhibitors, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biochemistry [q-bio.BM], Receptor, Cells, Cultured, Pharmacology, chemistry.chemical_classification, HIV, virus diseases, Lipid bilayer fusion, alpha-Glucosidases, Virology, Cell biology, Drug Combinations, chemistry, CD4 Antigens, Recombinant DNA, Molecular Medicine, Glycoprotein
Abstract

1-Deoxynojirimycin (DNM) is a saccharide decoy that inhibits cellular alpha-glucosidase I-II activity. Treatment by DNM of human immunodeficiency virus (HIV)-infected lymphocyte cultures inhibits virus spread. The functional properties of the membrane-associated Env glycoprotein (Env) modified in the presence of DNM remain unclear because previous reports on this subject have essentially used recombinant soluble Envs whose properties differ notably from those of Env anchored on the surface of the virus. To model virus-associated Env synthesized in the presence of DNM, native Env was expressed at the surface of mammalian cells treated with DNM. As expected, its glycosylation pattern was altered in the presence of the inhibitor. Env was found able to bind CD4, whereas its ability to induce membrane fusion was abolished. The immunoreactivity of regions involved in interactions of Env with CXCR4 (V1, V2, C2, and V3) was modified and Env displayed altered interaction with this coreceptor. These results are consistent with the inhibition by DNM of virus entry at the Env/coreceptor interaction step. Finally, preliminary data indicate that suboptimal concentrations of DNM and natural or synthetic CXCR4 ligands used in combination potently inhibit the Env-mediated membrane fusion process. Altogether, our results suggest that DNM and its analogs deserve further investigation as anti-HIV agents in combination with experimental compounds targeting CXCR4 to inhibit each partner of this crucial step of HIV entry.

Published
2002

4. An Anti-Human Immunodeficiency Virus Multiple Antigen Peptide Encompassing the Cleavage Region of the Env Precursor Interferes With Membrane Fusion at a Post-CD4 Binding Step

Author

Emmanuel Fenouillet, Etienne Decroly, Marie Paule Kieny, Rym Barbouche, Laboratoire des Venins et Toxines, Institut Pasteur de Tunis, Institut Pasteur de Tunis, Réseau International des Instituts Pasteur (RIIP)-Réseau International des Instituts Pasteur (RIIP), Pathogénie des infections à lentivirus, Institut National de la Santé et de la Recherche Médicale (INSERM)-IFR48, Institut des sciences biologiques (INSB-CNRS)-Institut des sciences biologiques (INSB-CNRS), Transgene SA, Neurobiologie des interactions cellulaires et neurophysiopathologie - NICN (NICN), and Université de la Méditerranée - Aix-Marseille 2-Centre National de la Recherche Scientifique (CNRS)

Subjects
Anti-HIV Agents, HIV Antigens, viruses, [SDV]Life Sciences [q-bio], Genetic Vectors, Molecular Sequence Data, Cell, membrane fusion, Vaccinia virus, Peptide, HIV Env, HIV Envelope Protein gp120, Biology, Cleavage (embryo), Giant Cells, Cell Line, Antigen, Virology, [SDV.BC.IC]Life Sciences [q-bio]/Cellular Biology/Cell Behavior [q-bio.CB], medicine, Humans, Amino Acid Sequence, Lymphocytes, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biochemistry [q-bio.BM], Peptide sequence, cleavage sequence, chemistry.chemical_classification, Syncytium, Cell Membrane, Gene Products, env, Lipid bilayer fusion, virus diseases, Molecular biology, Peptide Fragments, anti-HIV peptide, medicine.anatomical_structure, chemistry, Cell culture, CD4 Antigens, HIV-2, HIV-1, processing, Protein Processing, Post-Translational, Protein Binding
Abstract

CLIV is a multiple antigen peptide ([PTKAKRRVVQREKR](4)-K(2)-K-betaA) that encompasses the cleavage region of the human immunodeficiency virus type 1 (HIV-1) envelope precursor. It displays an antiviral activity against HIV-1 and HIV-2 and inhibits HIV-1 Env-mediated cell-to-cell fusion. This effect has previously been attributed to interference with Env processing, resulting in the expression of a nonfusogenic envelope [Virology (1998) 247, 137]. However, we show here that CLIV does not alter the status of Env cleavage at steady state. Using various aggregation/syncytium assays that allow us to discriminate between gp120/CD4 binding and binding followed by gp41-mediated fusion, we demonstrate that CLIV inhibits a step of the cell-to-cell fusion process after CD4 binding. We demonstrate also that CLIV binds at 37 degrees C to a single class of protein present at the CD4(+) cell surface (Scatchard analysis: K(d) = 8 nM; B(max) = 10(4) sites/cell) and that the fusion inhibition activity seems to correlate with binding to this proteic component. In contrast, CLIV interacts with neither membrane-inserted nor CD4-associated Env. We therefore propose that CLIV interferes after Env/CD4 binding with a step of the membrane fusion process that may involve the C-terminal domain of gp120.

Published
2000

5. Expression of heterologous genes in Mycobacterium bovis BCG: induction of a cellular response against HIV-1 Nef protein

Author

Marie Paule Kieny, Nathalie Winter, J. Timm, Brigitte Gicquel, Jean Rauzier, B. Guy, M. Gheorghiu, Micheline Lagranderie, Claude Leclerc, Institut Pasteur [Paris], Biologie des Régulations Immunitaires, Institut Pasteur [Paris]-Institut National de la Santé et de la Recherche Médicale (INSERM), Transgene SA, Institut Pasteur [Paris] (IP), Institut Pasteur [Paris] (IP)-Institut National de la Santé et de la Recherche Médicale (INSERM), and ProdInra, Migration

Subjects
Operon, PROLIFERATIVE RESPONSE, T-Lymphocytes, medicine.disease_cause, Lymphocyte Activation, Gene Products, nef, RECOMBINANT DNA, IMMUNOLOGY, HEAT-SHOCK PROMOTER, SEROPOSITIVE INDIVIDUALS, Promoter Regions, Genetic, 0303 health sciences, Mycobacterium bovis, Immunity, Cellular, General Medicine, STREPTOMYCES-ALBUS, Recombinant Proteins, Streptomyces, 3. Good health, Bacterial vaccine, [SDV.MP]Life Sciences [q-bio]/Microbiology and Parasitology, GROES/GROEL1 OPERON, Expression cassette, Genetic Vectors, Heterologous, FORTUITUM, VECTOR, Biology, Virus, Microbiology, Gene product, 03 medical and health sciences, EXPRESSION CASSETTE, Genetics, medicine, nef Gene Products, Human Immunodeficiency Virus, PAL5000, Escherichia coli, [SDV.MP] Life Sciences [q-bio]/Microbiology and Parasitology, 030304 developmental biology, ANTITUBERCULOSIS VACCINE, 030306 microbiology, FOREIGN ANTIGEN, BACTERIOPHAGE-LAMBDA, biology.organism_classification, Virology, HIV-1, bacteria, Lymph Nodes, PLASMID
Abstract

International audience; Mycobacterium bovis bacillus Calmette-Guerin (BCG) has been used as a live bacterial vaccine to immunize more than two billion people against tuberculosis. In an attempt to use this vaccinal strain as a vehicle for protective antigens, the human immunodeficiency virus type 1 gene encoding the Nef protein was cloned in a mycobacteria-Escherichia coli shuttle plasmid and transferred into BCG. The nef gene was expressed under the control of an expression cassette carrying the promoter of the groES/groEL1 operon from Streptomyces albus and a synthetic ribosome-binding site. Lymph node cells from mice immunized with BCG-nef proliferated vigorously in response to purified Nef protein. This first report of a proliferative response suggests that recombinant BCG strains may be used to immunize against pathogens for which T-cell-mediated responses are important for protection.

Published
1991

Catalog

Books, media, physical & digital resources
See catalog results