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Your search keyword '"Morand, Philippe"' showing total 4 results
Start Over Author "Morand, Philippe" Journal nature communications
4 results on '"Morand, Philippe"'

1. Strength of Neisseria meningitidis binding to endothelial cells requires highly-ordered CD147/β2-adrenoceptor clusters assembled by alpha-actinin-4

Author

Maïssa, Nawal, Covarelli, Valentina, Janel, Sébastien, Durel, Beatrice, Simpson, Nandi, Bernard, Sandra, Pardo-Lopez, Liliana, Bouzinba-Ségard, Haniaa, Faure, Camille, Scott, Mark G.H., Coureuil, Mathieu, Morand, Philippe, Lafont, Frank, Nassif, Xavier, Marullo, Stefano, Bourdoulous, Sandrine, Institut Cochin (IC UM3 (UMR 8104 / U1016)), Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Centre d’Infection et d’Immunité de Lille - INSERM U 1019 - UMR 9017 - UMR 8204 (CIIL), Institut Pasteur de Lille, Réseau International des Instituts Pasteur (RIIP)-Réseau International des Instituts Pasteur (RIIP)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Lille-Centre Hospitalier Régional Universitaire [Lille] (CHRU Lille)-Centre National de la Recherche Scientifique (CNRS), Institut Necker Enfants-Malades (INEM - UM 111 (UMR 8253 / U1151)), CHU Necker - Enfants Malades [AP-HP], Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP), N.M. was supported by a doctoral fellowship from Université Paris Descartes and the Fondation pour la Recherche Médicale of France. V.C. was supported by a postdoctoral fellowship from the Fondation pour la Recherche Médicale. S.C.B. was supported by a doctoral fellowship from Université Paris Diderot and Association pour la Recherche sur le Cancer. This work was supported by collaborative research grants the Agence Nationale de la Recherche of France (ANR-14-CE14-0010-02) and the Université Paris Descartes (AAP-2011) to S.B., X.N. and S.M., from the Fondation pour la Recherche Médicale to X.N. and S.M. and from the ANR (ANR-10-EQPX-04-01) to F.L., ANR-14-CE14-0010,NEMBRAIN,La barrière hémato-encéphalique: de la méningite bactérienne à la délivrance de médicaments dans le cerveau(2014), ANR-10-EQPX-0004,Imaginex BioMed,Plateau de microscopie de criblage à haut débit et d'analyse à très haute résolution(2010), Centre National de la Recherche Scientifique (CNRS)-Centre Hospitalier Régional Universitaire [Lille] (CHRU Lille)-Université de Lille-Institut National de la Santé et de la Recherche Médicale (INSERM)-Institut Pasteur de Lille, Réseau International des Instituts Pasteur (RIIP)-Réseau International des Instituts Pasteur (RIIP), Faure, Camille, Appel à projets générique - La barrière hémato-encéphalique: de la méningite bactérienne à la délivrance de médicaments dans le cerveau - - NEMBRAIN2014 - ANR-14-CE14-0010 - Appel à projets générique - VALID, and Equipements d'excellence - Plateau de microscopie de criblage à haut débit et d'analyse à très haute résolution - - Imaginex BioMed2010 - ANR-10-EQPX-0004 - EQPX - VALID

Subjects
[SDV] Life Sciences [q-bio], [SDV]Life Sciences [q-bio], Science
Abstract

International audience; Neisseria meningitidis (meningococcus) is an invasive bacterial pathogen that colonizes human vessels, causing thrombotic lesions and meningitis. Establishment of tight interactions with endothelial cells is crucial for meningococci to resist haemodynamic forces. Two endothelial receptors, CD147 and the β2-adrenergic receptor (β2AR), are sequentially engaged by meningococci to adhere and promote signalling events leading to vascular colonization, but their spatiotemporal coordination is unknown. Here we report that CD147 and β2AR form constitutive hetero-oligomeric complexes. The scaffolding protein α-actinin-4 directly binds to the cytosolic tail of CD147 and governs the assembly of CD147–β2AR complexes in highly ordered clusters at bacterial adhesion sites. This multimolecular assembly process increases the binding strength of meningococci to endothelial cells under shear stress, and creates molecular platforms for the elongation of membrane protrusions surrounding adherent bacteria. Thus, the specific organization of cellular receptors has major impacts on host–pathogen interaction.

Published
2017
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2. Pseudomonas aeruginosa eradicates Staphylococcus aureus by manipulating the host immunity

Author

Pernet, Erwan, primary, Guillemot, Laurent, additional, Burgel, Pierre-Régis, additional, Martin, Clémence, additional, Lambeau, Gérard, additional, Sermet-Gaudelus, Isabelle, additional, Sands, Dorota, additional, Leduc, Dominique, additional, Morand, Philippe C., additional, Jeammet, Louise, additional, Chignard, Michel, additional, Wu, Yongzheng, additional, and Touqui, Lhousseine, additional

Published
2014
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3. Strength of Neisseria meningitidis binding to endothelial cells requires highly-ordered CD147/β2-adrenoceptor clusters assembled by alpha-actinin-4.

Author

Maïssa, Nawal, Covarelli, Valentina, Janel, Sébastien, Durel, Beatrice, Simpson, Nandi, Bernard, Sandra C., Pardo-Lopez, Liliana, Bouzinba-Ségard, Haniaa, Faure, Camille, Scott, Mark G.H., Coureuil, Mathieu, Morand, Philippe C., Lafont, Frank, Nassif, Xavier, Marullo, Stefano, and Bourdoulous, Sandrine

Abstract

Neisseria meningitidis (meningococcus) is an invasive bacterial pathogen that colonizes human vessels, causing thrombotic lesions and meningitis. Establishment of tight interactions with endothelial cells is crucial for meningococci to resist haemodynamic forces. Two endothelial receptors, CD147 and the β2-adrenergic receptor (β2AR), are sequentially engaged by meningococci to adhere and promote signalling events leading to vascular colonization, but their spatiotemporal coordination is unknown. Here we report that CD147 and β2AR form constitutive hetero-oligomeric complexes. The scaffolding protein α-actinin-4 directly binds to the cytosolic tail of CD147 and governs the assembly of CD147-β2AR complexes in highly ordered clusters at bacterial adhesion sites. This multimolecular assembly process increases the binding strength of meningococci to endothelial cells under shear stress, and creates molecular platforms for the elongation of membrane protrusions surrounding adherent bacteria. Thus, the specific organization of cellular receptors has major impacts on host-pathogen interaction. [ABSTRACT FROM AUTHOR]

Published
2017
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4. Strength of Neisseria meningitidis binding to endothelial cells requires highly-ordered CD147/β 2 -adrenoceptor clusters assembled by alpha-actinin-4.

Author

Maïssa N, Covarelli V, Janel S, Durel B, Simpson N, Bernard SC, Pardo-Lopez L, Bouzinba-Ségard H, Faure C, Scott MGH, Coureuil M, Morand PC, Lafont F, Nassif X, Marullo S, and Bourdoulous S

Subjects
Bacterial Adhesion physiology, Basigin genetics, Endothelial Cells metabolism, Endothelial Cells microbiology, Humans, Multiprotein Complexes metabolism, Neisseria meningitidis pathogenicity, Receptors, Adrenergic, beta-2 genetics, Actinin metabolism, Basigin metabolism, Host-Pathogen Interactions physiology, Neisseria meningitidis metabolism, Receptors, Adrenergic, beta-2 metabolism
Abstract

Neisseria meningitidis (meningococcus) is an invasive bacterial pathogen that colonizes human vessels, causing thrombotic lesions and meningitis. Establishment of tight interactions with endothelial cells is crucial for meningococci to resist haemodynamic forces. Two endothelial receptors, CD147 and the β2-adrenergic receptor (β 2 AR), are sequentially engaged by meningococci to adhere and promote signalling events leading to vascular colonization, but their spatiotemporal coordination is unknown. Here we report that CD147 and β 2 AR form constitutive hetero-oligomeric complexes. The scaffolding protein α-actinin-4 directly binds to the cytosolic tail of CD147 and governs the assembly of CD147-β 2 AR complexes in highly ordered clusters at bacterial adhesion sites. This multimolecular assembly process increases the binding strength of meningococci to endothelial cells under shear stress, and creates molecular platforms for the elongation of membrane protrusions surrounding adherent bacteria. Thus, the specific organization of cellular receptors has major impacts on host-pathogen interaction.

Published
2017
Full Text
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