Strength of Neisseria meningitidis binding ...
Document type :
Compte-rendu et recension critique d'ouvrage
DOI :
PMID :
Title :
Strength of Neisseria meningitidis binding to endothelial cells requires highly-ordered CD147/β2-adrenoceptor clusters assembled by alpha-actinin-4
Author(s) :
Maïssa, Nawal [Auteur]
Institut Cochin [IC UM3 (UMR 8104 / U1016)]
Covarelli, Valentina [Auteur]
Institut Cochin [IC UM3 (UMR 8104 / U1016)]
Janel, Sébastien [Auteur]
Centre d’Infection et d’Immunité de Lille - INSERM U 1019 - UMR 9017 - UMR 8204 [CIIL]
Durel, Beatrice [Auteur]
Institut Cochin [IC UM3 (UMR 8104 / U1016)]
Simpson, Nandi [Auteur]
Institut Cochin [IC UM3 (UMR 8104 / U1016)]
Bernard, Sandra [Auteur]
Institut Cochin [IC UM3 (UMR 8104 / U1016)]
Pardo-Lopez, Liliana [Auteur]
Institut Cochin [IC UM3 (UMR 8104 / U1016)]
Bouzinba-Ségard, Haniaa [Auteur]
Institut Cochin [IC UM3 (UMR 8104 / U1016)]
Faure, Camille [Auteur]
Institut Cochin [IC UM3 (UMR 8104 / U1016)]
Scott, Mark G.H. [Auteur]
Institut Cochin [IC UM3 (UMR 8104 / U1016)]
Coureuil, Mathieu [Auteur]
Institut Necker Enfants-Malades [INEM - UM 111 (UMR 8253 / U1151)]
Morand, Philippe [Auteur]
Institut Cochin [IC UM3 (UMR 8104 / U1016)]
Lafont, Frank [Auteur]
Centre d’Infection et d’Immunité de Lille - INSERM U 1019 - UMR 9017 - UMR 8204 [CIIL]
Nassif, Xavier [Auteur]
Institut Necker Enfants-Malades [INEM - UM 111 (UMR 8253 / U1151)]
Hôpital Necker - Enfants Malades [AP-HP]
Marullo, Stefano [Auteur]
Institut Cochin [IC UM3 (UMR 8104 / U1016)]
Bourdoulous, Sandrine [Auteur correspondant]
Institut Cochin [IC UM3 (UMR 8104 / U1016)]
Institut Cochin [IC UM3 (UMR 8104 / U1016)]
Covarelli, Valentina [Auteur]
Institut Cochin [IC UM3 (UMR 8104 / U1016)]
Janel, Sébastien [Auteur]
Centre d’Infection et d’Immunité de Lille - INSERM U 1019 - UMR 9017 - UMR 8204 [CIIL]
Durel, Beatrice [Auteur]
Institut Cochin [IC UM3 (UMR 8104 / U1016)]
Simpson, Nandi [Auteur]
Institut Cochin [IC UM3 (UMR 8104 / U1016)]
Bernard, Sandra [Auteur]
Institut Cochin [IC UM3 (UMR 8104 / U1016)]
Pardo-Lopez, Liliana [Auteur]
Institut Cochin [IC UM3 (UMR 8104 / U1016)]
Bouzinba-Ségard, Haniaa [Auteur]
Institut Cochin [IC UM3 (UMR 8104 / U1016)]
Faure, Camille [Auteur]
Institut Cochin [IC UM3 (UMR 8104 / U1016)]
Scott, Mark G.H. [Auteur]
Institut Cochin [IC UM3 (UMR 8104 / U1016)]
Coureuil, Mathieu [Auteur]
Institut Necker Enfants-Malades [INEM - UM 111 (UMR 8253 / U1151)]
Morand, Philippe [Auteur]
Institut Cochin [IC UM3 (UMR 8104 / U1016)]
Lafont, Frank [Auteur]
![refId](/themes/Mirage2//images/idref.png)
Centre d’Infection et d’Immunité de Lille - INSERM U 1019 - UMR 9017 - UMR 8204 [CIIL]
Nassif, Xavier [Auteur]
Institut Necker Enfants-Malades [INEM - UM 111 (UMR 8253 / U1151)]
Hôpital Necker - Enfants Malades [AP-HP]
Marullo, Stefano [Auteur]
Institut Cochin [IC UM3 (UMR 8104 / U1016)]
Bourdoulous, Sandrine [Auteur correspondant]
Institut Cochin [IC UM3 (UMR 8104 / U1016)]
Journal title :
Nature Communications
Pages :
15764
Publisher :
Nature Publishing Group
Publication date :
2017-06-01
ISSN :
2041-1723
HAL domain(s) :
Sciences du Vivant [q-bio]
English abstract : [en]
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 ...
Show more >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.Show less >
Show more >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.Show less >
Language :
Anglais
Popular science :
Non
ANR Project :
Source :
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