Strength of Neisseria meningitidis binding to endothelial cells requires highly-ordered CD147/β2-adrenoceptor clusters assembled by alpha-actinin-4
Nawal Maïssa,
Valentina Covarelli,
Sébastien Janel,
Beatrice Durel,
Nandi Simpson,
Sandra C. Bernard,
Liliana Pardo-Lopez,
Haniaa Bouzinba-Ségard,
Camille Faure,
Mark G.H. Scott,
Mathieu Coureuil,
Philippe C. Morand,
Frank Lafont,
Xavier Nassif,
Stefano Marullo and
Sandrine Bourdoulous ()
Additional contact information
Nawal Maïssa: Inserm, U1016, Immunity and Inflammation, Institut Cochin
Valentina Covarelli: Inserm, U1016, Immunity and Inflammation, Institut Cochin
Sébastien Janel: Cellular Microbiology and Physics of infection, Center for Infection and Immunity of Lille, Institut Pasteur de Lille
Beatrice Durel: Inserm, U1016, Immunity and Inflammation, Institut Cochin
Nandi Simpson: Inserm, U1016, Immunity and Inflammation, Institut Cochin
Sandra C. Bernard: Inserm, U1016, Immunity and Inflammation, Institut Cochin
Liliana Pardo-Lopez: Inserm, U1016, Immunity and Inflammation, Institut Cochin
Haniaa Bouzinba-Ségard: Inserm, U1016, Immunity and Inflammation, Institut Cochin
Camille Faure: Inserm, U1016, Immunity and Inflammation, Institut Cochin
Mark G.H. Scott: Inserm, U1016, Immunity and Inflammation, Institut Cochin
Mathieu Coureuil: Inserm, unité U1151, Institut-Necker-Enfants-Malades
Philippe C. Morand: Inserm, U1016, Immunity and Inflammation, Institut Cochin
Frank Lafont: Cellular Microbiology and Physics of infection, Center for Infection and Immunity of Lille, Institut Pasteur de Lille
Xavier Nassif: Inserm, unité U1151, Institut-Necker-Enfants-Malades
Stefano Marullo: Inserm, U1016, Immunity and Inflammation, Institut Cochin
Sandrine Bourdoulous: Inserm, U1016, Immunity and Inflammation, Institut Cochin
Nature Communications, 2017, vol. 8, issue 1, 1-15
Abstract:
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.
Date: 2017
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:8:y:2017:i:1:d:10.1038_ncomms15764
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DOI: 10.1038/ncomms15764
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