Meningococci drive host membrane tubulation to recruit their signaling receptors
Abstract
Abstract Once passed into the bloodstream, bacterial pathogens have a limited time to interact with permissive receptors at the surface of host cells. Neisseria meningitidis has developed an extremely effective strategy allowing it to find its receptors in a few seconds. Here, we report that N. meningitidis type IV pili exploit the physical properties of host cells' plasma membranes to promote the formation of early tubular membrane structures essential for initial bacterial adhesion. These tubular structures, which form before any signaling events in host cells, concentrate and trap multiple plasma membrane-associated proteins in the vicinity of bacteria, thereby facilitating the selection, interaction and activation of specific adhesion and signaling receptors by bacterial ligands present on type IV pili. Our results define an additional paradigm for the recruitment of specific receptors by pathogenic bacteria, which depends on the physical property of bacterial pili to induce the formation of tubular plasma membrane structures enriched in integral plasma membrane receptors.
Article Details
Authors (21)
Audrey Laurent-Granger
Kévin Sollier
Bruno Saubaméa
Cellular and Molecular Imaging Platform (PICMO), US 25 Inserm, UAR 3612 CNRS, Faculté de Pharmacie de Paris
Virginie Mignon
Nicolas Goudin
Necker Bio-Image Analysis, INSERM US24/CNRS UMS 3633
Yaëlle Wormser
Morgane Wuckelt
Mahmoud Rifai
Thomas Heng
Lya L’hermitte
Marta Conflitti
Julie Meyer
INSERM U1151, CNRS UMR8253, Institut Necker-Enfants Malades, Université Paris Cité
Hervé Lécuyer
Anne Jamet
Nicolas Borghi
Philippe Girard
Investigation Network on Venous Thrombo-Embolism–French Clinical Research Infrastructure Network, Saint-Étienne, France
Emmanuelle Bille
INSERM U1151, CNRS UMR8253, Institut Necker-Enfants Malades, Université Paris Cité
Gregory Lavieu
Eric Rubinstein
Stefano Marullo
Mathieu Coureuil
INSERM U1151, CNRS UMR8253, Institut Necker-Enfants Malades, Université Paris Cité