# Meningococci drive host membrane tubulation to recruit their signaling receptors

## TL;DR

Meningococci use type IV pili to create membrane tubules that trap host proteins, helping them quickly find and activate receptors for adhesion.

## Contribution

The study reveals a novel mechanism by which meningococci exploit host membrane physics to recruit signaling receptors.

## Key findings

- Type IV pili induce tubular membrane structures before host cell signaling begins.
- These structures trap and concentrate membrane proteins near bacteria, aiding receptor activation.
- The process enables rapid adhesion and signaling by meningococci.

## 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.

The adhesion of meningococci to endothelial cells relies on type IV pili, which induce the formation of long tubular structures on the host cell membrane. Here, the authors show that the tubular structures accumulate and trap host membrane-associated proteins, which facilitates their interaction with bacterial ligands and the activation of adhesion and signaling receptors.