<p>Once passed into the bloodstream, bacterial pathogens have a limited time to interact with permissive receptors at the surface of host cells. <i>Neisseria meningitidis</i> has developed an extremely effective strategy allowing it to find its receptors in a few seconds. Here, we report that <i>N. meningitidis</i> 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&#xa0;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.</p>

错误:搜索内容不能为空,请输入英文关键词
错误:关键词超出字数限制,请精简
高级检索

Meningococci drive host membrane tubulation to recruit their signaling receptors

  • Audrey Laurent-Granger,
  • Kévin Sollier,
  • Bruno Saubamea,
  • Virginie Mignon,
  • Nicolas Goudin,
  • Yaëlle Wormser,
  • Morgane Wuckelt,
  • Mahmoud Rifai,
  • Thomas Heng,
  • Lya L’hermitte,
  • Marta Conflitti,
  • Julie Meyer,
  • Hervé Lecuyer,
  • Anne Jamet,
  • Nicolas Borghi,
  • Philippe Girard,
  • Emmanuelle Bille,
  • Grégory Lavieu,
  • Eric Rubinstein,
  • Stefano Marullo,
  • Mathieu Coureuil

摘要

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.