Structural and functional insights into the delivery of a bacterial Rhs pore-forming toxin to the membrane Journal Articles uri icon

  • Overview
  • Research
  • Identity
  • Additional Document Info
  • View All


  • AbstractBacterial competition is a significant driver of toxin polymorphism, which allows continual compensatory evolution between toxins and the resistance developed to overcome their activity. Bacterial Rearrangement hot spot (Rhs) proteins represent a widespread example of toxin polymorphism. Here, we present the 2.45 Å cryo-electron microscopy structure of Tse5, an Rhs protein central to Pseudomonas aeruginosa type VI secretion system-mediated bacterial competition. This structural insight, coupled with an extensive array of biophysical and genetic investigations, unravels the multifaceted functional mechanisms of Tse5. The data suggest that interfacial Tse5-membrane binding delivers its encapsulated pore-forming toxin fragment to the target bacterial membrane, where it assembles pores that cause cell depolarisation and, ultimately, bacterial death.


  • González-Magaña, Amaia
  • Tascón, Igor
  • Altuna-Alvarez, Jon
  • Queralt-Martín, María
  • Colautti, Jake
  • Velázquez, Carmen
  • Zabala, Maialen
  • Rojas-Palomino, Jessica
  • Cárdenas, Marité
  • Alcaraz, Antonio
  • Whitney, John
  • Ubarretxena-Belandia, Iban
  • Albesa-Jové, David

publication date

  • November 28, 2023