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

Amaia González-Magaña, Igor Tascón, Jon Altuna-Alvarez, María Queralt-Martín, Jake Colautti, Carmen Velázquez, Maialen Zabala, Jessica Rojas-Palomino, Marité Cárdenas, Antonio Alcaraz, John C. Whitney, Iban Ubarretxena-Belandia () and David Albesa-Jové ()
Additional contact information
Amaia González-Magaña: Fundación Biofísica Bizkaia/Biofisika Bizkaia Fundazioa (FBB)
Igor Tascón: Fundación Biofísica Bizkaia/Biofisika Bizkaia Fundazioa (FBB)
Jon Altuna-Alvarez: Fundación Biofísica Bizkaia/Biofisika Bizkaia Fundazioa (FBB)
María Queralt-Martín: University Jaume I
Jake Colautti: McMaster University
Carmen Velázquez: Fundación Biofísica Bizkaia/Biofisika Bizkaia Fundazioa (FBB)
Maialen Zabala: Fundación Biofísica Bizkaia/Biofisika Bizkaia Fundazioa (FBB)
Jessica Rojas-Palomino: University Jaume I
Marité Cárdenas: Fundación Biofísica Bizkaia/Biofisika Bizkaia Fundazioa (FBB)
Antonio Alcaraz: University Jaume I
John C. Whitney: McMaster University
Iban Ubarretxena-Belandia: Fundación Biofísica Bizkaia/Biofisika Bizkaia Fundazioa (FBB)
David Albesa-Jové: Fundación Biofísica Bizkaia/Biofisika Bizkaia Fundazioa (FBB)

Nature Communications, 2023, vol. 14, issue 1, 1-16

Abstract: Abstract Bacterial 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.

Date: 2023
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:14:y:2023:i:1:d:10.1038_s41467-023-43585-5

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DOI: 10.1038/s41467-023-43585-5

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