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

Author

Listed:
  • Amaia González-Magaña

    (Fundación Biofísica Bizkaia/Biofisika Bizkaia Fundazioa (FBB)
    University of the Basque Country)

  • Igor Tascón

    (Fundación Biofísica Bizkaia/Biofisika Bizkaia Fundazioa (FBB)
    Ikerbasque, Basque Foundation for Science)

  • 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)
    University of the Basque Country)

  • Maialen Zabala

    (Fundación Biofísica Bizkaia/Biofisika Bizkaia Fundazioa (FBB)
    University of the Basque Country)

  • Jessica Rojas-Palomino

    (University Jaume I)

  • Marité Cárdenas

    (Fundación Biofísica Bizkaia/Biofisika Bizkaia Fundazioa (FBB)
    Ikerbasque, Basque Foundation for Science)

  • Antonio Alcaraz

    (University Jaume I)

  • John C. Whitney

    (McMaster University)

  • Iban Ubarretxena-Belandia

    (Fundación Biofísica Bizkaia/Biofisika Bizkaia Fundazioa (FBB)
    Ikerbasque, Basque Foundation for Science)

  • David Albesa-Jové

    (Fundación Biofísica Bizkaia/Biofisika Bizkaia Fundazioa (FBB)
    University of the Basque Country
    Ikerbasque, Basque Foundation for Science)

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.

Suggested Citation

  • 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 , 2023. "Structural and functional insights into the delivery of a bacterial Rhs pore-forming toxin to the membrane," Nature Communications, Nature, vol. 14(1), pages 1-16, December.
    • Handle: RePEc:nat:natcom:v:14:y:2023:i:1:d:10.1038_s41467-023-43585-5
    DOI: 10.1038/s41467-023-43585-5
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    References listed on IDEAS

    as
    1. Alistair B. Russell & Rachel D. Hood & Nhat Khai Bui & Michele LeRoux & Waldemar Vollmer & Joseph D. Mougous, 2011. "Type VI secretion delivers bacteriolytic effectors to target cells," Nature, Nature, vol. 475(7356), pages 343-347, July.
    2. Jason N. Busby & Santosh Panjikar & Michael J. Landsberg & Mark R. H. Hurst & J. Shaun Lott, 2013. "The BC component of ABC toxins is an RHS-repeat-containing protein encapsulation device," Nature, Nature, vol. 501(7468), pages 547-550, September.
    3. Tong-Tong Pei & Hao Li & Xiaoye Liang & Zeng-Hang Wang & Guangfeng Liu & Li-Li Wu & Haeun Kim & Zhiping Xie & Ming Yu & Shuangjun Lin & Ping Xu & Tao G. Dong, 2020. "Publisher Correction: Intramolecular chaperone-mediated secretion of an Rhs effector toxin by a type VI secretion system," Nature Communications, Nature, vol. 11(1), pages 1-1, December.
    4. Verity A. Jackson & Dimphna H. Meijer & Maria Carrasquero & Laura S. Bezouwen & Edward D. Lowe & Colin Kleanthous & Bert J. C. Janssen & Elena Seiradake, 2018. "Structures of Teneurin adhesion receptors reveal an ancient fold for cell-cell interaction," Nature Communications, Nature, vol. 9(1), pages 1-9, December.
    5. Tong-Tong Pei & Hao Li & Xiaoye Liang & Zeng-Hang Wang & Guangfeng Liu & Li-Li Wu & Haeun Kim & Zhiping Xie & Ming Yu & Shuangjun Lin & Ping Xu & Tao G. Dong, 2020. "Intramolecular chaperone-mediated secretion of an Rhs effector toxin by a type VI secretion system," Nature Communications, Nature, vol. 11(1), pages 1-13, December.
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