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Biogenesis and structure of a type VI secretion membrane core complex

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  • Eric Durand

    (Laboratoire d’Ingénierie des Systèmes Macromoléculaires, Aix-Marseille Université - CNRS, UMR 7255
    Architecture et Fonction des Macromolécules Biologiques, CNRS, UMR 7257, Campus de Luminy, Case 932
    G5 Biologie structurale de la sécrétion bactérienne, Institut Pasteur
    UMR 3528, CNRS, Institut Pasteur)

  • Van Son Nguyen

    (Architecture et Fonction des Macromolécules Biologiques, CNRS, UMR 7257, Campus de Luminy, Case 932
    AFMB, Aix-Marseille Université, IHU Méditerranée Infection, Campus de Luminy, Case 932)

  • Abdelrahim Zoued

    (Laboratoire d’Ingénierie des Systèmes Macromoléculaires, Aix-Marseille Université - CNRS, UMR 7255)

  • Laureen Logger

    (Laboratoire d’Ingénierie des Systèmes Macromoléculaires, Aix-Marseille Université - CNRS, UMR 7255)

  • Gérard Péhau-Arnaudet

    (UMR 3528, CNRS, Institut Pasteur)

  • Marie-Stéphanie Aschtgen

    (Laboratoire d’Ingénierie des Systèmes Macromoléculaires, Aix-Marseille Université - CNRS, UMR 7255)

  • Silvia Spinelli

    (Architecture et Fonction des Macromolécules Biologiques, CNRS, UMR 7257, Campus de Luminy, Case 932
    AFMB, Aix-Marseille Université, IHU Méditerranée Infection, Campus de Luminy, Case 932)

  • Aline Desmyter

    (Architecture et Fonction des Macromolécules Biologiques, CNRS, UMR 7257, Campus de Luminy, Case 932
    AFMB, Aix-Marseille Université, IHU Méditerranée Infection, Campus de Luminy, Case 932)

  • Benjamin Bardiaux

    (UMR 3528, CNRS, Institut Pasteur
    Unité de Bioinformatique Structurale, Institut Pasteur)

  • Annick Dujeancourt

    (G5 Biologie structurale de la sécrétion bactérienne, Institut Pasteur
    UMR 3528, CNRS, Institut Pasteur)

  • Alain Roussel

    (Architecture et Fonction des Macromolécules Biologiques, CNRS, UMR 7257, Campus de Luminy, Case 932
    AFMB, Aix-Marseille Université, IHU Méditerranée Infection, Campus de Luminy, Case 932)

  • Christian Cambillau

    (Architecture et Fonction des Macromolécules Biologiques, CNRS, UMR 7257, Campus de Luminy, Case 932
    AFMB, Aix-Marseille Université, IHU Méditerranée Infection, Campus de Luminy, Case 932)

  • Eric Cascales

    (Laboratoire d’Ingénierie des Systèmes Macromoléculaires, Aix-Marseille Université - CNRS, UMR 7255)

  • Rémi Fronzes

    (G5 Biologie structurale de la sécrétion bactérienne, Institut Pasteur
    UMR 3528, CNRS, Institut Pasteur)

Abstract

Bacteria share their ecological niches with other microbes. The bacterial type VI secretion system is one of the key players in microbial competition, as well as being an important virulence determinant during bacterial infections. It assembles a nano-crossbow-like structure in the cytoplasm of the attacker cell that propels an arrow made of a haemolysin co-regulated protein (Hcp) tube and a valine–glycine repeat protein G (VgrG) spike and punctures the prey’s cell wall. The nano-crossbow is stably anchored to the cell envelope of the attacker by a membrane core complex. Here we show that this complex is assembled by the sequential addition of three type VI subunits (Tss)—TssJ, TssM and TssL—and present a structure of the fully assembled complex at 11.6 Å resolution, determined by negative-stain electron microscopy. With overall C5 symmetry, this 1.7-megadalton complex comprises a large base in the cytoplasm. It extends in the periplasm via ten arches to form a double-ring structure containing the carboxy-terminal domain of TssM (TssMct) and TssJ that is anchored in the outer membrane. The crystal structure of the TssMct–TssJ complex coupled to whole-cell accessibility studies suggest that large conformational changes induce transient pore formation in the outer membrane, allowing passage of the attacking Hcp tube/VgrG spike.

Suggested Citation

  • Eric Durand & Van Son Nguyen & Abdelrahim Zoued & Laureen Logger & Gérard Péhau-Arnaudet & Marie-Stéphanie Aschtgen & Silvia Spinelli & Aline Desmyter & Benjamin Bardiaux & Annick Dujeancourt & Alain , 2015. "Biogenesis and structure of a type VI secretion membrane core complex," Nature, Nature, vol. 523(7562), pages 555-560, July.
  • Handle: RePEc:nat:nature:v:523:y:2015:i:7562:d:10.1038_nature14667
    DOI: 10.1038/nature14667
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    Cited by:

    1. Selina Fecht & Patricia Paracuellos & Sujatha Subramoni & Casandra Ai Zhu Tan & Aravindan Ilangovan & Tiago R. D. Costa & Alain Filloux, 2024. "Functionality of chimeric TssA proteins in the type VI secretion system reveals sheath docking specificity within their N-terminal domains," Nature Communications, Nature, vol. 15(1), pages 1-13, December.
    2. Benjamin Kostiuk & Francis J. Santoriello & Laura Diaz-Satizabal & Fabiana Bisaro & Kyung-Jo Lee & Anna N. Dhody & Daniele Provenzano & Daniel Unterweger & Stefan Pukatzki, 2021. "Type VI secretion system mutations reduced competitive fitness of classical Vibrio cholerae biotype," Nature Communications, Nature, vol. 12(1), pages 1-11, December.
    3. Steven J. Jensen & Bonnie J. Cuthbert & Fernando Garza-Sánchez & Colette C. Helou & Rodger Miranda & Celia W. Goulding & Christopher S. Hayes, 2024. "Advanced glycation end-product crosslinking activates a type VI secretion system phospholipase effector protein," Nature Communications, Nature, vol. 15(1), pages 1-13, December.
    4. Thibault R. Bongiovanni & Casey J. Latario & Youn Cras & Evan Trus & Sophie Robitaille & Kerry Swartz & Danica Schmidtke & Maxence Vincent & Artemis Kosta & Jan Orth & Florian Stengel & Riccardo Pella, 2024. "Assembly of a unique membrane complex in type VI secretion systems of Bacteroidota," Nature Communications, Nature, vol. 15(1), pages 1-16, December.

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