IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v523y2015i7562d10.1038_nature14667.html
   My bibliography  Save this article

Biogenesis and structure of a type VI secretion membrane core complex

Author

Listed:
  • 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
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/nature14667
    File Function: Abstract
    Download Restriction: Access to the full text of the articles in this series is restricted.
    File URL: https://libkey.io/10.1038/nature14667?utm_source=ideas
    LibKey link: if access is restricted and if your library uses this service, LibKey will redirect you to where you can use your library subscription to access this item
    ---><---

    As the access to this document is restricted, you may want to search for a different version of it.

    Citations

    Citations are extracted by the CitEc Project, subscribe to its RSS feed for this item.
    as


    Cited by:

    1. 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.
    2. 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.
    3. 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.

    More about this item

    Statistics

    Access and download statistics

    Corrections

    All material on this site has been provided by the respective publishers and authors. You can help correct errors and omissions. When requesting a correction, please mention this item's handle: RePEc:nat:nature:v:523:y:2015:i:7562:d:10.1038_nature14667. See general information about how to correct material in RePEc.

    If you have authored this item and are not yet registered with RePEc, we encourage you to do it here. This allows to link your profile to this item. It also allows you to accept potential citations to this item that we are uncertain about.

    We have no bibliographic references for this item. You can help adding them by using this form .

    If you know of missing items citing this one, you can help us creating those links by adding the relevant references in the same way as above, for each refering item. If you are a registered author of this item, you may also want to check the "citations" tab in your RePEc Author Service profile, as there may be some citations waiting for confirmation.

    For technical questions regarding this item, or to correct its authors, title, abstract, bibliographic or download information, contact: Sonal Shukla or Springer Nature Abstracting and Indexing (email available below). General contact details of provider: http://www.nature.com .

    Please note that corrections may take a couple of weeks to filter through the various RePEc services.

    IDEAS is a RePEc service. RePEc uses bibliographic data supplied by the respective publishers.