IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v483y2012i7388d10.1038_nature10846.html
   My bibliography  Save this article

Type VI secretion requires a dynamic contractile phage tail-like structure

Author

Listed:
  • M. Basler

    (Harvard Medical School, 200 Longwood Avenue, Boston, Massachusetts 02115, USA)

  • M. Pilhofer

    (California Institute of Technology, 1200 East California Boulevard, Pasadena, California 91125, USA
    Howard Hughes Medical Institute, California Institute of Technology, 1200 East California Boulevard, Pasadena, California 91125, USA)

  • G. P. Henderson

    (California Institute of Technology, 1200 East California Boulevard, Pasadena, California 91125, USA)

  • G. J. Jensen

    (California Institute of Technology, 1200 East California Boulevard, Pasadena, California 91125, USA
    Howard Hughes Medical Institute, California Institute of Technology, 1200 East California Boulevard, Pasadena, California 91125, USA)

  • J. J. Mekalanos

    (Harvard Medical School, 200 Longwood Avenue, Boston, Massachusetts 02115, USA)

Abstract

Type VI secretion systems are bacterial virulence-associated nanomachines composed of proteins that are evolutionarily related to components of bacteriophage tails. Here we show that protein secretion by the type VI secretion system of Vibrio cholerae requires the action of a dynamic intracellular tubular structure that is structurally and functionally homologous to contractile phage tail sheath. Time-lapse fluorescence light microscopy reveals that sheaths of the type VI secretion system cycle between assembly, quick contraction, disassembly and re-assembly. Whole-cell electron cryotomography further shows that the sheaths appear as long tubular structures in either extended or contracted conformations that are connected to the inner membrane by a distinct basal structure. These data support a model in which the contraction of the type VI secretion system sheath provides the energy needed to translocate proteins out of effector cells and into adjacent target cells.

Suggested Citation

  • M. Basler & M. Pilhofer & G. P. Henderson & G. J. Jensen & J. J. Mekalanos, 2012. "Type VI secretion requires a dynamic contractile phage tail-like structure," Nature, Nature, vol. 483(7388), pages 182-186, March.
    • Handle: RePEc:nat:nature:v:483:y:2012:i:7388:d:10.1038_nature10846
    DOI: 10.1038/nature10846
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/nature10846
    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/nature10846?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. Katarzyna Kanarek & Chaya Mushka Fridman & Eran Bosis & Dor Salomon, 2023. "The RIX domain defines a class of polymorphic T6SS effectors and secreted adaptors," Nature Communications, Nature, vol. 14(1), pages 1-13, December.
    2. Brooke K. Hayes & Marina Harper & Hariprasad Venugopal & Jessica M. Lewis & Amy Wright & Han-Chung Lee & Joel R. Steele & David L. Steer & Ralf B. Schittenhelm & John D. Boyce & Sheena McGowan, 2024. "Structure of a Rhs effector clade domain provides mechanistic insights into type VI secretion system toxin delivery," Nature Communications, Nature, vol. 15(1), pages 1-15, December.
    3. Ana Teresa López-Jiménez & Serge Mostowy, 2021. "Emerging technologies and infection models in cellular microbiology," Nature Communications, Nature, vol. 12(1), pages 1-13, December.
    4. 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.
    5. 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:483:y:2012:i:7388:d:10.1038_nature10846. 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.