IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v475y2011i7356d10.1038_nature10244.html
   My bibliography  Save this article

Type VI secretion delivers bacteriolytic effectors to target cells

Author

Listed:
  • Alistair B. Russell

    (University of Washington)

  • Rachel D. Hood

    (University of Washington)

  • Nhat Khai Bui

    (Centre for Bacterial Cell Biology, Institute for Cell and Molecular Biosciences, Newcastle University, Newcastle upon Tyne NE2 4HH, UK)

  • Michele LeRoux

    (Molecular and Cellular Biology Program, University of Washington)

  • Waldemar Vollmer

    (Centre for Bacterial Cell Biology, Institute for Cell and Molecular Biosciences, Newcastle University, Newcastle upon Tyne NE2 4HH, UK)

  • Joseph D. Mougous

    (University of Washington)

Abstract

Peptidoglycan is the major structural constituent of the bacterial cell wall, forming a meshwork outside the cytoplasmic membrane that maintains cell shape and prevents lysis. In Gram-negative bacteria, peptidoglycan is located in the periplasm, where it is protected from exogenous lytic enzymes by the outer membrane. Here we show that the type VI secretion system of Pseudomonas aeruginosa breaches this barrier to deliver two effector proteins, Tse1 and Tse3, to the periplasm of recipient cells. In this compartment, the effectors hydrolyse peptidoglycan, thereby providing a fitness advantage for P. aeruginosa cells in competition with other bacteria. To protect itself from lysis by Tse1 and Tse3, P. aeruginosa uses specific periplasmically localized immunity proteins. The requirement for these immunity proteins depends on intercellular self-intoxication through an active type VI secretion system, indicating a mechanism for export whereby effectors do not access donor cell periplasm in transit.

Suggested Citation

  • 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.
    • Handle: RePEc:nat:nature:v:475:y:2011:i:7356:d:10.1038_nature10244
    DOI: 10.1038/nature10244
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/nature10244
    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/nature10244?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. 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.
    2. Dandan Wang & Lingfang Zhu & Xiangkai Zhen & Daoyan Yang & Changfu Li & Yating Chen & Huannan Wang & Yichen Qu & Xiaozhen Liu & Yanling Yin & Huawei Gu & Lei Xu & Chuanxing Wan & Yao Wang & Songying O, 2022. "A secreted effector with a dual role as a toxin and as a transcriptional factor," Nature Communications, Nature, vol. 13(1), pages 1-15, December.
    3. Massimiliano Marazzato & Daniela Scribano & Meysam Sarshar & Francesca Brunetti & Silvia Fillo & Antonella Fortunato & Florigio Lista & Anna Teresa Palamara & Carlo Zagaglia & Cecilia Ambrosi, 2022. "Genetic Diversity of Antimicrobial Resistance and Key Virulence Features in Two Extensively Drug-Resistant Acinetobacter baumannii Isolates," IJERPH, MDPI, vol. 19(5), pages 1-14, March.
    4. Toshiki Nagakubo & Tatsuya Nishiyama & Tatsuya Yamamoto & Nobuhiko Nomura & Masanori Toyofuku, 2024. "Contractile injection systems facilitate sporogenic differentiation of Streptomyces davawensis through the action of a phage tapemeasure protein-related effector," Nature Communications, Nature, vol. 15(1), pages 1-12, 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:475:y:2011:i:7356:d:10.1038_nature10244. 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.