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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
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    Cited by:

    1. 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.
    2. 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.
    3. 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.
    4. 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.
    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.

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