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Action of a minimal contractile bactericidal nanomachine

Author

Listed:
  • Peng Ge

    (University of California, Los Angeles (UCLA)
    University of California, Los Angeles (UCLA))

  • Dean Scholl

    (Pylum Biosciences)

  • Nikolai S. Prokhorov

    (University of Texas Medical Branch, Department of Biochemistry and Molecular Biology, Sealy Center for Structural Biology and Molecular Biophysics)

  • Jaycob Avaylon

    (University of California, Los Angeles (UCLA)
    University of California, Los Angeles (UCLA))

  • Mikhail M. Shneider

    (Laboratory of Molecular Bioengineering)

  • Christopher Browning

    (Vertex Pharmaceuticals (Europe) Ltd)

  • Sergey A. Buth

    (University of Texas Medical Branch, Department of Biochemistry and Molecular Biology, Sealy Center for Structural Biology and Molecular Biophysics)

  • Michel Plattner

    (University of Texas Medical Branch, Department of Biochemistry and Molecular Biology, Sealy Center for Structural Biology and Molecular Biophysics)

  • Urmi Chakraborty

    (Pylum Biosciences)

  • Ke Ding

    (University of California, Los Angeles (UCLA)
    University of California, Los Angeles (UCLA))

  • Petr G. Leiman

    (University of Texas Medical Branch, Department of Biochemistry and Molecular Biology, Sealy Center for Structural Biology and Molecular Biophysics)

  • Jeff F. Miller

    (University of California, Los Angeles (UCLA)
    University of California, Los Angeles (UCLA))

  • Z. Hong Zhou

    (University of California, Los Angeles (UCLA)
    University of California, Los Angeles (UCLA))

Abstract

R-type bacteriocins are minimal contractile nanomachines that hold promise as precision antibiotics1–4. Each bactericidal complex uses a collar to bridge a hollow tube with a contractile sheath loaded in a metastable state by a baseplate scaffold1,2. Fine-tuning of such nucleic acid-free protein machines for precision medicine calls for an atomic description of the entire complex and contraction mechanism, which is not available from baseplate structures of the (DNA-containing) T4 bacteriophage5. Here we report the atomic model of the complete R2 pyocin in its pre-contraction and post-contraction states, each containing 384 subunits of 11 unique atomic models of 10 gene products. Comparison of these structures suggests the following sequence of events during pyocin contraction: tail fibres trigger lateral dissociation of baseplate triplexes; the dissociation then initiates a cascade of events leading to sheath contraction; and this contraction converts chemical energy into mechanical force to drive the iron-tipped tube across the bacterial cell surface, killing the bacterium.

Suggested Citation

  • Peng Ge & Dean Scholl & Nikolai S. Prokhorov & Jaycob Avaylon & Mikhail M. Shneider & Christopher Browning & Sergey A. Buth & Michel Plattner & Urmi Chakraborty & Ke Ding & Petr G. Leiman & Jeff F. Mi, 2020. "Action of a minimal contractile bactericidal nanomachine," Nature, Nature, vol. 580(7805), pages 658-662, April.
  • Handle: RePEc:nat:nature:v:580:y:2020:i:7805:d:10.1038_s41586-020-2186-z
    DOI: 10.1038/s41586-020-2186-z
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    Cited by:

    1. Latinovic, Zoran & Chatterjee, Sharmila C., 2022. "Achieving the promise of AI and ML in delivering economic and relational customer value in B2B," Journal of Business Research, Elsevier, vol. 144(C), pages 966-974.
    2. Ravi R. Sonani & Lee K. Palmer & Nathaniel C. Esteves & Abigail A. Horton & Amanda L. Sebastian & Rebecca J. Kelly & Fengbin Wang & Mark A. B. Kreutzberger & William K. Russell & Petr G. Leiman & Birg, 2024. "An extensive disulfide bond network prevents tail contraction in Agrobacterium tumefaciens phage Milano," Nature Communications, Nature, vol. 15(1), pages 1-15, December.
    3. Xiaoying Cai & Yao He & Iris Yu & Anthony Imani & Dean Scholl & Jeff F. Miller & Z. Hong Zhou, 2024. "Atomic structures of a bacteriocin targeting Gram-positive bacteria," Nature Communications, Nature, vol. 15(1), pages 1-13, December.
    4. Fenglin Li & Chun-Feng David Hou & Ravi K. Lokareddy & Ruoyu Yang & Francesca Forti & Federica Briani & Gino Cingolani, 2023. "High-resolution cryo-EM structure of the Pseudomonas bacteriophage E217," Nature Communications, Nature, vol. 14(1), pages 1-16, December.

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