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Architecture and self-assembly of the jumbo bacteriophage nuclear shell

Author

Listed:
  • Thomas G. Laughlin

    (University of California San Diego)

  • Amar Deep

    (University of California San Diego)

  • Amy M. Prichard

    (University of California San Diego)

  • Christian Seitz

    (University of California San Diego)

  • Yajie Gu

    (University of California San Diego)

  • Eray Enustun

    (University of California San Diego)

  • Sergey Suslov

    (University of California San Diego)

  • Kanika Khanna

    (University of California San Diego
    University of California)

  • Erica A. Birkholz

    (University of California San Diego)

  • Emily Armbruster

    (University of California San Diego)

  • J. Andrew McCammon

    (University of California San Diego
    University of California San Diego)

  • Rommie E. Amaro

    (University of California San Diego)

  • Joe Pogliano

    (University of California San Diego)

  • Kevin D. Corbett

    (University of California San Diego
    University of California San Diego)

  • Elizabeth Villa

    (University of California San Diego
    University of California San Diego)

Abstract

Bacteria encode myriad defences that target the genomes of infecting bacteriophage, including restriction–modification and CRISPR–Cas systems1. In response, one family of large bacteriophages uses a nucleus-like compartment to protect its replicating genomes by excluding host defence factors2–4. However, the principal composition and structure of this compartment remain unknown. Here we find that the bacteriophage nuclear shell assembles primarily from one protein, which we name chimallin (ChmA). Combining cryo-electron tomography of nuclear shells in bacteriophage-infected cells and cryo-electron microscopy of a minimal chimallin compartment in vitro, we show that chimallin self-assembles as a flexible sheet into closed micrometre-scale compartments. The architecture and assembly dynamics of the chimallin shell suggest mechanisms for its nucleation and growth, and its role as a scaffold for phage-encoded factors mediating macromolecular transport, cytoskeletal interactions, and viral maturation.

Suggested Citation

  • Thomas G. Laughlin & Amar Deep & Amy M. Prichard & Christian Seitz & Yajie Gu & Eray Enustun & Sergey Suslov & Kanika Khanna & Erica A. Birkholz & Emily Armbruster & J. Andrew McCammon & Rommie E. Ama, 2022. "Architecture and self-assembly of the jumbo bacteriophage nuclear shell," Nature, Nature, vol. 608(7922), pages 429-435, August.
    • Handle: RePEc:nat:nature:v:608:y:2022:i:7922:d:10.1038_s41586-022-05013-4
    DOI: 10.1038/s41586-022-05013-4
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    Cited by:

    1. Eliza S. Nieweglowska & Axel F. Brilot & Melissa Méndez-Moran & Claire Kokontis & Minkyung Baek & Junrui Li & Yifan Cheng & David Baker & Joseph Bondy-Denomy & David A. Agard, 2023. "The ϕPA3 phage nucleus is enclosed by a self-assembling 2D crystalline lattice," Nature Communications, Nature, vol. 14(1), pages 1-12, December.
    2. Andrea Fossati & Deepto Mozumdar & Claire Kokontis & Melissa Mèndez-Moran & Eliza Nieweglowska & Adrian Pelin & Yuping Li & Baron Guo & Nevan J. Krogan & David A. Agard & Joseph Bondy-Denomy & Daniell, 2023. "Next-generation proteomics for quantitative Jumbophage-bacteria interaction mapping," Nature Communications, Nature, vol. 14(1), pages 1-16, December.
    3. Pankaj Sharma & Elena Maklashina & Markus Voehler & Sona Balintova & Sarka Dvorakova & Michal Kraus & Katerina Hadrava Vanova & Zuzana Nahacka & Renata Zobalova & Stepana Boukalova & Kristyna Cunatova, 2024. "Disordered-to-ordered transitions in assembly factors allow the complex II catalytic subunit to switch binding partners," Nature Communications, Nature, vol. 15(1), pages 1-15, December.

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