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Structural assembly of the tailed bacteriophage ϕ29

Author

Listed:
  • Jingwei Xu

    (Tsinghua University
    Eidgenössische Technische Hochschule Zürich)

  • Dianhong Wang

    (Tsinghua University)

  • Miao Gui

    (Tsinghua University
    Harvard Medical School)

  • Ye Xiang

    (Tsinghua University)

Abstract

The mature virion of the tailed bacteriophage ϕ29 is an ~33 MDa complex that contains more than 450 subunits of seven structural proteins assembling into a prolate head and a short non-contractile tail. Here, we report the near-atomic structures of the ϕ29 pre-genome packaging head (prohead), the mature virion and the genome-emptied virion. Structural comparisons suggest local rotation or oscillation of the head-tail connector upon DNA packaging and release. Termination of the DNA packaging occurs through pressure-dependent correlative positional and conformational changes in the connector. The funnel-shaped tail lower collar attaches the expanded narrow end of the connector and has a 180-Å long, 24-strand β barrel narrow stem tube that undergoes conformational changes upon genome release. The appendages form an interlocked assembly attaching the tail around the collar. The membrane active long loops at the distal end of the tail knob exit during the late stage of infection and form the cone-shaped tip of a largely hydrophobic helix barrel, prepared for membrane penetration.

Suggested Citation

  • Jingwei Xu & Dianhong Wang & Miao Gui & Ye Xiang, 2019. "Structural assembly of the tailed bacteriophage ϕ29," Nature Communications, Nature, vol. 10(1), pages 1-16, December.
    • Handle: RePEc:nat:natcom:v:10:y:2019:i:1:d:10.1038_s41467-019-10272-3
    DOI: 10.1038/s41467-019-10272-3
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    Cited by:

    1. Igor Orlov & Stéphane Roche & Sandrine Brasilès & Natalya Lukoyanova & Marie-Christine Vaney & Paulo Tavares & Elena V. Orlova, 2022. "CryoEM structure and assembly mechanism of a bacterial virus genome gatekeeper," Nature Communications, Nature, vol. 13(1), pages 1-12, December.

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