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Portal protein functions akin to a DNA-sensor that couples genome-packaging to icosahedral capsid maturation

Author

Listed:
  • Ravi K. Lokareddy

    (Thomas Jefferson University)

  • Rajeshwer S. Sankhala

    (Thomas Jefferson University)

  • Ankoor Roy

    (Thomas Jefferson University
    Rutgers University)

  • Pavel V. Afonine

    (Lawrence Berkeley National Laboratory)

  • Tina Motwani

    (University of Connecticut)

  • Carolyn M. Teschke

    (University of Connecticut)

  • Kristin N. Parent

    (Michigan State University)

  • Gino Cingolani

    (Thomas Jefferson University
    Institute of Biomembranes and Bioenergetics, National Research Council)

Abstract

Tailed bacteriophages and herpesviruses assemble infectious particles via an empty precursor capsid (or ‘procapsid’) built by multiple copies of coat and scaffolding protein and by one dodecameric portal protein. Genome packaging triggers rearrangement of the coat protein and release of scaffolding protein, resulting in dramatic procapsid lattice expansion. Here, we provide structural evidence that the portal protein of the bacteriophage P22 exists in two distinct dodecameric conformations: an asymmetric assembly in the procapsid (PC-portal) that is competent for high affinity binding to the large terminase packaging protein, and a symmetric ring in the mature virion (MV-portal) that has negligible affinity for the packaging motor. Modelling studies indicate the structure of PC-portal is incompatible with DNA coaxially spooled around the portal vertex, suggesting that newly packaged DNA triggers the switch from PC- to MV-conformation. Thus, we propose the signal for termination of ‘Headful Packaging’ is a DNA-dependent symmetrization of portal protein.

Suggested Citation

  • Ravi K. Lokareddy & Rajeshwer S. Sankhala & Ankoor Roy & Pavel V. Afonine & Tina Motwani & Carolyn M. Teschke & Kristin N. Parent & Gino Cingolani, 2017. "Portal protein functions akin to a DNA-sensor that couples genome-packaging to icosahedral capsid maturation," Nature Communications, Nature, vol. 8(1), pages 1-11, April.
    • Handle: RePEc:nat:natcom:v:8:y:2017:i:1:d:10.1038_ncomms14310
    DOI: 10.1038/ncomms14310
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    Cited by:

    1. Marta Šiborová & Tibor Füzik & Michaela Procházková & Jiří Nováček & Martin Benešík & Anders S. Nilsson & Pavel Plevka, 2022. "Tail proteins of phage SU10 reorganize into the nozzle for genome delivery," Nature Communications, Nature, vol. 13(1), pages 1-13, December.
    2. 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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