Architecture and self-assembly of the jumbo bacteriophage nuclear shell

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. Amaro, Joe Pogliano (), Kevin D. Corbett () and Elizabeth Villa ()
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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
Erica A. Birkholz: University of California San Diego
Emily Armbruster: University of California San Diego
J. Andrew McCammon: 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
Elizabeth Villa: University of California San Diego

Nature, 2022, vol. 608, issue 7922, 429-435

Abstract: 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.

Date: 2022
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DOI: 10.1038/s41586-022-05013-4

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