High-resolution cryo-EM structure of the Pseudomonas bacteriophage E217

Fenglin Li, Chun-Feng David Hou, Ravi K. Lokareddy, Ruoyu Yang, Francesca Forti, Federica Briani () and Gino Cingolani ()
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Fenglin Li: Thomas Jefferson University
Chun-Feng David Hou: Thomas Jefferson University
Ravi K. Lokareddy: Thomas Jefferson University
Ruoyu Yang: Thomas Jefferson University
Francesca Forti: Università degli Studi di Milano
Federica Briani: Università degli Studi di Milano
Gino Cingolani: Thomas Jefferson University

Nature Communications, 2023, vol. 14, issue 1, 1-16

Abstract: Abstract E217 is a Pseudomonas phage used in an experimental cocktail to eradicate cystic fibrosis-associated Pseudomonas aeruginosa. Here, we describe the structure of the whole E217 virion before and after DNA ejection at 3.1 Å and 4.5 Å resolution, respectively, determined using cryogenic electron microscopy (cryo-EM). We identify and build de novo structures for 19 unique E217 gene products, resolve the tail genome-ejection machine in both extended and contracted states, and decipher the complete architecture of the baseplate formed by 66 polypeptide chains. We also determine that E217 recognizes the host O-antigen as a receptor, and we resolve the N-terminal portion of the O-antigen-binding tail fiber. We propose that E217 design principles presented in this paper are conserved across PB1-like Myoviridae phages of the Pbunavirus genus that encode a ~1.4 MDa baseplate, dramatically smaller than the coliphage T4.

Date: 2023
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DOI: 10.1038/s41467-023-39756-z

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