Document Type
Article
Publication Date
7-8-2023
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.
Recommended Citation
Li, Fenglin; Hou, Chun-Feng; Lokareddy, Ravi K.; Yang, Ruoyu; Forti, Francesca; Briani, Federica; and Cingolani, Gino, "High-Resolution Cryo-EM Structure of the Pseudomonas Bacteriophage E217" (2023). Department of Biochemistry and Molecular Biology Faculty Papers. Paper 242.
https://jdc.jefferson.edu/bmpfp/242
Creative Commons License
This work is licensed under a Creative Commons Attribution-Share Alike 4.0 License.
PubMed ID
37422479
Language
English
Comments
This article is the author’s final published version in Nature Communications, Volume 14, 2023, Article number 4052.
The published version is available at https://doi.org/10.1038/s41467-023-39756-z. © 2023. The Author(s).