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- Title
High-resolution cryo-EM structure of the Pseudomonas bacteriophage E217.
- Authors
Li, Fenglin; Hou, Chun-Feng David; Lokareddy, Ravi K.; Yang, Ruoyu; Forti, Francesca; Briani, Federica; Cingolani, Gino
- 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. E217 is a Myoviridae used in an experimental phage cocktail to eradicate Pseudomonas aeruginosa. Here, the authors utilize cryo-EM and functional analysis to delineate E217 structural proteins, tail dynamics, and mechanisms of host recognition.
- Subjects
BACTERIOPHAGE T4; PSEUDOMONAS; CYTOSKELETAL proteins; ELECTRON microscopy; FUNCTIONAL analysis; BACTERIOPHAGES; PSEUDOMONAS aeruginosa
- Publication
Nature Communications, 2023, Vol 14, Issue 1, p1
- ISSN
2041-1723
- Publication type
Article
- DOI
10.1038/s41467-023-39756-z