Structural highlights
Function
A0A2K8HL59_9CAUD
Publication Abstract from PubMed
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 A and 4.5 A 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.
High-resolution cryo-EM structure of the Pseudomonas bacteriophage E217.,Li F, Hou CD, Lokareddy RK, Yang R, Forti F, Briani F, Cingolani G Nat Commun. 2023 Jul 8;14(1):4052. doi: 10.1038/s41467-023-39756-z. PMID:37422479[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Li F, Hou CD, Lokareddy RK, Yang R, Forti F, Briani F, Cingolani G. High-resolution cryo-EM structure of the Pseudomonas bacteriophage E217. Nat Commun. 2023 Jul 8;14(1):4052. PMID:37422479 doi:10.1038/s41467-023-39756-z
