Structure and replication of Pseudomonas aeruginosa phage JBD30
Language English Country Great Britain, England Media print-electronic
Document type Journal Article
Grant support
101043452
EC | European Research Council (ERC)
LX22NPO5103
EC | HORIZON EUROPE Framework Programme (Horizon Europe)
LM2023050
Ministerstvo Školství, Mládeže a Tělovýchovy (MŠMT)
LM2023042
Ministerstvo Školství, Mládeže a Tělovýchovy (MŠMT)
90254
Ministerstvo Školství, Mládeže a Tělovýchovy (MŠMT)
N/A
Brno city municipality
PubMed
39143239
PubMed Central
PMC11445458
DOI
10.1038/s44318-024-00195-1
PII: 10.1038/s44318-024-00195-1
Knihovny.cz E-resources
- Keywords
- Pseudomonas aeruginosa, Cryo-EM, Phage, Pili, Structure,
- MeSH
- Fimbriae, Bacterial metabolism ultrastructure virology MeSH
- DNA, Viral metabolism genetics MeSH
- Cryoelectron Microscopy * MeSH
- Pseudomonas Phages * ultrastructure genetics metabolism physiology MeSH
- Pseudomonas aeruginosa * virology metabolism MeSH
- Virus Replication * MeSH
- Siphoviridae genetics ultrastructure physiology metabolism MeSH
- Capsid Proteins metabolism chemistry genetics MeSH
- Publication type
- Journal Article MeSH
- Names of Substances
- DNA, Viral MeSH
- Capsid Proteins MeSH
Bacteriophages are the most abundant biological entities on Earth, but our understanding of many aspects of their lifecycles is still incomplete. Here, we have structurally analysed the infection cycle of the siphophage Casadabanvirus JBD30. Using its baseplate, JBD30 attaches to Pseudomonas aeruginosa via the bacterial type IV pilus, whose subsequent retraction brings the phage to the bacterial cell surface. Cryo-electron microscopy structures of the baseplate-pilus complex show that the tripod of baseplate receptor-binding proteins attaches to the outer bacterial membrane. The tripod and baseplate then open to release three copies of the tape-measure protein, an event that is followed by DNA ejection. JBD30 major capsid proteins assemble into procapsids, which expand by 7% in diameter upon filling with phage dsDNA. The DNA-filled heads are finally joined with 180-nm-long tails, which bend easily because flexible loops mediate contacts between the successive discs of major tail proteins. It is likely that the structural features and replication mechanisms described here are conserved among siphophages that utilize the type IV pili for initial cell attachment.
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