ArticleJournal of virology2014
Insights into bacteriophage T5 structure from analysis of its morphogenesis genes and protein components.
Article in Journal of virology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.
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Who cites it
56 citing papers in PubMed.
- Article
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- Bacterial Schlafen proteins mediate phage defence.Nature microbiology · 2026Article
- A dramatic protein fold switch powers a bactericidal nanomachine.bioRxiv : the preprint server for biology · 2026Article
- Characterization and comparative genome analysis of a new Tequintavirus isolated on Salmonella enterica serotype Tennessee.BMC research notes · 2025Article
- Bacterial Schlafens mediate anti-phage defense.bioRxiv : the preprint server for biology · 2025Article
- Global structural survey of the flagellotropic myophage φTE infecting agricultural pathogen Pectobacterium atrosepticum.Nature communications · 2025Article
- Completing the BASEL phage collection to unlock hidden diversity for systematic exploration of phage-host interactions.PLoS biology · 2025Article
- Reply to: About proteins of a siphophage tail tip complex reverting to their pre-ejection fold after DNA ejection.Nature communications · 2025Article
- About proteins of a siphophage tail tip complex reverting to their pre-ejection fold after DNA ejection.Nature communications · 2025Article
- About bacteriophage tail terminator and tail completion proteins: structure of the proximal extremity of siphophage T5 tail.Journal of virology · 2025Article
- Exploring Viral Interactions inLife (Basel, Switzerland) · 2025Article
- Structures of Mature and Urea-Treated Empty Bacteriophage T5: Insights into Siphophage Infection and DNA Ejection.International journal of molecular sciences · 2024Article
- Dual function of a highly conserved bacteriophage tail completion protein essential for bacteriophage infectivity.Communications biology · 2024Article
- Antigen self-anchoring onto bacteriophage T5 capsid-like particles for vaccine design.NPJ vaccines · 2024Article
- Nearly complete structure of bacteriophage DT57C reveals architecture of head-to-tail interface and lateral tail fibers.Nature communications · 2023Article
- Molecular Characterization ofMicroorganisms · 2023Article
- The saclayvirus Aci01-1 very long and complex fiber and its receptor at the Acinetobacter baumannii surface.Archives of virology · 2023Article
- Broad-host-range lytic Erwinia phage Key with exopolysaccharide degrading activity.Virus research · 2023Article
- Deciphering Bacteriophage T5 Host Recognition Mechanism and Infection Trigger.Journal of virology · 2023Article
Corrections and comments
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Authors and funding
12 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bacteriophage T5 represents a large family of lytic Siphoviridae infecting Gram-negative bacteria. The low-resolution structure of T5 showed the T=13 geometry of the capsid and the unusual trimeric organization of the tail tube, and the assembly pathway of the capsid was established. Although major structural proteins of T5 have been identified in these studies, most of the genes encoding the morphogenesis proteins remained to be identified. Here, we combine a proteomic analysis of T5 particles with a bioinformatic study and electron microscopic immunolocalization to assign function to the genes encoding the structural proteins, the packaging proteins, and other nonstructural components required for T5 assembly. A head maturation protease that likely accounts for the cleavage of the different capsid proteins is identified. Two other proteins involved in capsid maturation add originality to the T5 capsid assembly mechanism: the single head-to-tail joining protein, which closes the T5 capsid after DNA packaging, and the nicking endonuclease responsible for the single-strand interruptions in the T5 genome. We localize most of the tail proteins that were hitherto uncharacterized and provide a detailed description of the tail tip composition. Our findings highlight novel variations of viral assembly strategies and of virion particle architecture. They further recommend T5 for exploring phage structure and assembly and for deciphering conformational rearrangements that accompany DNA transfer from the capsid to the host cytoplasm.
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