ArticleProceedings of the National Academy of Sciences of the United States of America2015
Structural rearrangements in the phage head-to-tail interface during assembly and infection.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.
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Who cites it
48 citing papers in PubMed.
- Cryo-EM structure of bacteriophage Nocturne116: insights into the architecture of c2-likeJournal of virology · 2026Article
- Amino acid homorepeats in tape measure proteins correlate with bacteriophage tail length.The Journal of general virology · 2026Article
- Host Range Breadth Correlates with Genic Diversity in Honeybee Phages.Genome biology and evolution · 2026Article
- Cryo-EM structures of bacteriophage T4 portal-neck assembly intermediates reveal a viral genome retention mechanism.Nature communications · 2026Article
- Structure of a Brochothrix thermosphacta bacteriophage reveals cell wall adsorption mechanism in Gram-positive infecting siphophages.Nature communications · 2026Article
- Genome anchoring, retention, and release by neck proteins of Staphylococcus phage 812.Communications biology · 2026Article
- Cryo-EM resolves the structure of the archaeal dsDNA virus HFTV1 from head to tail.Science advances · 2025Article
- Cryo-EM and cryo-ET reveal the molecular architecture and host interactions of mycobacteriophage Douge.Cell reports · 2025Article
- Article
- About bacteriophage tail terminator and tail completion proteins: structure of the proximal extremity of siphophage T5 tail.Journal of virology · 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
- Observation of Bacteriophage Ultrastructure by Cryo-Electron Microscopy.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Cryo-electron microscopy in the study of virus entry and infection.Frontiers in molecular biosciences · 2024Review
- Viral Genomic DNA Packaging Machinery.Sub-cellular biochemistry · 2024Review
- Nearly complete structure of bacteriophage DT57C reveals architecture of head-to-tail interface and lateral tail fibers.Nature communications · 2023Article
- Structure of the siphophage neck-Tail complex suggests that conserved tail tip proteins facilitate receptor binding and tail assembly.PLoS biology · 2023Article
- Structure ofViruses · 2023Article
- Insights into a viral motor: the structure of the HK97 packaging termination assembly.Nucleic acids research · 2023Article
- Structure and proposed DNA delivery mechanism of a marine roseophage.Nature communications · 2023Article
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Authors and funding
8 authors.
Funding
Abstract
Many icosahedral viruses use a specialized portal vertex to control genome encapsidation and release from the viral capsid. In tailed bacteriophages, the portal system is connected to a tail structure that provides the pipeline for genome delivery to the host cell. We report the first, to our knowledge, subnanometer structures of the complete portal-phage tail interface that mimic the states before and after DNA release during phage infection. They uncover structural rearrangements associated with intimate protein-DNA interactions. The portal protein gp6 of bacteriophage SPP1 undergoes a concerted reorganization of the structural elements of its central channel during interaction with DNA. A network of protein-protein interactions primes consecutive binding of proteins gp15 and gp16 to extend and close the channel. This critical step that prevents genome leakage from the capsid is achieved by a previously unidentified allosteric mechanism: gp16 binding to two different regions of gp15 drives correct positioning and folding of an inner gp16 loop to interact with equivalent loops of the other gp16 subunits. Together, these loops build a plug that closes the channel. Gp16 then fastens the tail to yield the infectious virion. The gatekeeper system opens for viral genome exit at the beginning of infection but recloses afterward, suggesting a molecular diaphragm-like mechanism to control DNA efflux. The mechanisms described here, controlling the essential steps of phage genome movements during virus assembly and infection, are likely to be conserved among long-tailed phages, the largest group of viruses in the Biosphere.
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