ArticleThe Journal of biological chemistry2015
Bacteriophage SPP1 tail tube protein self-assembles into β-structure-rich tubes.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 28 citations in OpenAlex.
- Specialized Listeria monocytogenes produce tailocins to provide a population-level competitive growth advantage.Nature microbiology · 2024Article
- Structure of the siphophage neck-Tail complex suggests that conserved tail tip proteins facilitate receptor binding and tail assembly.PLoS biology · 2023Article
- Conformational dynamics control assembly of an extremely long bacteriophage tail tube.The Journal of biological chemistry · 2023Article
- Tall tails: cryo-electron microscopy of phage tail DNA ejection conduits.Biochemical Society transactions · 2022Article
- Article
- Architecture of the flexible tail tube of bacteriophage SPP1.Nature communications · 2020Article
- Structure of the host cell recognition and penetration machinery of a Staphylococcus aureus bacteriophage.PLoS pathogens · 2020Article
- Mobile Loops and Electrostatic Interactions Maintain the Flexible Tail Tube of Bacteriophage Lambda.Journal of molecular biology · 2020Article
- Self-Assembly of Tail Tube Protein of Bacteriophage vB_EcoS_NBD2 into Extremely Long Polytubes inViruses · 2019Article
- Article
- Protein-Protein Interfaces Probed by Methyl Labeling and Proton-Detected Solid-State NMR Spectroscopy.Chemphyschem : a European journal of chemical physics and physical chemistry · 2018Article
- Bacteriophage T5 tail tube structure suggests a trigger mechanism for Siphoviridae DNA ejection.Nature communications · 2017Article
- Bacteriophage Tail-Tube Assembly Studied by Proton-Detected 4D Solid-State NMR.Angewandte Chemie (International ed. in English) · 2017Article
- Functional and structural dissection of the tape measure protein of lactococcal phage TP901-1.Scientific reports · 2016Article
- Structural rearrangements in the phage head-to-tail interface during assembly and infection.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
Corrections and comments
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Authors and funding
15 authors at 7 institutions in 3 countries.
Funding
Abstract
The majority of known bacteriophages have long tails that serve for bacterial target recognition and viral DNA delivery into the host. These structures form a tube from the viral capsid to the bacterial cell. The tube is formed primarily by a helical array of tail tube protein (TTP) subunits. In phages with a contractile tail, the TTP tube is surrounded by a sheath structure. Here, we report the first evidence that a phage TTP, gp17.1 of siphophage SPP1, self-assembles into long tubes in the absence of other viral proteins. gp17.1 does not exhibit a stable globular structure when monomeric in solution, even if it was confidently predicted to adopt the β-sandwich fold of phage λ TTP. However, Fourier transform infrared and nuclear magnetic resonance spectroscopy analyses showed that its β-sheet content increases significantly during tube assembly, suggesting that gp17.1 acquires a stable β-sandwich fold only after self-assembly. EM analyses revealed that the tube is formed by hexameric rings stacked helicoidally with the same organization and helical parameters found for the tail of SPP1 virions. These parameters were used to build a pseudo-atomic model of the TTP tube. The large loop spanning residues 40-56 is located on the inner surface of the tube, at the interface between adjacent monomers and hexamers. In line with our structural predictions, deletion of this loop hinders gp17.1 tube assembly in vitro and interferes with SPP1 tail assembly during phage particle morphogenesis in bacteria.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.