ArticleScientific reports2017
High affinity anchoring of the decoration protein pb10 onto the bacteriophage T5 capsid.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 30 citations in OpenAlex.
- About proteins of a siphophage tail tip complex reverting to their pre-ejection fold after DNA ejection.Nature communications · 2025Article
- Atlas of Interactions Between Decoration Proteins and Major Capsid Proteins of Coliphage N4.Viruses · 2024Article
- Structure and replication of Pseudomonas aeruginosa phage JBD30.The EMBO journal · 2024Article
- Structures of Mature and Urea-Treated Empty Bacteriophage T5: Insights into Siphophage Infection and DNA Ejection.International journal of molecular sciences · 2024Article
- Antigen self-anchoring onto bacteriophage T5 capsid-like particles for vaccine design.NPJ vaccines · 2024Article
- Cryo-EM structure of a Shigella podophage reveals a hybrid tail and novel decoration proteins.Structure (London, England : 1993) · 2024Article
- Structure and Function of Hoc-A Novel Environment Sensing Device Encoded by T4 and Other Bacteriophages.Viruses · 2023Article
- Article
- A lipopolysaccharide-dependent phage infects a pseudomonad phytopathogen and can evolve to evade phage resistance.Environmental microbiology · 2022Article
- Strategies for Bacteriophage T5 Mutagenesis: Expanding the Toolbox for Phage Genome Engineering.Frontiers in microbiology · 2021Article
- The Missing Tailed Phages: Prediction of Small Capsid Candidates.Microorganisms · 2020Article
- Keeping It Together: Structures, Functions, and Applications of Viral Decoration Proteins.Viruses · 2020Review
- Ecology, Structure, and Evolution ofAnnual review of virology · 2020Review
- Article
- A cornucopia of Shigella phages from the Cornhusker State.Virology · 2019Article
- Capsid expansion of bacteriophage T5 revealed by high resolution cryoelectron microscopy.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- The phage L capsid decoration protein has a novel OB-fold and an unusual capsid binding strategy.eLife · 2019Article
- Shigella Phages Isolated during a Dysentery Outbreak Reveal Uncommon Structures and Broad Species Diversity.Journal of virology · 2018Article
Corrections and comments
- Erratum issued
Authors and funding
15 authors at 7 institutions in 3 countries.
Funding
Abstract
Bacteriophage capsids constitute icosahedral shells of exceptional stability that protect the viral genome. Many capsids display on their surface decoration proteins whose structure and function remain largely unknown. The decoration protein pb10 of phage T5 binds at the centre of the 120 hexamers formed by the major capsid protein. Here we determined the 3D structure of pb10 and investigated its capsid-binding properties using NMR, SAXS, cryoEM and SPR. Pb10 consists of an α-helical capsid-binding domain and an Ig-like domain exposed to the solvent. It binds to the T5 capsid with a remarkably high affinity and its binding kinetics is characterized by a very slow dissociation rate. We propose that the conformational exchange events observed in the capsid-binding domain enable rearrangements upon binding that contribute to the quasi-irreversibility of the pb10-capsid interaction. Moreover we show that pb10 binding is a highly cooperative process, which favours immediate rebinding of newly dissociated pb10 to the 120 hexamers of the capsid protein. In extreme conditions, pb10 protects the phage from releasing its genome. We conclude that pb10 may function to reinforce the capsid thus favouring phage survival in harsh environments.
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Registered trials
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.