ArticleStructure (London, England : 1993)2024
Cryo-EM structure of a Shigella podophage reveals a hybrid tail and novel decoration proteins.
Article in Structure (London, England : 1993), 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 13 citations in OpenAlex.
- Insights into Genome Ejection by a Therapeutic phiKMV-like Bacteriophage.Journal of molecular biology · 2026Article
- Novel Koutsourovirus phages disrupt clinical multidrug-resistant Enterobacter cloacae biofilms: genomic and functional characterization.Folia microbiologica · 2026Article
- TheJournal of virology · 2025Article
- High-resolution Cryo-EM Analysis of the Therapeutic Pseudomonas Phage Pa223.Journal of molecular biology · 2025Article
- Elucidating double stranded DNA viral scaffolding protein structures through advances in cryogenic electron microscopy data processing.Current opinion in structural biology · 2025Review
- Article
- Moo19 and B2: Structures ofScience advances · 2024Article
- Isolation, characterization, and receptor-binding protein specificity of phages PAS7, PAS59 and PAS61 infecting Shiga toxin-producing Escherichia coli O103 and O146.Scientific reports · 2024Article
- Ejectosome ofPNAS nexus · 2024Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
There is a paucity of high-resolution structures of phages infecting Shigella, a human pathogen and a serious threat to global health. HRP29 is a Shigella podophage belonging to the Autographivirinae family, and has very low sequence identity to other known phages. Here, we resolved the structure of the entire HRP29 virion by cryo-EM. Phage HRP29 has a highly unusual tail that is a fusion of a T7-like tail tube and P22-like tailspikes mediated by interactions from a novel tailspike adaptor protein. Understanding phage tail structures is critical as they mediate hosts interactions. Furthermore, we show that the HRP29 capsid is stabilized by two novel, and essential decoration proteins, gp47 and gp48. Only one high resolution structure is currently available for Shigella podophages. The presence of a hybrid tail and an adapter protein suggests that it may be a product of horizontal gene transfer, and may be prevalent in other phages.
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