ArticleNature communications2024
Structural mechanism of bacteriophage lambda tail's interaction with the bacterial receptor.
Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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Who cites it
37 citing papers in PubMed.
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- Biophysical and functional characterization of the Escherichia coli Dr fimbrial envelope reveals its importance for pathogenesis and lithogenesis.PLoS pathogens · 2026Article
- Phage therapy: from basic biology to clinical application.Nature reviews. Microbiology · 2026Review
- Novel LyticViruses · 2026Article
- Lethal permeabilization of host bacteria to small-molecule compounds during phage penetration.Nature communications · 2026Article
- Cryo-EM reveals a conserved baseplate architecture and distinct accessory protein assemblies in mycobacteriophages Claus, Corndog and Mysterious.Research square · 2026Article
- Dynamic adhesion device of phage OE33PA drives Gram-positive host recognition.bioRxiv : the preprint server for biology · 2026Article
- Diversity-generating retroelements for programmable targeted hypermutagenesis.Nature biotechnology · 2026Article
- Article
- From structure to design: experimental and AI-driven approaches in receptor-binding protein engineering for reprogramming phage host range.Archives of microbiology · 2026Review
- Review
- Resolution of a T1-Like Bacteriophage Outbreak by Receptor Engineering.Molecular biotechnology · 2026Article
- A dramatic protein fold switch powers a bactericidal nanomachine.bioRxiv : the preprint server for biology · 2026Article
- Structure of a Brochothrix thermosphacta bacteriophage reveals cell wall adsorption mechanism in Gram-positive infecting siphophages.Nature communications · 2026Article
- Advances in mycobacteriophage research: from lytic mechanisms to one health applications.Frontiers in cellular and infection microbiology · 2026Review
- A prophage-encoded sRNA limits phage infection of adherent-invasive E. coli.PLoS pathogens · 2026Article
- Review
- Structural basis of bacteriophage Ur-lambda infection initiation.Science advances · 2025Article
- Isolation and characterization of bacteriophages from clinical enterohemorrhagicMicrobiology spectrum · 2025Article
- Predicted Structures ofViruses · 2025Article
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2 authors.
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Abstract
Bacteriophage infection, a pivotal process in microbiology, initiates with the phage's tail recognizing and binding to the bacterial cell surface, which then mediates the injection of viral DNA. Although comprehensive studies on the interaction between bacteriophage lambda and its outer membrane receptor, LamB, have provided rich information about the system's biochemical properties, the precise molecular mechanism remains undetermined. This study revealed the high-resolution cryo-electron microscopy (cryo-EM) structures of the bacteriophage lambda tail complexed with its irreversible Shigella sonnei 3070 LamB receptor and the closed central tail fiber. These structures reveal the complex processes that trigger infection and demonstrate a substantial conformational change in the phage lambda tail tip upon LamB binding. Providing detailed structures of bacteriophage lambda infection initiation, this study contributes to the expanding knowledge of lambda-bacterial interaction, which holds significance in the fields of microbiology and therapeutic development.
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