ArticleProceedings of the National Academy of Sciences of the United States of America2022
Structural basis for host recognition and superinfection exclusion by bacteriophage T5.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2022. 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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37 citing papers in PubMed, 49 citations in OpenAlex.
- Surviving phage attack primes bacterial immunity to defeat counterdefenses.bioRxiv : the preprint server for biology · 2026Article
- Bacterial immune systems.Antonie van Leeuwenhoek · 2026Review
- Classification of Sir2-HerA systems reveals a multilayered regulatory cascade gating the type III antiphage activity.Nucleic acids research · 2026Article
- Auxin (Indole-3-acetic acid) modulation of quorum sensing enhances phage susceptibility in Klebsiella pneumoniae.European journal of clinical microbiology & infectious diseases : official publication of the European Society of Clinical Microbiology · 2026Article
- Detection and characterization of protein methylation in bacteriophages and their host,mSystems · 2026Article
- Analysis of a Novel T1-like Phage KanT1 Reveals a Standalone SH3 Domain as a Widespread Component ofInternational journal of molecular sciences · 2026Article
- Resolution of a T1-Like Bacteriophage Outbreak by Receptor Engineering.Molecular biotechnology · 2026Article
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- Small siphophage binding to an open state of the LptDE outer membrane lipopolysaccharide translocon.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- The structure of the bacterial outer membrane transporter FusA enabled by addition of the native lipid lipopolysaccharide.Journal of structural biology: X · 2025Article
- KlebPhaCol: a community-driven resource for Klebsiella research identified a novel phage family.Nucleic acids research · 2025Article
- High-Throughput Identification and Characterization of LptDE-Binding Bicycle Peptides Using Phage Display and Cryo-EM.Journal of medicinal chemistry · 2025Article
- Phage Therapy as a Novel Alternative to Antibiotics Through Adaptive Evolution and Fitness Trade-Offs.Antibiotics (Basel, Switzerland) · 2025Review
- High-affinity PQQ import is widespread in Gram-negative bacteria.Science advances · 2025Article
- The Current Landscape of Phage-Antibiotic Synergistic (PAS) Interactions.Antibiotics (Basel, Switzerland) · 2025Review
- About proteins of a siphophage tail tip complex reverting to their pre-ejection fold after DNA ejection.Nature communications · 2025Article
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- Episomal virus maintenance enables bacterial population recovery from infection and promotes virus-bacterial coexistence.The ISME journal · 2025Article
- Deep learning-guided structural analysis of a novel bacteriophage KPP105 against multidrug-resistantComputational and structural biotechnology journal · 2025Article
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
A key but poorly understood stage of the bacteriophage life cycle is the binding of phage receptor-binding proteins (RBPs) to receptors on the host cell surface, leading to injection of the phage genome and, for lytic phages, host cell lysis. To prevent secondary infection by the same or a closely related phage and nonproductive phage adsorption to lysed cell fragments, superinfection exclusion (SE) proteins can prevent the binding of RBPs via modulation of the host receptor structure in ways that are also unclear. Here, we present the cryogenic electron microscopy (cryo-EM) structure of the phage T5 outer membrane (OM) receptor FhuA in complex with the T5 RBP pb5, and the crystal structure of FhuA complexed to the OM SE lipoprotein Llp. Pb5 inserts four loops deeply into the extracellular lumen of FhuA and contacts the plug but does not cause any conformational changes in the receptor, supporting the view that DNA translocation does not occur through the lumen of OM channels. The FhuA-Llp structure reveals that Llp is periplasmic and binds to a nonnative conformation of the plug of FhuA, causing the inward folding of two extracellular loops via "reverse" allostery. The inward-folded loops of FhuA overlap with the pb5 binding site, explaining how Llp binding to FhuA abolishes further infection of
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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.