ArticleViruses2016
Branched Lateral Tail Fiber Organization in T5-Like Bacteriophages DT57C and DT571/2 is Revealed by Genetic and Functional Analysis.
Article in Viruses, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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Who cites it
41 citing papers in PubMed, 70 citations in OpenAlex.
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- Proteomic Analysis of Marine Bacteriophages: Structural Conservation, Post-Translational Modifications, and Phage-Host Interactions.Environmental microbiology · 2025Article
- The change of long tail fibers expanded the host range of a T5-like Salmonella phage and its application in milk.BMC microbiology · 2025Article
- At what cost? The impact of bacteriophage resistance on the growth kinetics and protein synthesis of Escherichia coli.Environmental microbiology reports · 2024Article
- Isolation, Characterization, and Unlocking the Potential of Mimir124 Phage for Personalized Treatment of Difficult, Multidrug-Resistant UropathogenicInternational journal of molecular sciences · 2024Article
- Integrative structural analysis of Pseudomonas phage DEV reveals a genome ejection motor.Nature communications · 2024Article
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- Bacterial Virus Forcing of Bacterial O-Antigen Shields: Lessons from Coliphages.International journal of molecular sciences · 2023Review
- Nearly complete structure of bacteriophage DT57C reveals architecture of head-to-tail interface and lateral tail fibers.Nature communications · 2023Article
- Article
- RB49-like Bacteriophages Recognize O Antigens as One of the Alternative Primary Receptors.International journal of molecular sciences · 2022Article
- Expansion of the Plaquing Host Range and Improvement of the Absorption Rate of a T5-like Salmonella Phage by Altering the Long Tail Fibers.Applied and environmental microbiology · 2022Article
- Complete genome sequencing of aFrontiers in microbiology · 2022Article
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Authors and funding
8 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The T5-like siphoviruses DT57C and DT571/2, isolated from horse feces, are very closely related to each other, and most of their structural proteins are also nearly identical to T5 phage. Their LTFs (L-shaped tail fibers), however, are composed of two proteins, LtfA and LtfB, instead of the single Ltf of bacteriophage T5. In silico and mutant analysis suggests a possible branched structure of DT57C and DT571/2 LTFs, where the LtfB protein is connected to the phage tail via the LtfA protein and with both proteins carrying receptor recognition domains. Such adhesin arrangement has not been previously recognized in siphoviruses. The LtfA proteins of our phages are found to recognize different host O-antigen types: E. coli O22-like for DT57C phage and E. coli O87 for DT571/2. LtfB proteins are identical in both phages and recognize another host receptor, most probably lipopolysaccharide (LPS) of E. coli O81 type. In these two bacteriophages, LTF function is essential to penetrate the shield of the host's O-antigens. We also demonstrate that LTF-mediated adsorption becomes superfluous when the non-specific cell protection by O-antigen is missing, allowing the phages to bind directly to their common secondary receptor, the outer membrane protein BtuB. The LTF independent adsorption was also demonstrated on an O22-like host mutant missing O-antigen O-acetylation, thus showing the biological value of this O-antigen modification for cell protection against phages.
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