ArticleNature communications2023
Distantly related Alteromonas bacteriophages share tail fibers exhibiting properties of transient chaperone caps.
Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 22 citations in OpenAlex.
- Modular plug-and-play engineering of Klebsiella phages with dual receptor-binding proteins for efficient host range design.Journal of biological engineering · 2026Article
- EAGP: an efficient generative augmentation framework for phage protein classification under severe class imbalance.Bioinformatics (Oxford, England) · 2026Article
- From structure to design: experimental and AI-driven approaches in receptor-binding protein engineering for reprogramming phage host range.Archives of microbiology · 2026Review
- A comprehensive catalogue of receptor-binding domains in extracellular contractile injection systems.Nature communications · 2026Article
- Genomic analysis ofVirus evolution · 2026Article
- Advanced Strategies in Phage Research: Innovations, Applications, and Challenges.Microorganisms · 2025Review
- Completing the BASEL phage collection to unlock hidden diversity for systematic exploration of phage-host interactions.PLoS biology · 2025Article
- Review
- Characterization of two novel bacteriophages (PSV6 and PSV3) as biocontrol agents againstFrontiers in microbiology · 2025Article
- Heterodimerization of staphylococcal phage φ2638A endolysin isoforms and their functional role in bacterial lysis.microLife · 2025Article
- Campycins are novel broad-spectrum antibacterials killing Campylobacter jejuni.Applied microbiology and biotechnology · 2024Article
- Bacteriophage Receptor Recognition and Nucleic Acid Transfer.Sub-cellular biochemistry · 2024Review
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The host recognition modules encoding the injection machinery and receptor binding proteins (RBPs) of bacteriophages are predisposed to mutation and recombination to maintain infectivity towards co-evolving bacterial hosts. In this study, we reveal how Alteromonas mediterranea schitovirus A5 shares its host recognition module, including tail fiber and cognate chaperone, with phages from distantly related families including Alteromonas myovirus V22. While the V22 chaperone is essential for producing active tail fibers, here we demonstrate production of functional A5 tail fibers regardless of chaperone co-expression. AlphaFold-generated models of tail fiber and chaperone pairs from phages A5, V22, and other Alteromonas phages reveal how amino acid insertions within both A5-like proteins results in a knob domain duplication in the tail fiber and a chaperone β-hairpin "tentacle" extension. These structural modifications are linked to differences in chaperone dependency between the A5 and V22 tail fibers. Structural similarity between the chaperones and intramolecular chaperone domains of other phage RBPs suggests an additional function of these chaperones as transient fiber "caps". Finally, our identification of homologous host recognition modules from morphologically distinct phages implies that horizontal gene transfer and recombination events between unrelated phages may be a more common process than previously thought among Caudoviricetes phages.
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