ArticleScientific reports2016
Structure of the host-recognition device of Staphylococcus aureus phage ϕ11.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 52 citations in OpenAlex.
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- Key directions of fundamental research on bacteriophage Receptor Binding Proteins with applied potential.Frontiers in microbiology · 2026Review
- Prophage landscapes in clinical MRSA: safety profiling and discovery of Lys81, a broad-spectrum bacteriolytic enzyme.Frontiers in microbiology · 2026Article
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- Phage Adsorption to Gram-Positive Bacteria.Viruses · 2023Review
- High-resolution cryo-EM structure of theScience advances · 2022Article
- Phage-encoded carbohydrate-interacting proteins in the human gut.Frontiers in microbiology · 2022Review
- Structure and Topology Prediction of Phage Adhesion Devices Using AlphaFold2: The Case of TwoMicroorganisms · 2021Article
- Staphylococcus epidermidis Phages Transduce Antimicrobial Resistance Plasmids and Mobilize Chromosomal Islands.mSphere · 2021Article
- Reprogramming bacteriophage host range: design principles and strategies for engineering receptor binding proteins.Current opinion in biotechnology · 2021Review
- β-Lactams against the Fortress of the Gram-PositiveChemical reviews · 2021Review
- Exploring Mucin as Adjunct to Phage Therapy.Microorganisms · 2021Review
- Bacteriophage Treatment: Critical Evaluation of Its Application on World Health Organization Priority Pathogens.Viruses · 2020Review
- Conserved and Diverse Traits of Adhesion Devices fromViruses · 2020Review
- Structure of the host cell recognition and penetration machinery of a Staphylococcus aureus bacteriophage.PLoS pathogens · 2020Article
- Structure and genome ejection mechanism ofScience advances · 2019Article
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Authors and funding
7 authors at 5 institutions in 4 countries.
Funding
Abstract
Phages play key roles in the pathogenicity and adaptation of the human pathogen Staphylococcus aureus. However, little is known about the molecular recognition events that mediate phage adsorption to the surface of S. aureus. The lysogenic siphophage ϕ11 infects S. aureus SA113. It was shown previously that ϕ11 requires α- or β-N-acetylglucosamine (GlcNAc) moieties on cell wall teichoic acid (WTA) for adsorption. Gp45 was identified as the receptor binding protein (RBP) involved in this process and GlcNAc residues on WTA were found to be the key component of the ϕ11 receptor. Here we report the crystal structure of the RBP of ϕ11, which assembles into a large, multidomain homotrimer. Each monomer contains a five-bladed propeller domain with a cavity that could accommodate a GlcNAc moiety. An electron microscopy reconstruction of the ϕ11 host adhesion component, the baseplate, reveals that six RBP trimers are assembled around the baseplate core. The Gp45 and baseplate structures provide insights into the overall organization and molecular recognition process of the phage ϕ11 tail. This assembly is conserved among most glycan-recognizing Siphoviridae, and the RBP orientation would allow host adhesion and infection without an activation step.
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