ArticleViruses2023
Structure and Function of Hoc-A Novel Environment Sensing Device Encoded by T4 and Other Bacteriophages.
Article in Viruses, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 18 citations in OpenAlex.
- Bacteriophages 6phi8, 6phi10, and 6phi13 Isolated from the Therapeutic Cocktail "SextaphagBiotech (Basel (Switzerland)) · 2026Article
- Characterization and genomic analysis of DSF2: a novel lytic phage infecting multidrug-resistantFrontiers in microbiology · 2026Article
- Structural Remodeling of Phage φPNJ-6 Hoc Promotes Adhesion to the Intestinal Epithelium.Transboundary and emerging diseases · 2026Article
- Targeted bacteriophage T4 nanoparticles reverse HIV-1 latency in human T cell line models.iScience · 2025Article
- Cryo-EM structure of bacteriophage Bas63 reveals structural conservation and diversity in theScience advances · 2025Article
- A Modular Bacteriophage T4 Nanoparticle Platform Enables Rapid Design of Dual COVID-19-Flu Mucosal Vaccines.Small science · 2025Article
- Article
- The structure of Shigella virus Sf14 reveals the presence of two decoration proteins and two long tail fibers.Communications biology · 2025Article
- Atlas of Interactions Between Decoration Proteins and Major Capsid Proteins of Coliphage N4.Viruses · 2024Article
- Bacteriophage T4 as a Protein-Based, Adjuvant- and Needle-Free, Mucosal Pandemic Vaccine Design Platform.Annual review of virology · 2024Review
- Ejectosome ofPNAS nexus · 2024Article
- Megataxonomy and global ecology of the virosphere.The ISME journal · 2024Review
- Antigen self-anchoring onto bacteriophage T5 capsid-like particles for vaccine design.NPJ vaccines · 2024Article
- Tentaclins-A Novel Family of Phage Receptor-Binding Proteins That Can Be Hypermutated by DGR Systems.International journal of molecular sciences · 2023Article
Corrections and comments
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Authors and funding
6 authors at 4 institutions in 2 countries.
Funding
Abstract
Bacteriophage T4 is decorated with 155 180 Å-long fibers of the highly antigenic outer capsid protein (Hoc). In this study, we describe a near-atomic structural model of Hoc by combining cryo-electron microscopy and AlphaFold structure predictions. It consists of a conserved C-terminal capsid-binding domain attached to a string of three variable immunoglobulin (Ig)-like domains, an architecture well-preserved in hundreds of Hoc molecules found in phage genomes. Each T4-Hoc fiber attaches randomly to the center of gp23* hexameric capsomers in one of the six possible orientations, though at the vertex-proximal hexamers that deviate from 6-fold symmetry, Hoc binds in two preferred orientations related by 180° rotation. Remarkably, each Hoc fiber binds to all six subunits of the capsomer, though the interactions are greatest with three of the subunits, resulting in the off-centered attachment of the C-domain. Biochemical analyses suggest that the acidic Hoc fiber (pI, ~4-5) allows for the clustering of virions in acidic pH and dispersion in neutral/alkaline pH. Hoc appears to have evolved as a sensing device that allows the phage to navigate its movements through reversible clustering-dispersion transitions so that it reaches its destination, the host bacterium, and persists in various ecological niches such as the human/mammalian gut.
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Registered trials
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 Socratic graph.